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  • Mutation  (141)
  • American Association for the Advancement of Science (AAAS)  (141)
  • Annual Reviews
  • EDP Sciences
  • Elsevier
  • Nature Publishing Group
  • 2015-2019
  • 2005-2009  (141)
  • 1985-1989
  • 1980-1984
  • 1940-1944
  • 2005  (141)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (141)
  • Annual Reviews
  • EDP Sciences
  • Elsevier
  • Nature Publishing Group
Years
  • 2015-2019
  • 2005-2009  (141)
  • 1985-1989
  • 1980-1984
  • 1940-1944
Year
  • 1
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    The centromeric protein Sgo1 is required to sense lack of tension on mitotic chromosomes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: Chromosome alignment on the mitotic spindle is monitored by the spindle checkpoint. We identify Sgo1, a protein involved in meiotic chromosome cohesion, as a spindle checkpoint component. Budding yeast cells with mutations in SGO1 respond normally to microtubule depolymerization but not to lack of tension at the kinetochore, and they have difficulty attaching sister chromatids to opposite poles of the spindle. Sgo1 is thus required for sensing tension between sister chromatids during mitosis, and its degradation when they separate may prevent cell cycle arrest and chromosome loss in anaphase, a time when sister chromatids are no longer under tension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Indjeian, Vahan B -- Stern, Bodo M -- Murray, Andrew W -- GM043987/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):130-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637284" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromatids/physiology ; Chromosomal Proteins, Non-Histone ; Chromosome Segregation ; Chromosomes, Fungal/*physiology ; Kinetochores/physiology ; *Mitosis ; Mutation ; Nuclear Proteins/genetics/metabolism/*physiology ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Saccharomyces cerevisiae/genetics/*physiology ; Saccharomyces cerevisiae Proteins/genetics/metabolism/*physiology ; Spindle Apparatus/*physiology ; Ubiquitin-Protein Ligase Complexes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Neurodegeneration. Huntington's research points to possible new therapies (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):43-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autophagy ; Brain-Derived Neurotrophic Factor/metabolism ; Cells, Cultured ; Clinical Trials as Topic ; Corpus Striatum/pathology ; Disease Models, Animal ; Gene Expression Regulation ; Humans ; Huntington Disease/*drug therapy/genetics/pathology/*physiopathology ; Mice ; Mitochondria/metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/*genetics/metabolism/*physiology ; Neurons/*physiology ; Nuclear Proteins/chemistry/*genetics/metabolism/*physiology ; Peptides ; Transcription Factors/metabolism ; Trinucleotide Repeat Expansion
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Cell signaling. Frizzled at the cutting edge of the synapse (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez Arias, Alfonso -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1284-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK. ama11@hermes.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16311322" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell Nucleus/metabolism ; Drosophila Proteins/chemistry/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Endocytosis ; Frizzled Receptors ; Models, Neurological ; Mutation ; Neuromuscular Junction/*metabolism ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/*metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/*metabolism ; *Signal Transduction ; Wnt1 Protein
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Genetics. Two genes link two distinct psychoses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sawa, Akira -- Snyder, Solomon H -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1128-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA. asawa1@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293746" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/*genetics/physiology ; Affective Disorders, Psychotic/enzymology/*genetics ; Carrier Proteins/physiology ; Cyclic AMP/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Enzyme Activation ; Humans ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Protein Binding ; Schizophrenia/*genetics ; Signal Transduction ; Translocation, Genetic
    Print ISSN: 0036-8075
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  • 5
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    Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of poleta and poliota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poleta is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bienko, Marzena -- Green, Catherine M -- Crosetto, Nicola -- Rudolf, Fabian -- Zapart, Grzegorz -- Coull, Barry -- Kannouche, Patricia -- Wider, Gerhard -- Peter, Matthias -- Lehmann, Alan R -- Hofmann, Kay -- Dikic, Ivan -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1821-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biochemistry II, Goethe University Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Computational Biology ; DNA/*biosynthesis ; *DNA Damage ; DNA Repair ; DNA Replication ; DNA-Directed DNA Polymerase/*chemistry/genetics/*metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Point Mutation ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Binding ; Protein Conformation ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Transfection ; Ubiquitin/*metabolism ; Xeroderma Pigmentosum/genetics ; Zinc Fingers
    Print ISSN: 0036-8075
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  • 6
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    Obesity and metabolic syndrome in circadian Clock mutant mice (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-23
    Description: The CLOCK transcription factor is a key component of the molecular circadian clock within pacemaker neurons of the hypothalamic suprachiasmatic nucleus. We found that homozygous Clock mutant mice have a greatly attenuated diurnal feeding rhythm, are hyperphagic and obese, and develop a metabolic syndrome of hyperleptinemia, hyperlipidemia, hepatic steatosis, hyperglycemia, and hypoinsulinemia. Expression of transcripts encoding selected hypothalamic peptides associated with energy balance was attenuated in the Clock mutant mice. These results suggest that the circadian clock gene network plays an important role in mammalian energy balance.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3764501/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3764501/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turek, Fred W -- Joshu, Corinne -- Kohsaka, Akira -- Lin, Emily -- Ivanova, Ganka -- McDearmon, Erin -- Laposky, Aaron -- Losee-Olson, Sue -- Easton, Amy -- Jensen, Dalan R -- Eckel, Robert H -- Takahashi, Joseph S -- Bass, Joseph -- AG11412/AG/NIA NIH HHS/ -- AG18200/AG/NIA NIH HHS/ -- DK02675/DK/NIDDK NIH HHS/ -- DK26356/DK/NIDDK NIH HHS/ -- HL59598/HL/NHLBI NIH HHS/ -- HL75029/HL/NHLBI NIH HHS/ -- K08 DK002675/DK/NIDDK NIH HHS/ -- P01 AG011412/AG/NIA NIH HHS/ -- R01 AG018200/AG/NIA NIH HHS/ -- R01 DK026356/DK/NIDDK NIH HHS/ -- R01 HL059598/HL/NHLBI NIH HHS/ -- R01 HL075029/HL/NHLBI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2005 May 13;308(5724):1043-5. Epub 2005 Apr 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15845877" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/pathology ; Animals ; Body Weight ; Brain/metabolism ; CLOCK Proteins ; *Circadian Rhythm ; Dietary Fats/administration & dosage ; Energy Intake ; *Energy Metabolism ; *Feeding Behavior ; Hepatocytes/pathology ; Hyperglycemia ; Hyperlipidemias ; Insulin/blood ; Leptin/blood ; Metabolic Syndrome X/genetics/*physiopathology ; Mice ; Mice, Inbred C57BL ; Motor Activity ; Mutation ; Neuropeptides/genetics/metabolism ; Obesity/genetics/*physiopathology ; Trans-Activators/*genetics/*physiology ; Weight Gain
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
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    Experience-driven plasticity of visual cortex limited by myelin and Nogo receptor (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: Monocular deprivation normally alters ocular dominance in the visual cortex only during a postnatal critical period (20 to 32 days postnatal in mice). We find that mutations in the Nogo-66 receptor (NgR) affect cessation of ocular dominance plasticity. In NgR-/- mice, plasticity during the critical period is normal, but it continues abnormally such that ocular dominance at 45 or 120 days postnatal is subject to the same plasticity as at juvenile ages. Thus, physiological NgR signaling from myelin-derived Nogo, MAG, and OMgp consolidates the neural circuitry established during experience-dependent plasticity. After pathological trauma, similar NgR signaling limits functional recovery and axonal regeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856689/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856689/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGee, Aaron W -- Yang, Yupeng -- Fischer, Quentin S -- Daw, Nigel W -- Strittmatter, Stephen M -- R01 NS039962/NS/NINDS NIH HHS/ -- R01 NS039962-10/NS/NINDS NIH HHS/ -- R01 NS042304/NS/NINDS NIH HHS/ -- R01 NS042304-08/NS/NINDS NIH HHS/ -- R01 NS056485/NS/NINDS NIH HHS/ -- R01 NS056485-04/NS/NINDS NIH HHS/ -- R37 NS033020/NS/NINDS NIH HHS/ -- R37 NS033020-15/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2222-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Yale University School of Medicine, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195464" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chondroitin Sulfate Proteoglycans/metabolism ; Darkness ; Dominance, Ocular/*physiology ; Electrophysiology ; GPI-Linked Proteins ; Gene Targeting ; Mice ; Mice, Inbred C57BL ; Mutation ; Myelin Basic Protein/metabolism ; Myelin Proteins/genetics/metabolism/*physiology ; Myelin Sheath/*physiology ; Myelin-Associated Glycoprotein/metabolism ; Neurites/physiology ; Neuronal Plasticity/*physiology ; Neurons/*physiology ; Photic Stimulation ; Receptors, Cell Surface/genetics/*physiology ; Signal Transduction ; Visual Cortex/cytology/growth & development/*physiology ; gamma-Aminobutyric Acid/physiology
    Print ISSN: 0036-8075
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  • 8
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    Physiology. Boosting gene extends mouse life span (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1310-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123271" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Blood Glucose/analysis ; Female ; Glucuronidase ; Insulin/blood/metabolism ; Insulin Resistance ; Insulin-Like Growth Factor I/metabolism ; Longevity/*genetics ; Male ; Membrane Proteins/blood/*genetics/*physiology ; Mice ; Mutation ; Signal Transduction
    Print ISSN: 0036-8075
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  • 9
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    Reproductive biology. A powerful first KiSS-1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):551-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16040685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/physiology ; Circadian Rhythm ; Female ; Gonadotropin-Releasing Hormone/physiology/secretion ; Humans ; Hypogonadism/genetics ; Kisspeptins ; Leptin/genetics/physiology ; Male ; Mutation ; Neurons/physiology ; Proteins/genetics/*physiology ; Puberty/*physiology ; Receptors, Cell Surface/genetics/metabolism ; Receptors, G-Protein-Coupled ; Receptors, Leptin ; Receptors, Neuropeptide/genetics/*physiology ; Reproduction ; Signal Transduction ; Tumor Suppressor Proteins
    Print ISSN: 0036-8075
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  • 10
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    Direct control of germline stem cell division and cyst growth by neural insulin in Drosophila (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-16
    Description: Stem cells reside in specialized niches that provide signals required for their maintenance and division. Tissue-extrinsic signals can also modify stem cell activity, although this is poorly understood. Here, we report that neural-derived Drosophila insulin-like peptides (DILPs) directly regulate germline stem cell division rate, demonstrating that signals mediating the ovarian response to nutritional input can modify stem cell activity in a niche-independent manner. We also reveal a crucial direct role of DILPs in controlling germline cyst growth and vitellogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaFever, Leesa -- Drummond-Barbosa, Daniela -- GM 069875/GM/NIGMS NIH HHS/ -- R01 GM069875/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1071-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, Vanderbilt University Medical Center, 4120B Medical Research Building III, 465 21st Avenue South, Nashville, TN 37232-8240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099985" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Proliferation ; Drosophila/cytology/genetics/*physiology ; Drosophila Proteins/genetics/*physiology ; Female ; Food ; Germ Cells/*cytology ; Insulin/*physiology ; Mutation ; Ovarian Follicle/cytology/physiology ; Ovary/cytology/physiology ; Peptides/physiology ; Receptor Protein-Tyrosine Kinases/genetics/physiology ; *Signal Transduction ; Stem Cells/*cytology ; Vitellogenesis
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  • 11
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    SLC24A5, a putative cation exchanger, affects pigmentation in zebrafish and humans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: Lighter variations of pigmentation in humans are associated with diminished number, size, and density of melanosomes, the pigmented organelles of melanocytes. Here we show that zebrafish golden mutants share these melanosomal changes and that golden encodes a putative cation exchanger slc24a5 (nckx5) that localizes to an intracellular membrane, likely the melanosome or its precursor. The human ortholog is highly similar in sequence and functional in zebrafish. The evolutionarily conserved ancestral allele of a human coding polymorphism predominates in African and East Asian populations. In contrast, the variant allele is nearly fixed in European populations, is associated with a substantial reduction in regional heterozygosity, and correlates with lighter skin pigmentation in admixed populations, suggesting a key role for the SLC24A5 gene in human pigmentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamason, Rebecca L -- Mohideen, Manzoor-Ali P K -- Mest, Jason R -- Wong, Andrew C -- Norton, Heather L -- Aros, Michele C -- Jurynec, Michael J -- Mao, Xianyun -- Humphreville, Vanessa R -- Humbert, Jasper E -- Sinha, Soniya -- Moore, Jessica L -- Jagadeeswaran, Pudur -- Zhao, Wei -- Ning, Gang -- Makalowska, Izabela -- McKeigue, Paul M -- O'donnell, David -- Kittles, Rick -- Parra, Esteban J -- Mangini, Nancy J -- Grunwald, David J -- Shriver, Mark D -- Canfield, Victor A -- Cheng, Keith C -- CA73935/CA/NCI NIH HHS/ -- EY11308/EY/NEI NIH HHS/ -- HD37572/HD/NICHD NIH HHS/ -- HD40179/HD/NICHD NIH HHS/ -- HG002154/HG/NHGRI NIH HHS/ -- HL077910/HL/NHLBI NIH HHS/ -- RR017441/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jake Gittlen Cancer Research Foundation, Department of Pathology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357253" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; African Continental Ancestry Group/genetics ; Alanine/genetics ; Alleles ; Amino Acid Sequence ; Animals ; Antiporters/chemistry/*genetics/physiology ; Asian Continental Ancestry Group/genetics ; Biological Evolution ; Calcium/metabolism ; European Continental Ancestry Group/genetics ; Gene Frequency ; Genes ; Genetic Variation ; Haplotypes ; Heterozygote ; Humans ; Ion Transport ; Melanins/analysis ; Melanosomes/chemistry/ultrastructure ; Mice ; Molecular Sequence Data ; Multifactorial Inheritance ; Mutation ; Pigment Epithelium of Eye/chemistry/ultrastructure ; Polymorphism, Single Nucleotide ; Selection, Genetic ; Skin Pigmentation/*genetics ; Threonine/genetics ; Zebrafish/embryology/*genetics/metabolism ; Zebrafish Proteins/chemistry/*genetics/physiology
    Print ISSN: 0036-8075
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  • 12
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    FD, a bZIP protein mediating signals from the floral pathway integrator FT at the shoot apex (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-16
    Description: FLOWERING LOCUS T (FT) is a conserved promoter of flowering that acts downstream of various regulatory pathways, including one that mediates photoperiodic induction through CONSTANS (CO), and is expressed in the vasculature of cotyledons and leaves. A bZIP transcription factor, FD, preferentially expressed in the shoot apex is required for FT to promote flowering. FD and FT are interdependent partners through protein interaction and act at the shoot apex to promote floral transition and to initiate floral development through transcriptional activation of a floral meristem identity gene, APETALA1 (AP1). FT may represent a long-distance signal in flowering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abe, Mitsutomo -- Kobayashi, Yasushi -- Yamamoto, Sumiko -- Daimon, Yasufumi -- Yamaguchi, Ayako -- Ikeda, Yoko -- Ichinoki, Harutaka -- Notaguchi, Michitaka -- Goto, Koji -- Araki, Takashi -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1052-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099979" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Cell Nucleus/metabolism ; Cotyledon/metabolism ; Flowers/*growth & development ; Gene Expression ; Gene Expression Regulation, Plant ; Genes, Plant ; Homeodomain Proteins/genetics/metabolism ; MADS Domain Proteins ; Meristem/genetics/metabolism ; Morphogenesis ; Mutation ; Phenotype ; Plant Leaves/metabolism ; Plant Proteins/genetics/metabolism ; Plant Shoots/metabolism ; Protein Interaction Mapping ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transcriptional Activation
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  • 13
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    Microbiology. Translocation of anthrax toxin: lord of the rings (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Heijne, Gunnar -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):709-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm, Sweden. gunnar@dbb.su.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051774" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/chemistry ; Amino Acid Substitution ; Antigens, Bacterial/*chemistry/genetics/*metabolism ; Bacillus anthracis/*chemistry/metabolism ; Bacterial Toxins/*chemistry/genetics/*metabolism ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Mutation ; Onium Compounds/metabolism ; Organophosphorus Compounds/metabolism ; Phenylalanine/*chemistry ; Protein Conformation ; Protein Folding ; Quaternary Ammonium Compounds/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    Functional genomic analysis of the Wnt-wingless signaling pathway (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-09
    Description: The Wnt-Wingless (Wg) pathway is one of a core set of evolutionarily conserved signaling pathways that regulates many aspects of metazoan development. Aberrant Wnt signaling has been linked to human disease. In the present study, we used a genomewide RNA interference (RNAi) screen in Drosophila cells to screen for regulators of the Wnt pathway. We identified 238 potential regulators, which include known pathway components, genes with functions not previously linked to this pathway, and genes with no previously assigned functions. Reciprocal-Best-Blast analyses reveal that 50% of the genes identified in the screen have human orthologs, of which approximately 18% are associated with human disease. Functional assays of selected genes from the cell-based screen in Drosophila, mammalian cells, and zebrafish embryos demonstrated that these genes have evolutionarily conserved functions in Wnt signaling. High-throughput RNAi screens in cultured cells, followed by functional analyses in model organisms, prove to be a rapid means of identifying regulators of signaling pathways implicated in development and disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DasGupta, Ramanuj -- Kaykas, Ajamete -- Moon, Randall T -- Perrimon, Norbert -- New York, N.Y. -- Science. 2005 May 6;308(5723):826-33. Epub 2005 Apr 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Howard Hughes Medical Institute (HHMI), Harvard Medical School, New Research Building, No. 339, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. rdasgupt@genetics.med.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15817814" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Line ; Cloning, Molecular ; Computational Biology ; Cytoskeletal Proteins/metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/*genetics/metabolism ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; Epistasis, Genetic ; *Gene Expression Regulation ; Genes, Insect ; Genes, Reporter ; *Genomics ; Mutation ; Phenotype ; Phosphorylation ; Protein Kinases/metabolism ; Proteins/metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; *RNA Interference ; *Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors/chemistry/genetics/metabolism ; Transfection ; Wnt Proteins ; Wnt1 Protein ; Wnt3 Protein ; Zebrafish ; Zebrafish Proteins ; beta Catenin ; rab5 GTP-Binding Proteins/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors. In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta. gammac is then recruited to the composite surface formed by the IL-2/IL-2Rbeta complex. Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2. The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID). This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xinquan -- Rickert, Mathias -- Garcia, K Christopher -- AI51321/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1159-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Microbiology and Immunology, Stanford University School of Medicine, 299 Campus Drive, Fairchild D319, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293754" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Humans ; Interleukin Receptor Common gamma Subunit ; Interleukin-2/*chemistry/metabolism/therapeutic use ; Interleukin-2 Receptor alpha Subunit ; Interleukin-2 Receptor beta Subunit ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Receptors, Interleukin/*chemistry/metabolism ; Receptors, Interleukin-2/*chemistry/genetics/metabolism ; Recombinant Proteins/therapeutic use ; Severe Combined Immunodeficiency/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Genetics. Harvesting medical information from the human family tree (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altshuler, David -- Clark, Andrew G -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1052-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Broad Institute of Harvard and Massachusetts Institute of Technology, and Massachusetts General Hospital, Boston, MA 02114, USA. altshuler@molbio.mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15718454" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/*genetics ; Asian Continental Ancestry Group/*genetics ; Chromosome Mapping ; Databases, Genetic ; European Continental Ancestry Group/*genetics ; Evolution, Molecular ; Female ; Gene Frequency ; Genetic Markers ; *Genetic Predisposition to Disease ; Genetic Variation ; *Genome, Human ; Genotype ; Haplotypes ; Humans ; Linkage Disequilibrium ; Male ; *Multifactorial Inheritance ; Mutation ; *Polymorphism, Single Nucleotide ; Recombination, Genetic ; Risk Factors ; Selection, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Nodulation signaling in legumes requires NSP2, a member of the GRAS family of transcriptional regulators (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-18
    Description: Rhizobial bacteria enter a symbiotic interaction with legumes, activating diverse responses in roots through the lipochito oligosaccharide signaling molecule Nod factor. Here, we show that NSP2 from Medicago truncatula encodes a GRAS protein essential for Nod-factor signaling. NSP2 functions downstream of Nod-factor-induced calcium spiking and a calcium/calmodulin-dependent protein kinase. We show that NSP2-GFP expressed from a constitutive promoter is localized to the endoplasmic reticulum/nuclear envelope and relocalizes to the nucleus after Nod-factor elicitation. This work provides evidence that a GRAS protein transduces calcium signals in plants and provides a possible regulator of Nod-factor-inducible gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalo, Peter -- Gleason, Cynthia -- Edwards, Anne -- Marsh, John -- Mitra, Raka M -- Hirsch, Sibylle -- Jakab, Julia -- Sims, Sarah -- Long, Sharon R -- Rogers, Jane -- Kiss, Gyorgy B -- Downie, J Allan -- Oldroyd, Giles E D -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1786-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Disease and Stress Biology and Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961668" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Calcium/metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/metabolism ; Cell Nucleus/metabolism ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/*metabolism ; Medicago/genetics/*metabolism/*microbiology ; Molecular Sequence Data ; Mutation ; Oligonucleotide Array Sequence Analysis ; Peas/genetics/metabolism ; Plant Proteins/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Sinorhizobium meliloti/*physiology ; Symbiosis ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic
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  • 18
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    Circadian clock control by SUMOylation of BMAL1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-20
    Description: The molecular machinery that governs circadian rhythmicity is based on clock proteins organized in regulatory feedback loops. Although posttranslational modification of clock proteins is likely to finely control their circadian functions, only limited information is available to date. Here, we show that BMAL1, an essential transcription factor component of the clock mechanism, is SUMOylated on a highly conserved lysine residue (Lys259) in vivo. BMAL1 shows a circadian pattern of SUMOylation that parallels its activation in the mouse liver. SUMOylation of BMAL1 requires and is induced by CLOCK, the heterodimerization partner of BMAL1. Ectopic expression of a SUMO-deficient BMAL1 demonstrates that SUMOylation plays an important role in BMAL1 circadian expression and clock rhythmicity. This reveals an additional level of regulation within the core mechanism of the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cardone, Luca -- Hirayama, Jun -- Giordano, Francesca -- Tamaru, Teruya -- Palvimo, Jorma J -- Sassone-Corsi, Paolo -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1390-4. Epub 2005 Aug 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire, 1 rue Laurent Fries, 67404 Illkirch, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109848" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; CLOCK Proteins ; COS Cells ; Cell Cycle Proteins ; Cell Line ; *Circadian Rhythm ; Dimerization ; Ethylmaleimide/pharmacology ; Gene Expression Regulation ; Liver/metabolism ; Lysine/metabolism ; Mice ; Mutation ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; SUMO-1 Protein/*metabolism ; Trans-Activators/genetics/metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Pesticide resistance via transposition-mediated adaptive gene truncation in Drosophila (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-30
    Description: To study adaptation, it is essential to identify multiple adaptive mutations and to characterize their molecular, phenotypic, selective, and ecological consequences. Here we describe a genomic screen for adaptive insertions of transposable elements in Drosophila. Using a pilot application of this screen, we have identified an adaptive transposable element insertion, which truncates a gene and apparently generates a functional protein in the process. The insertion of this transposable element confers increased resistance to an organophosphate pesticide and has spread in D. melanogaster recently.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aminetzach, Yael T -- Macpherson, J Michael -- Petrov, Dmitri A -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):764-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, 371 Serra Mall, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051794" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Alleles ; Amino Acid Substitution ; Animals ; Azinphosmethyl/pharmacology ; Base Sequence ; Choline/metabolism ; Crosses, Genetic ; *DNA Transposable Elements ; Drosophila/drug effects/genetics/physiology ; Drosophila Proteins/chemistry/*genetics/physiology ; Drosophila melanogaster/drug effects/*genetics/physiology ; *Evolution, Molecular ; Exons ; Female ; Gene Expression ; *Genes, Insect ; Haplotypes ; Insecticide Resistance/*genetics ; Insecticides/pharmacology ; Introns ; Long Interspersed Nucleotide Elements ; Molecular Sequence Data ; Mutation ; Polymorphism, Genetic ; Recombination, Genetic ; Selection, Genetic
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  • 20
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    Plant circadian clocks increase photosynthesis, growth, survival, and competitive advantage (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-26
    Description: Circadian clocks are believed to confer an advantage to plants, but the nature of that advantage has been unknown. We show that a substantial photosynthetic advantage is conferred by correct matching of the circadian clock period with that of the external light-dark cycle. In wild type and in long- and short-circadian period mutants of Arabidopsis thaliana, plants with a clock period matched to the environment contain more chlorophyll, fix more carbon, grow faster, and survive better than plants with circadian periods differing from their environment. This explains why plants gain advantage from circadian control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dodd, Antony N -- Salathia, Neeraj -- Hall, Anthony -- Kevei, Eva -- Toth, Reka -- Nagy, Ferenc -- Hibberd, Julian M -- Millar, Andrew J -- Webb, Alex A R -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):630-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge, CB2 3EA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16040710" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/*physiology ; Arabidopsis Proteins/genetics/metabolism ; Biological Clocks/*physiology ; Biomass ; Carbon Dioxide/metabolism ; Chlorophyll/metabolism ; Circadian Rhythm/*physiology ; Darkness ; Gene Expression Regulation, Plant ; Genotype ; Light ; Mutation ; *Photosynthesis ; Plant Leaves/metabolism ; Seeds/growth & development ; Transcription Factors/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Regulation of mammalian tooth cusp patterning by ectodin (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-24
    Description: Mammalian tooth crowns have precise functional requirements but cannot be substantially remodeled after eruption. In developing teeth, epithelial signaling centers, the enamel knots, form at future cusp positions and are the first signs of cusp patterns that distinguish species. We report that ectodin, a secreted bone morphogenetic protein (BMP) inhibitor, is expressed as a "negative" image of mouse enamel knots. Furthermore, we show that ectodin-deficient mice have enlarged enamel knots, highly altered cusp patterns, and extra teeth. Unlike in normal teeth, excess BMP accelerates patterning in ectodin-deficient teeth. We propose that ectodin is critical for robust spatial delineation of enamel knots and cusps.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kassai, Yoshiaki -- Munne, Pauliina -- Hotta, Yuhei -- Penttila, Enni -- Kavanagh, Kathryn -- Ohbayashi, Norihiko -- Takada, Shinji -- Thesleff, Irma -- Jernvall, Jukka -- Itoh, Nobuyuki -- New York, N.Y. -- Science. 2005 Sep 23;309(5743):2067-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetic Biochemistry, Kyoto University Graduate School of Pharmaceutical Sciences, Kyoto 606-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179481" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Bone Morphogenetic Protein 4 ; Bone Morphogenetic ; Proteins/biosynthesis/genetics/metabolism/pharmacology/*physiology ; Cell Cycle Proteins/biosynthesis/genetics/physiology ; Chimera ; Cyclin-Dependent Kinase Inhibitor p21 ; Dental Enamel/embryology ; Gene Expression Regulation, Developmental ; Hedgehog Proteins ; Heterozygote ; Mice ; Mice, Inbred C57BL ; Microscopy, Confocal ; Molar/embryology/metabolism ; Mutation ; *Odontogenesis ; Organ Culture Techniques ; Tooth Crown/*embryology ; Trans-Activators/biosynthesis/genetics
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    fgf20 is essential for initiating zebrafish fin regeneration (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-24
    Description: Epimorphic regeneration requires the presence or creation of pluripotent cells capable of reproducing lost organs. Zebrafish fin regeneration is mediated by the creation of blastema cells. Here, we characterize the devoid of blastema (dob) mutant that fails fin regeneration during initial steps, forms abnormal regeneration epithelium, and does not form blastema. This mutation has no impact on embryonic survival. Dob results from an fgf20a null mutation, Y148S. Fgf20a is expressed during initiation of fin regeneration at the epithelial-mesenchymal boundary and later overlaps with the blastema marker msxb. Thus, fgf20a has a regeneration-specific requirement, initiating fin regeneration, and controlling blastema formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitehead, Geoffrey G -- Makino, Shinji -- Lien, Ching-Ling -- Keating, Mark T -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1957-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Cell Biology, Harvard Medical School, Department of Cardiology, Children's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Extremities ; Fibroblast Growth Factors/*physiology ; Homeodomain Proteins/biosynthesis ; Male ; Mesoderm ; Mutation ; Regeneration/genetics/*physiology ; Temperature ; Wound Healing ; Zebrafish ; Zebrafish Proteins/biosynthesis/*physiology
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  • 23
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    Contact-dependent inhibition of growth in Escherichia coli (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-20
    Description: Bacteria have developed mechanisms to communicate and compete with each other for limited environmental resources. We found that certain Escherichia coli, including uropathogenic strains, contained a bacterial growth-inhibition system that uses direct cell-to-cell contact. Inhibition was conditional, dependent upon the growth state of the inhibitory cell and the pili expression state of the target cell. Both a large cell-surface protein designated Contact-dependent inhibitor A (CdiA) and two-partner secretion family member CdiB were required for growth inhibition. The CdiAB system may function to regulate the growth of specific cells within a differentiated bacterial population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aoki, Stephanie K -- Pamma, Rupinderjit -- Hernday, Aaron D -- Bickham, Jessica E -- Braaten, Bruce A -- Low, David A -- AI23348/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular, Cellular, and Developmental Biology, University of California-Santa Barbara (UCSB), Santa Barbara, CA 93106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109881" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Computational Biology ; Contact Inhibition ; Culture Media, Conditioned ; Escherichia coli/genetics/*growth & development/pathogenicity/physiology ; Escherichia coli K12/genetics/*growth & development/physiology ; Escherichia coli Proteins/chemistry/genetics/*physiology ; Fimbriae, Bacterial/metabolism ; Genes, Bacterial ; Genetic Complementation Test ; Genomic Islands ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Virulence
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  • 24
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    Integration of spatial and temporal information during floral induction in Arabidopsis (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-16
    Description: Flowering of Arabidopsis is regulated by several environmental and endogenous signals. An important integrator of these inputs is the FLOWERING LOCUS T (FT) gene, which encodes a small, possibly mobile protein. A primary response to floral induction is the activation of FT RNA expression in leaves. Because flowers form at a distant site, the shoot apex, these data suggest that FT primarily controls the timing of flowering. Integration of temporal and spatial information is mediated in part by the bZIP transcription factor FD, which is already expressed at the shoot apex before floral induction. A complex of FT and FD proteins in turn can activate floral identity genes such as APETALA1 (AP1).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wigge, Philip A -- Kim, Min Chul -- Jaeger, Katja E -- Busch, Wolfgang -- Schmid, Markus -- Lohmann, Jan U -- Weigel, Detlef -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1056-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany. philip.wigge@bbsrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099980" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Chromatin Immunoprecipitation ; DNA-Binding Proteins/genetics/metabolism ; Flowers/*growth & development ; Gene Expression Regulation, Plant ; Homeodomain Proteins/genetics/metabolism ; MADS Domain Proteins ; Models, Biological ; Mutation ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Plant Leaves/metabolism ; Plant Proteins/genetics/metabolism ; Plant Shoots/metabolism ; Protein Interaction Mapping ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Time Factors ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic ; Two-Hybrid System Techniques
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  • 25
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    Structure of SARS coronavirus spike receptor-binding domain complexed with receptor (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Fang -- Li, Wenhui -- Farzan, Michael -- Harrison, Stephen C -- AI061601/AI/NIAID NIH HHS/ -- CA13202/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1864-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166518" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antibodies, Viral/immunology ; Binding Sites ; Carboxypeptidases/*chemistry/metabolism ; Cell Line ; Crystallography, X-Ray ; Disease Outbreaks ; Epitopes ; Glycosylation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/*chemistry/genetics/immunology/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Peptidyl-Dipeptidase A ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*chemistry/metabolism ; SARS Virus/*chemistry/genetics/physiology ; Severe Acute Respiratory Syndrome/transmission/*virology ; Species Specificity ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/*chemistry/genetics/immunology/*metabolism ; Viral Vaccines ; Viverridae/virology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Self-renewal and cancer of the gut: two sides of a coin (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: The intestinal epithelium follows the paradigms of stem cell biology established for other self-renewing tissues. With a unique topology, it constitutes a two-dimensional structure folded into valleys and hills: the proliferative crypts and the differentiated villi. Its unprecedented self-renewal rate appears reflected in a high susceptibility to malignant transformation. The molecular mechanisms that control homeostatic self-renewal and those that underlie colorectal cancer are remarkably symmetrical. Here, we discuss the biology of the intestinal epithelium, emphasizing the roles played by Wnt, bone morphogenic protein, and Notch signaling cascades in epithelial self-renewal and cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radtke, Freddy -- Clevers, Hans -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1904-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, Chemin de Boveresses 155, CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790842" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/genetics/metabolism/pathology ; Animals ; Bone Morphogenetic Proteins/metabolism ; Cell Transformation, Neoplastic ; Colorectal Neoplasms/*etiology/genetics/pathology/physiopathology ; Colorectal Neoplasms, Hereditary Nonpolyposis/genetics/metabolism/pathology ; Helix-Loop-Helix Motifs ; Humans ; Intercellular Signaling Peptides and Proteins/metabolism ; Intestinal Mucosa/*cytology/embryology/*physiology ; Membrane Proteins/metabolism ; Mutation ; Receptors, Notch ; Signal Transduction ; Stem Cells/cytology/physiology ; Wnt Proteins
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    The beta-glucuronidase klotho hydrolyzes and activates the TRPV5 channel (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-22
    Description: Blood calcium concentration is maintained within a narrow range despite large variations in dietary input and body demand. The Transient Receptor Potential ion channel TRPV5 has been implicated in this process. We report here that TRPV5 is stimulated by the mammalian hormone klotho. Klotho, a beta-glucuronidase, hydrolyzes extracellular sugar residues on TRPV5, entrapping the channel in the plasma membrane. This maintains durable calcium channel activity and membrane calcium permeability in kidney. Thus, klotho activates a cell surface channel by hydrolysis of its extracellular N-linked oligosaccharides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Q -- Hoefs, S -- van der Kemp, A W -- Topala, C N -- Bindels, R J -- Hoenderop, J G -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):490-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, 6500 HB Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239475" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Channels/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; Glucuronidase/antagonists & inhibitors/metabolism ; Glycosylation ; Humans ; Hydrolysis ; Kidney/cytology/metabolism ; Membrane Proteins/*metabolism ; Mice ; Mice, Inbred C57BL ; Mutation ; Patch-Clamp Techniques ; Protein Transport ; Rabbits ; Sodium/metabolism ; TRPV Cation Channels/genetics/*metabolism ; Transfection
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    Structural insights into the activity of enhancer-binding proteins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: Activators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2756573/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2756573/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rappas, Mathieu -- Schumacher, Jorg -- Beuron, Fabienne -- Niwa, Hajime -- Bordes, Patricia -- Wigneshweraraj, Sivaramesh -- Keetch, Catherine A -- Robinson, Carol V -- Buck, Martin -- Zhang, Xiaodong -- B17129/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1972-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College London, London, SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790859" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Cryoelectron Microscopy ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/metabolism ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; *Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Polymerase Sigma 54 ; Sigma Factor/chemistry/metabolism ; Trans-Activators/*chemistry/*metabolism ; Transcription Factors/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Cell biology. A fungal Achilles' heel (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitman, Joseph -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2175-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA. heitm001@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195450" target="_blank"〉PubMed〈/a〉
    Keywords: Antifungal Agents/pharmacology ; Aspergillus/drug effects/genetics ; Benzoquinones ; Biological Evolution ; Calcineurin/*physiology ; Calcineurin Inhibitors ; Candida albicans/drug effects/genetics ; Cyclosporine/pharmacology/therapeutic use ; *Drug Resistance, Fungal ; Drug Therapy, Combination ; Ergosterol/metabolism ; HSP90 Heat-Shock Proteins/antagonists & inhibitors/*physiology ; Humans ; Lactams, Macrocyclic ; Mutation ; Mycoses/drug therapy/microbiology ; Phenotype ; Quinones/pharmacology/therapeutic use ; Saccharomyces cerevisiae/*drug effects/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/antagonists & inhibitors/*physiology ; Tacrolimus/pharmacology/therapeutic use
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    Aconitase couples metabolic regulation to mitochondrial DNA maintenance (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-05
    Description: Mitochondrial DNA (mtDNA) is essential for cells to maintain respiratory competency and is inherited as a protein-DNA complex called the nucleoid. We have identified 22 mtDNA-associated proteins in yeast, among which is mitochondrial aconitase (Aco1p). We show that this Krebs-cycle enzyme is essential for mtDNA maintenance independent of its catalytic activity. Regulation of ACO1 expression by the HAP and retrograde metabolic signaling pathways directly affects mtDNA maintenance. When constitutively expressed, Aco1p can replace the mtDNA packaging function of the high-mobility-group protein Abf2p. Thus, Aco1p may integrate metabolic signals and mtDNA maintenance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Xin Jie -- Wang, Xiaowen -- Kaufman, Brett A -- Butow, Ronald A -- GM22525/GM/NIGMS NIH HHS/ -- GM33510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):714-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390-9148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692048" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; CCAAT-Binding Factor/genetics/metabolism ; DNA, Fungal/*metabolism ; DNA, Mitochondrial/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Glucose/metabolism ; Iron Regulatory Protein 1/genetics/*metabolism ; Mutation ; Repressor Proteins/genetics/metabolism ; Saccharomyces cerevisiae/enzymology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Signal Transduction ; Spores, Fungal/physiology ; Transcription Factors/genetics/metabolism ; Transformation, Genetic
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    RNA polymerase IV directs silencing of endogenous DNA (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-05
    Description: Plants encode subunits for a fourth RNA polymerase (Pol IV) in addition to the well-known DNA-dependent RNA polymerases I, II, and III. By mutation of the two largest subunits (NRPD1a and NRPD2), we show that Pol IV silences certain transposons and repetitive DNA in a short interfering RNA pathway involving RNA-dependent RNA polymerase 2 and Dicer-like 3. The existence of this distinct silencing polymerase may explain the paradoxical involvement of an RNA silencing pathway in maintenance of transcriptional silencing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herr, A J -- Jensen, M B -- Dalmay, T -- Baulcombe, D C -- New York, N.Y. -- Science. 2005 Apr 1;308(5718):118-20. Epub 2005 Feb 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics ; Arabidopsis Proteins/chemistry/genetics/metabolism ; Base Sequence ; Chromatin/metabolism ; DNA Methylation ; DNA Transposable Elements ; DNA, Plant/*genetics/metabolism ; DNA-Directed RNA Polymerases/chemistry/genetics/*metabolism ; *Gene Silencing ; Genes, Plant ; Genetic Complementation Test ; Green Fluorescent Proteins/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Oryza/enzymology/genetics ; Plants, Genetically Modified ; Protein Subunits/chemistry/genetics/metabolism ; RNA Interference ; RNA Polymerase II/metabolism ; RNA, Plant/metabolism ; RNA, Small Interfering/metabolism ; Repetitive Sequences, Nucleic Acid ; Transgenes
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    Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Min -- Arulandu, Arockiasamy -- Struck, Douglas K -- Swanson, Stephanie -- Sacchettini, James C -- Young, Ry -- GM27099/GM/NIGMS NIH HHS/ -- GM62410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637279" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage P1/*enzymology ; Binding Sites ; Catalytic Domain ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallography, X-Ray ; Cysteine/chemistry ; Enzyme Activation ; Escherichia coli/enzymology/virology ; Isomerism ; Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Muramidase/*chemistry/genetics/*metabolism ; Mutation ; Physicochemical Phenomena ; Protein Conformation ; Protein Sorting Signals ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism
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    Cell biology. Does Notch take the sweet road to success? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, John B -- 1P01CA71932/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1570-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor, MI 48109-2216, USA. johnlowe@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Cell Membrane/*metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Endoplasmic Reticulum/enzymology/metabolism ; Fucose/metabolism ; Fucosyltransferases/chemistry/genetics/*metabolism ; Guanosine Diphosphate Fucose/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Mutation ; Protein Folding ; Protein Transport ; RNA Interference ; Receptors, Cell Surface/*metabolism ; Receptors, Notch ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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    Cancer. An anchor for tumor cell invasion (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuspa, Stuart H -- Epstein, Ervin H Jr -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1727-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. sy12j@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774745" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Squamous Cell/etiology/genetics/pathology/*physiopathology ; Cell Adhesion Molecules/metabolism ; Cell Transformation, Neoplastic ; Collagen Type VII/chemistry/*genetics/*physiology ; Disease Susceptibility ; Epidermolysis Bullosa Dystrophica/complications/*genetics/metabolism/pathology ; Genes, ras ; Humans ; I-kappa B Proteins/genetics/metabolism ; Keratinocytes/*metabolism/pathology ; Mice ; Mutation ; Neoplasm Invasiveness ; Protein Structure, Tertiary ; Skin Neoplasms/etiology/genetics/pathology/*physiopathology ; Transduction, Genetic ; Transforming Growth Factor beta/metabolism
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    Stat3 dimerization regulated by reversible acetylation of a single lysine residue (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-18
    Description: Upon cytokine treatment, members of the signal transducers and activators of transcription (STAT) family of proteins are phosphorylated on tyrosine and serine sites within the carboxyl-terminal region in cells. We show that in response to cytokine treatment, Stat3 is also acetylated on a single lysine residue, Lys685. Histone acetyltransferase p300-mediated Stat3 acetylation on Lys685 was reversible by type I histone deacetylase (HDAC). Use of a prostate cancer cell line (PC3) that lacks Stat3 and PC3 cells expressing wild-type Stat3 or a Stat3 mutant containing a Lys685-to-Arg substitution revealed that Lys685 acetylation was critical for Stat3 to form stable dimers required for cytokine-stimulated DNA binding and transcriptional regulation, to enhance transcription of cell growth-related genes, and to promote cell cycle progression in response to treatment with oncostatin M.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, Zheng-Long -- Guan, Ying-Jie -- Chatterjee, Devasis -- Chin, Y Eugene -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):269-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, Brown University Medical School-Rhode Island Hospital, Providence, RI 02903, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653507" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/metabolism ; Arginine/chemistry/metabolism ; Cell Cycle ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cyclin D1/metabolism ; Cytokines/pharmacology/*physiology ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; HeLa Cells ; Histone Acetyltransferases ; Histone Deacetylases/metabolism ; Humans ; Interferon-alpha/pharmacology ; Lysine/*metabolism ; Mutation ; Nuclear Proteins/metabolism ; Oncostatin M ; Peptides/pharmacology ; Phosphorylation ; Protein Structure, Secondary ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Proto-Oncogene Proteins c-myc/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/chemistry/genetics/*metabolism ; Transcriptional Activation ; bcl-X Protein ; src Homology Domains
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    Functional interaction between beta-catenin and FOXO in oxidative stress signaling (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-21
    Description: beta-Catenin is a multifunctional protein that mediates Wnt signaling by binding to members of the T cell factor (TCF) family of transcription factors. Here, we report an evolutionarily conserved interaction of beta-catenin with FOXO transcription factors, which are regulated by insulin and oxidative stress signaling. beta-Catenin binds directly to FOXO and enhances FOXO transcriptional activity in mammalian cells. In Caenorhabditis elegans, loss of the beta-catenin BAR-1 reduces the activity of the FOXO ortholog DAF-16 in dauer formation and life span. Association of beta-catenin with FOXO was enhanced in cells exposed to oxidative stress. Furthermore, BAR-1 was required for the oxidative stress-induced expression of the DAF-16 target gene sod-3 and for resistance to oxidative damage. These results demonstrate a role for beta-catenin in regulating FOXO function that is particularly important under conditions of oxidative stress.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Essers, Marieke A G -- de Vries-Smits, Lydia M M -- Barker, Nick -- Polderman, Paulien E -- Burgering, Boudewijn M T -- Korswagen, Hendrik C -- New York, N.Y. -- Science. 2005 May 20;308(5725):1181-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry and Center for Biomedical Genetics, University Medical Center, Universiteitsweg 100, 3584 CG Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905404" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/genetics/*metabolism/physiology ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Carrier Proteins/genetics/metabolism ; Cell Cycle ; Cell Line ; Cell Line, Tumor ; Cyclin-Dependent Kinase Inhibitor p27 ; Cytoskeletal Proteins/chemistry/genetics/*metabolism ; DNA-Binding Proteins/metabolism ; Forkhead Transcription Factors ; Humans ; Hydrogen Peroxide/pharmacology ; Immunoprecipitation ; Insulin/pharmacology ; Intracellular Signaling Peptides and Proteins/genetics/metabolism ; Lithium Chloride/pharmacology ; Longevity ; Mice ; Mutation ; *Oxidative Stress ; Receptor, Insulin/genetics/metabolism ; *Signal Transduction ; Superoxide Dismutase/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/*metabolism ; Transfection ; beta Catenin
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    Carotenoid cation formation and the regulation of photosynthetic light harvesting (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-22
    Description: Photosynthetic light harvesting in excess light is regulated by a process known as feedback deexcitation. Femtosecond transient absorption measurements on thylakoid membranes show selective formation of a carotenoid radical cation upon excitation of chlorophyll under conditions of maximum, steady-state feedback deexcitation. Studies on transgenic Arabidopsis thaliana plants confirmed that this carotenoid radical cation formation is correlated with feedback deexcitation and requires the presence of zeaxanthin, the specific carotenoid synthesized during high light exposure. These results indicate that energy transfer from chlorophyll molecules to a chlorophyllzeaxanthin heterodimer, which then undergoes charge separation, is the mechanism for excess energy dissipation during feedback deexcitation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holt, Nancy E -- Zigmantas, Donatas -- Valkunas, Leonas -- Li, Xiao-Ping -- Niyogi, Krishna K -- Fleming, Graham R -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):433-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662017" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/metabolism ; Cations/metabolism ; Chlorophyll/*metabolism ; Feedback, Physiological ; Free Radicals ; Hydrogen-Ion Concentration ; Light ; Light-Harvesting Protein Complexes ; Mutation ; *Photosynthesis ; Photosynthetic Reaction Center Complex Proteins/metabolism ; Photosystem II Protein Complex/metabolism ; Plants, Genetically Modified ; Spectrometry, Fluorescence ; Spectrum Analysis ; Spinacia oleracea ; Thylakoids/*metabolism ; Xanthophylls ; Zeaxanthins ; beta Carotene/*analogs & derivatives/*metabolism
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    Antagonistic control of disease resistance protein stability in the plant immune system (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-25
    Description: Pathogen recognition by the plant immune system is governed by structurally related, polymorphic products of disease resistance (R) genes. RAR1 and/or SGT1b mediate the function of many R proteins. RAR1 controls preactivation R protein accumulation by an unknown mechanism. We demonstrate that Arabidopsis SGT1b has two distinct, genetically separable functions in the plant immune system: SGT1b antagonizes RAR1 to negatively regulate R protein accumulation before infection, and SGT1b has a RAR1-independent function that regulates programmed cell death during infection. The balanced activities of RAR1 and SGT1, in concert with cytosolic HSP90, modulate preactivation R protein accumulation and signaling competence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holt, Ben F 3rd -- Belkhadir, Youssef -- Dangl, Jeffery L -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):929-32. Epub 2005 Jun 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976272" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis ; Arabidopsis/*immunology/microbiology ; Arabidopsis Proteins/genetics/immunology/*physiology ; Carrier Proteins/antagonists & inhibitors/immunology/*physiology ; Cell Cycle Proteins/immunology/*physiology ; Genes, Plant ; HSP90 Heat-Shock Proteins/immunology/physiology ; Mutation ; Peronospora/physiology ; Plant Diseases/microbiology ; Plant Proteins/antagonists & inhibitors/immunology/*physiology ; Plants, Genetically Modified ; Signal Transduction
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    Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: Innate immunity in higher plants invokes a sophisticated surveillance system capable of recognizing bacterial effector proteins. In Arabidopsis, resistance to infection by strains of Pseudomonas syringae expressing the effector AvrRpt2 requires the plant resistance protein RPS2. AvrRpt2 was identified as a putative cysteine protease that results in the elimination of the Arabidopsis protein RIN4. RIN4 cleavage serves as a signal to activate RPS2-mediated resistance. AvrRpt2 is delivered into the plant cell, where it is activated by a eukaryotic factor that we identify as cyclophilin. This activation of AvrRpt2 is necessary for protease activity. Active AvrRpt2 can then directly cleave RIN4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coaker, Gitta -- Falick, Arnold -- Staskawicz, Brian -- R01-FM069680-01/PHS HHS/ -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):548-50. Epub 2005 Mar 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746386" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*immunology/*metabolism/microbiology ; Arabidopsis Proteins/genetics/*metabolism ; Bacterial Proteins/chemistry/*metabolism ; Carrier Proteins/genetics/*metabolism ; Cyclophilins/*metabolism ; Cyclosporine/pharmacology ; Cysteine Endopeptidases/metabolism ; Enzyme Activation ; Escherichia coli ; Mass Spectrometry ; Mutation ; Peptide Mapping ; Plant Diseases ; Pseudomonas syringae/*metabolism/pathogenicity ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; Sirolimus/pharmacology
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    Cell-to-cell transfer of bacterial outer membrane lipoproteins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Myxococcus xanthus cells can glide forward by retracting type IV pili. Tgl, an outer membrane lipoprotein, is necessary to assemble pili. Tgl mutants can be transiently "stimulated" if brought into end-to-end contact with tgl+ donor cells. By separating the stimulated recipient cells from donor cells, we found that Tgl protein was transferred from the donors to the rescued recipient cells. Mutants lacking CglB lipoprotein, which is part of a second gliding engine, could also be stimulated, and CglB protein was transferred from donor to recipient cells. The high transfer efficiency of Tgl and CglB proteins suggests that donor and recipient cells briefly fuse their outer membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nudleman, Eric -- Wall, Daniel -- Kaiser, Dale -- GM23441/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):125-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Developmental Biology and Biochemistry, Stanford University School of Medicine, B300 Beckman Center, 279 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994555" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Bacterial/genetics/*metabolism ; Bacterial Proteins/genetics/*metabolism ; Cell Membrane/physiology ; Fimbriae Proteins/metabolism ; Flow Cytometry ; Green Fluorescent Proteins/genetics/metabolism ; Immunoblotting ; Lipoproteins/genetics/*metabolism ; Membrane Fusion ; Membrane Proteins/genetics/*metabolism ; Microscopy, Fluorescence ; Microscopy, Phase-Contrast ; Movement ; Mutation ; Myxococcus xanthus/genetics/*metabolism/physiology
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    Reconstructing the origin of Andaman Islanders (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-14
    Description: The origin of the Andaman "Negrito" and Nicobar "Mongoloid" populations has been ambiguous. Our analyses of complete mitochondrial DNA sequences from Onges and Great Andaman populations revealed two deeply branching clades that share their most recent common ancestor in founder haplogroup M, with lineages spread among India, Africa, East Asia, New Guinea, and Australia. This distribution suggests that these two clades have likely survived in genetic isolation since the initial settlement of the islands during an out-of-Africa migration by anatomically modern humans. In contrast, Nicobarese sequences illustrate a close genetic relationship with populations from Southeast Asia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thangaraj, Kumarasamy -- Chaubey, Gyaneshwer -- Kivisild, Toomas -- Reddy, Alla G -- Singh, Vijay Kumar -- Rasalkar, Avinash A -- Singh, Lalji -- New York, N.Y. -- Science. 2005 May 13;308(5724):996.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Cellular and Molecular Biology, Hyderabad-500 007, India.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890876" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Asia ; Asia, Southeastern ; Chromosomes, Human, Y/genetics ; DNA, Mitochondrial/*genetics ; Emigration and Immigration ; Ethnic Groups/*genetics ; Founder Effect ; Genetic Drift ; Genetics, Population ; Geography ; Haplotypes ; Humans ; India ; Mutation ; Phylogeny ; Sequence Analysis, DNA
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    T helper cell fate specified by kinase-mediated interaction of T-bet with GATA-3 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-22
    Description: Cell lineage specification depends on both gene activation and gene silencing, and in the differentiation of T helper progenitors to Th1 or Th2 effector cells, this requires the action of two opposing transcription factors, T-bet and GATA-3. T-bet is essential for the development of Th1 cells, and GATA-3 performs an equivalent role in Th2 development. We report that T-bet represses Th2 lineage commitment through tyrosine kinase-mediated interaction between the two transcription factors that interferes with the binding of GATA-3 to its target DNA. These results provide a novel function for tyrosine phosphorylation of a transcription factor in specifying alternate fates of a common progenitor cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, Eun Sook -- Szabo, Susanne J -- Schwartzberg, Pamela L -- Glimcher, Laurie H -- AI48126/AI/NIAID NIH HHS/ -- AI56296/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Lineage ; Cytokines/pharmacology/physiology ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; GATA3 Transcription Factor ; Interleukin-5/genetics ; Mice ; Mice, Inbred BALB C ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/metabolism ; T-Box Domain Proteins ; T-Lymphocytes, Helper-Inducer/cytology/*physiology ; Th1 Cells/cytology/physiology ; Th2 Cells/cytology/*physiology ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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    Virology. Culture systems for hepatitis C virus in sight at last (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1539-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947152" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Genes, Viral ; Hepacivirus/*genetics/*growth & development/isolation & purification ; Hepatitis C/virology ; Humans ; Liver ; Mutation ; RNA, Viral/genetics ; *Replicon ; Transfection ; Viral Nonstructural Proteins/genetics ; Virus Cultivation/*methods ; Virus Replication
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    A conserved checkpoint monitors meiotic chromosome synapsis in Caenorhabditis elegans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-13
    Description: We report the discovery of a checkpoint that monitors synapsis between homologous chromosomes to ensure accurate meiotic segregation. Oocytes containing unsynapsed chromosomes selectively undergo apoptosis even if a germline DNA damage checkpoint is inactivated. This culling mechanism is specifically activated by unsynapsed pairing centers, cis-acting chromosome sites that are also required to promote synapsis in Caenorhabditis elegans. Apoptosis due to synaptic failure also requires the C. elegans homolog of PCH2, a budding yeast pachytene checkpoint gene, which suggests that this surveillance mechanism is widely conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhalla, Needhi -- Dernburg, Abby F -- 1 F32 GM67408-01A1/GM/NIGMS NIH HHS/ -- 1 R01 GM/CA655591-01/GM/NIGMS NIH HHS/ -- F32 GM067408/GM/NIGMS NIH HHS/ -- F32 GM067408-01A1/GM/NIGMS NIH HHS/ -- F32 GM067408-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1683-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339446" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Caenorhabditis elegans/genetics/*physiology ; Caenorhabditis elegans Proteins/genetics/physiology ; Chromosome Pairing/*physiology ; Chromosome Segregation ; Disorders of Sex Development ; Female ; Genes, Helminth ; Male ; *Meiosis ; Mutation ; Oocytes/physiology ; Recombination, Genetic ; Transgenes ; X Chromosome/genetics/physiology
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    A homolog of Drosophila grainy head is essential for epidermal integrity in mice (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-04-16
    Description: The Drosophila cuticle is essential for maintaining the surface barrier defenses of the fly. Integral to cuticle resilience is the transcription factor grainy head, which regulates production of the enzyme required for covalent cross-linking of the cuticular structural components. We report that formation and maintenance of the epidermal barrier in mice are dependent on a mammalian homolog of grainy head, Grainy head-like 3. Mice lacking this factor display defective skin barrier function and deficient wound repair, accompanied by reduced expression of transglutaminase 1, the key enzyme involved in cross-linking the structural components of the superficial epidermis. These findings suggest that the functional mechanisms involving protein cross-linking that maintain the epidermal barrier and induce tissue repair are conserved across 700 million years of evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ting, Stephen B -- Caddy, Jacinta -- Hislop, Nikki -- Wilanowski, Tomasz -- Auden, Alana -- Zhao, Lin-Lin -- Ellis, Sarah -- Kaur, Pritinder -- Uchida, Yoshikazu -- Holleran, Walter M -- Elias, Peter M -- Cunningham, John M -- Jane, Stephen M -- P01 HL53749-03/HL/NHLBI NIH HHS/ -- P01-AR39448/AR/NIAMS NIH HHS/ -- P30 CA 21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):411-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rotary Bone Marrow Research Laboratories, c/o Royal Melbourne Hospital Post Office, Grattan Street, Parkville, Victoria, Australia 3050.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831758" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biological Evolution ; DNA-Binding Proteins/*genetics/metabolism/*physiology ; Embryo, Mammalian/physiology ; Embryonic Development ; Epidermis/*embryology/*physiology ; Epithelium/physiology ; Gene Expression ; Kruppel-Like Transcription Factors ; Mice ; Mutation ; Permeability ; Transcription Factors/*genetics/metabolism/*physiology ; Transglutaminases/genetics/metabolism ; Wound Healing/*physiology
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    Widespread parallel evolution in sticklebacks by repeated fixation of Ectodysplasin alleles (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-03-26
    Description: Major phenotypic changes evolve in parallel in nature by molecular mechanisms that are largely unknown. Here, we use positional cloning methods to identify the major chromosome locus controlling armor plate patterning in wild threespine sticklebacks. Mapping, sequencing, and transgenic studies show that the Ectodysplasin (EDA) signaling pathway plays a key role in evolutionary change in natural populations and that parallel evolution of stickleback low-plated phenotypes at most freshwater locations around the world has occurred by repeated selection of Eda alleles derived from an ancestral low-plated haplotype that first appeared more than two million years ago. Members of this clade of low-plated alleles are present at low frequencies in marine fish, which suggests that standing genetic variation can provide a molecular basis for rapid, parallel evolution of dramatic phenotypic change in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colosimo, Pamela F -- Hosemann, Kim E -- Balabhadra, Sarita -- Villarreal, Guadalupe Jr -- Dickson, Mark -- Grimwood, Jane -- Schmutz, Jeremy -- Myers, Richard M -- Schluter, Dolph -- Kingsley, David M -- 1P50HG02568/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1928-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305-5329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790847" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; *Biological Evolution ; Body Patterning ; Chromosome Walking ; Cloning, Molecular ; Ectodysplasins ; Fresh Water ; Gene Frequency ; Genetic Variation ; Haplotypes ; Linkage Disequilibrium ; Membrane Proteins/*genetics/physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Polymorphism, Single Nucleotide ; Seawater ; Selection, Genetic ; Sequence Analysis, DNA ; Signal Transduction ; Smegmamorpha/*anatomy & histology/classification/*genetics/growth & development
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    Type VII collagen is required for Ras-driven human epidermal tumorigenesis (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-03-19
    Description: Type VII collagen defects cause recessive dystrophic epidermolysis bullosa (RDEB), a blistering skin disorder often accompanied by epidermal cancers. To study the role of collagen VII in these cancers, we examined Ras-driven tumorigenesis in RDEB keratinocytes. Cells devoid of collagen VII did not form tumors in mice, whereas those retaining a specific collagen VII fragment (the amino-terminal noncollagenous domain NC1) were tumorigenic. Forced NC1 expression restored tumorigenicity to collagen VII-null epidermis in a non-cell-autonomous fashion. Fibronectin-like sequences within NC1 (FNC1) promoted tumor cell invasion in a laminin 5-dependent manner and were required for tumorigenesis. Tumor-stroma interactions mediated by collagen VII thus promote neoplasia, and retention of NC1 sequences in a subset of RDEB patients may contribute to their increased susceptibility to squamous cell carcinoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ortiz-Urda, Susana -- Garcia, John -- Green, Cheryl L -- Chen, Lei -- Lin, Qun -- Veitch, Dallas P -- Sakai, Lynn Y -- Lee, Hyangkyu -- Marinkovich, M Peter -- Khavari, Paul A -- AR43799/AR/NIAMS NIH HHS/ -- AR44012/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1773-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉VA Palo Alto Healthcare System, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774758" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Animals ; Antibodies/immunology ; Apoptosis ; Carcinoma, Squamous Cell/etiology/*physiopathology ; Cell Adhesion Molecules/immunology/metabolism ; Cell Proliferation ; Cell Transformation, Neoplastic ; Child ; Collagen Type VII/chemistry/*genetics/immunology/*physiology ; Disease Susceptibility ; Epidermolysis Bullosa Dystrophica/complications/*genetics/metabolism/pathology ; Female ; *Genes, ras ; Humans ; I-kappa B Proteins/genetics/metabolism ; Keratinocytes/*metabolism/pathology ; Male ; Mice ; Mice, SCID ; Middle Aged ; Mutation ; Neoplasm Invasiveness ; Protein Structure, Tertiary ; Skin Neoplasms/etiology/pathology/*physiopathology
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    Cell signaling. Stat acetylation--a key facet of cytokine signaling? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, John J -- Kanno, Yuka -- Chen, Xiaomin -- Levy, David E -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):217-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653493" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/metabolism ; Active Transport, Cell Nucleus ; Cell Nucleus/metabolism ; Cells, Cultured ; Cytokines/*physiology ; Cytoplasm/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; Histone Acetyltransferases ; Histone Deacetylases/metabolism ; Lysine/*metabolism ; Mutation ; NF-kappa B/metabolism ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Processing, Post-Translational ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/chemistry/genetics/*metabolism ; Transcriptional Activation ; src Homology Domains
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    The pseudo-response regulator Ppd-H1 provides adaptation to photoperiod in barley (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-15
    Description: Plants commonly use photoperiod (day length) to control the timing of flowering during the year, and variation in photoperiod response has been selected in many crops to provide adaptation to different environments and farming practices. Positional cloning identified Ppd-H1, the major determinant of barley photoperiod response, as a pseudo-response regulator, a class of genes involved in circadian clock function. Reduced photoperiod responsiveness of the ppd-H1 mutant, which is highly advantageous in spring-sown varieties, is explained by altered circadian expression of the photoperiod pathway gene CONSTANS and reduced expression of its downstream target, FT, a key regulator of flowering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turner, Adrian -- Beales, James -- Faure, Sebastien -- Dunford, Roy P -- Laurie, David A -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1031-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crop Genetics Department, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284181" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Circadian Rhythm ; Cloning, Molecular ; Crosses, Genetic ; Flowers/physiology ; Gene Expression Profiling ; Gene Expression Regulation, Plant ; *Genes, Plant ; Hordeum/genetics/*physiology ; Molecular Sequence Data ; Mutation ; *Photoperiod ; Plant Proteins/chemistry/genetics/*physiology ; Polymerase Chain Reaction ; Polymorphism, Single Nucleotide ; Protein Structure, Tertiary
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Editing at the crossroad of innate and adaptive immunity (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-19
    Description: Genetic information can be altered through the enzymatic modification of nucleotide sequences. This process, known as editing, was originally identified in the mitochondrial RNA of trypanosomes and later found to condition events as diverse as neurotransmission and lipid metabolism in mammals. Recent evidence reveals that editing enzymes may fulfill one of their most essential roles in the defense against infectious agents: first, as the mediators of antibody diversification, a step crucial for building adaptive immunity, and second, as potent intracellular poisons for the replication of viruses. Exciting questions are raised, which take us to the depth of the intimate relations between vertebrates and the microbial underworld.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turelli, Priscilla -- Trono, Didier -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1061-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Life Sciences, Ecole Polytechnique Federale de Lausanne, CH-1015 Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15718460" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytidine/metabolism ; Cytidine Deaminase/*metabolism ; DNA, Viral/*metabolism ; Deamination ; Evolution, Molecular ; Hepatitis B virus/genetics/physiology ; Humans ; *Immunity, Active ; *Immunity, Innate ; Mutation ; *RNA Editing ; RNA, Viral/metabolism ; Retroelements ; Retroviridae/pathogenicity/physiology ; Virus Diseases/*immunology/metabolism/virology ; Virus Replication
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Plant sciences. Recognition at a distance (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulze-Lefert, Paul -- Bieri, Stephane -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):506-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Microbe Interactions, Max-Planck-Institut fur Zuchtungsforschung, D-50829 Koln, Germany. schlef@mpiz-koeln.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15845841" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*immunology/metabolism/microbiology ; Arabidopsis Proteins/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Carrier Proteins/metabolism ; Cladosporium/immunology/metabolism ; Cyclophilins/metabolism ; Fungal Proteins/*metabolism ; Leucine ; Lycopersicon esculentum/*immunology/metabolism/microbiology ; Models, Immunological ; Mutation ; Peptide Hydrolases/genetics/metabolism ; Plant Diseases ; Plant Proteins/chemistry/genetics/*metabolism ; Protein Conformation ; Pseudomonas syringae/immunology/metabolism ; Recombinant Proteins/metabolism ; Repetitive Sequences, Amino Acid
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    Human symbionts use a host-like pathway for surface fucosylation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: The mammalian intestine harbors a beneficial microbiota numbering approximately 10(12) organisms per gram of colonic content. The host tolerates this tremendous bacterial load while maintaining the ability to efficiently respond to pathogenic organisms. In this study, we show that the Bacteroides use a mammalian-like pathway to decorate numerous surface capsular polysaccharides and glycoproteins with l-fucose, an abundant surface molecule of intestinal epithelial cells, resulting in the coordinated expression of this surface molecule by host and symbiont. A Bacteroides mutant deficient in the ability to cover its surface with L-fucose is defective in colonizing the mammalian intestine under competitive conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coyne, Michael J -- Reinap, Barbara -- Lee, Martin M -- Comstock, Laurie E -- AI44193/AI/NIAID NIH HHS/ -- AI53694/AI/NIAID NIH HHS/ -- R01 AI044193/AI/NIAID NIH HHS/ -- R01 AI044193-07/AI/NIAID NIH HHS/ -- R01 AI053694/AI/NIAID NIH HHS/ -- R01 AI053694-03/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1778-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774760" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Bacterial Capsules/biosynthesis/chemistry/*metabolism ; Bacterial Proteins/biosynthesis/metabolism ; Bacteroides fragilis/enzymology/genetics/growth & development/*metabolism ; Culture Media ; Feces/microbiology ; Fucose/*metabolism ; Gene Deletion ; Genes, Bacterial ; Glycoproteins/biosynthesis/*metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Hydro-Lyases/genetics/metabolism ; Intestinal Mucosa/metabolism ; Intestines/*microbiology ; Mice ; Molecular Mimicry ; Molecular Sequence Data ; Mutation ; Phosphotransferases (Alcohol Group Acceptor)/genetics/metabolism ; *Symbiosis
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    Extrusion and death of DPP/BMP-compromised epithelial cells in the developing Drosophila wing (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: During animal development, epithelial cell fates are specified according to spatial position by extracellular signaling pathways. Among these, the transforming growth factor beta/bone morphogenetic protein (TGF-beta/BMP) pathways are evolutionarily conserved and play crucial roles in the development and homeostasis of a wide range of multicellular tissues. Here we show that in the developing Drosophila wing imaginal epithelium, cell clones deprived of the BMP-like ligand Decapentaplegic (DPP) do not die as previously thought but rather extrude from the cell layer as viable cysts exhibiting marked abnormalities in cell shape and cytoskeletal organization. We propose that in addition to assigning cell fates, a crucial developmental function of DPP/BMP signaling is the position-specific control of epithelial architecture.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, Matthew C -- Perrimon, Norbert -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1785-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774762" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/analysis ; Alleles ; Animals ; Apoptosis ; Body Patterning ; Cell Death ; Cell Shape ; Clone Cells/cytology/physiology/ultrastructure ; Drosophila Proteins/genetics/*metabolism ; Drosophila melanogaster/*cytology/genetics/growth & development/physiology ; Epithelial Cells/cytology/*physiology/ultrastructure ; Ethyl Methanesulfonate ; JNK Mitogen-Activated Protein Kinases/metabolism ; Microtubules/ultrastructure ; Morphogenesis ; Mutagens ; Mutation ; Phenotype ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Receptors, Cell Surface/genetics/metabolism ; *Signal Transduction ; Transforming Growth Factor beta/metabolism ; Wings, Animal/*cytology/embryology/growth & development
    Print ISSN: 0036-8075
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    Chitin induces natural competence in Vibrio cholerae (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: The mosaic-structured Vibrio cholerae genome points to the importance of horizontal gene transfer (HGT) in the evolution of this human pathogen. We showed that V. cholerae can acquire new genetic material by natural transformation during growth on chitin, a biopolymer that is abundant in aquatic habitats (e.g., from crustacean exoskeletons), where it lives as an autochthonous microbe. Transformation competence was found to require a type IV pilus assembly complex, a putative DNA binding protein, and three convergent regulatory cascades, which are activated by chitin, increasing cell density, and nutrient limitation, a decline in growth rate, or stress.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meibom, Karin L -- Blokesch, Melanie -- Dolganov, Nadia A -- Wu, Cheng-Yen -- Schoolnik, Gary K -- AI053706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1824-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases and Geographic Medicine, Department of Microbiology and Immunology, and Stanford Institute for the Environment, Stanford University, Stanford, CA 94305, USA. kmeibom@necker.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357262" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/genetics/metabolism/physiology ; Biofilms/growth & development ; Brachyura/microbiology ; Chitin/metabolism/*physiology ; Culture Media ; DNA-Binding Proteins/genetics/metabolism ; Fimbriae Proteins/biosynthesis/genetics ; Fimbriae, Bacterial/metabolism ; Frameshift Mutation ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Models, Biological ; Mutation ; Phenotype ; Regulon ; Sigma Factor/metabolism ; *Transformation, Bacterial ; Vibrio cholerae/*genetics/growth & development/metabolism/physiology ; Vibrio cholerae O1/*genetics/growth & development/metabolism/physiology
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    What genetic changes made us uniquely human? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culotta, Elizabeth -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior ; *Biological Evolution ; Brain/physiology ; Forecasting ; Genome ; *Genome, Human ; Hominidae/*genetics ; Humans ; Mutation ; Primates/*genetics ; Selection, Genetic ; Speech
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    Evolution. The synthesis and evolution of a supermodel (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, Greg -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1890-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, North Carolina State University, Raleigh, NC 27695, USA. ggibson@ncsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790836" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Animals, Genetically Modified ; *Biological Evolution ; Chromosome Mapping ; Chromosome Walking ; Crosses, Genetic ; Ectodysplasins ; Fresh Water ; Gene Frequency ; Genetic Variation ; Haplotypes ; Membrane Proteins/*genetics ; Mutation ; Seawater ; Selection, Genetic ; Smegmamorpha/*anatomy & histology/*genetics/growth & development
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    Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: Hsp90 is a molecular chaperone for many signal transducers and may influence evolution by releasing previously silent genetic variation in response to environmental change. In fungi separated by approximately 800 million years of evolution, Hsp90 potentiated the evolution of drug resistance in a different way, by enabling new mutations to have immediate phenotypic consequences. Resistance was abrogated by Hsp90 inhibitors and by febrile temperatures, suggesting new therapeutic strategies and a clinical benefit of fever. During selection in a human host, drug resistance that was initially Hsp90-dependent evolved toward independence. Thus, Hsp90 can act in diverse ways to couple environmental contingency to the emergence and fixation of new traits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cowen, Leah E -- Lindquist, Susan -- P30ES02109/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2185-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195452" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Opportunistic Infections/microbiology ; Antifungal Agents/*pharmacology ; Aspergillosis/microbiology ; Aspergillus/drug effects/genetics ; *Biological Evolution ; Calcineurin/genetics/*physiology ; Calcineurin Inhibitors ; Candida albicans/*drug effects/genetics ; Candidiasis/microbiology ; Cyclophilin A/metabolism ; *Drug Resistance, Fungal ; Echinocandins ; Ergosterol/biosynthesis ; Fluconazole/pharmacology ; HSP90 Heat-Shock Proteins/antagonists & inhibitors/genetics/*physiology ; Humans ; Mutation ; Peptides, Cyclic/pharmacology ; Phenotype ; Saccharomyces cerevisiae/*drug effects/genetics/metabolism ; Saccharomyces cerevisiae Proteins/antagonists & inhibitors/genetics/*physiology ; Selection, Genetic
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    Regulated pole-to-pole oscillations of a bacterial gliding motility protein (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-08
    Description: Little is known about directed motility of bacteria that move by type IV pilus-mediated (twitching) motility. Here, we found that during periodic cell reversals of Myxoccocus xanthus, type IV pili were disassembled at one pole and reassembled at the other pole. Accompanying these reversals, FrzS, a protein required for directed motility, moved in an oscillatory pattern between the cell poles. The frequency of the oscillations was controlled by the Frz chemosensory system, which is essential for directed motility. Pole-to-pole migration of FrzS appeared to involve movement along a filament running the length of the cell. FrzS dynamics may thus regulate cell polarity during directed motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mignot, Tam -- Merlie, John P Jr -- Zusman, David R -- GM20509/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 4;310(5749):855-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, Department of Molecular and Cell Biology, Berkeley, CA 94720-3204, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16272122" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Cell Polarity ; Cytosol/metabolism ; Fimbriae, Bacterial/*physiology ; Fluorescence Recovery After Photobleaching ; Green Fluorescent Proteins/metabolism ; Microscopy, Fluorescence ; Movement ; Mutation ; Myxococcus xanthus/cytology/*physiology ; Recombinant Fusion Proteins/metabolism
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    Genetics. Was the Human Genome Project worth the effort? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-17
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2582021/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2582021/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daiger, Stephen P -- R01 EY007142/EY/NEI NIH HHS/ -- R01 EY007142-12A2/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):362-4. Epub 2005 Mar 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genetics Center, University of Texas Health Sciences Center, Houston, TX 77030, USA. stephen.p.daiger@uth.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15769856" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/genetics ; Alleles ; Amino Acid Substitution ; Case-Control Studies ; Chromosome Mapping ; Chromosomes, Human, Pair 1/genetics ; Complement Factor H/chemistry/*genetics/metabolism ; Complement System Proteins/physiology ; Genetic Markers ; Genetic Predisposition to Disease ; Genetic Variation ; Haplotypes ; Histidine/genetics ; *Human Genome Project ; Humans ; Immunity, Innate ; Macular Degeneration/*genetics ; Mutation ; Oligonucleotide Array Sequence Analysis ; Polymorphism, Genetic ; Polymorphism, Single Nucleotide ; Retrospective Studies ; Risk Factors
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    Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perez-Morga, David -- Vanhollebeke, Benoit -- Paturiaux-Hanocq, Francoise -- Nolan, Derek P -- Lins, Laurence -- Homble, Fabrice -- Vanhamme, Luc -- Tebabi, Patricia -- Pays, Annette -- Poelvoorde, Philippe -- Jacquet, Alain -- Brasseur, Robert -- Pays, Etienne -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):469-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Parasitology, IBMM, Universite Libre de Bruxelles, 12, rue des Profs Jeener et Brachet, B6041 Gosselies, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020735" target="_blank"〉PubMed〈/a〉
    Keywords: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid/pharmacology ; Amino Acid Sequence ; Animals ; Anions/metabolism ; Apolipoproteins/*chemistry/genetics/*metabolism/pharmacology ; Cells, Immobilized ; Chlorides/metabolism ; Colicins/chemistry/pharmacology ; Escherichia coli/drug effects/growth & development ; Humans ; Intracellular Membranes/drug effects/*metabolism/ultrastructure ; Ion Channels/metabolism ; Lipid Bilayers/chemistry ; Lipoproteins, HDL/*chemistry/genetics/*metabolism/pharmacology ; Lysosomes/drug effects/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Permeability ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/metabolism ; Trypanosoma brucei brucei/drug effects/*metabolism/ultrastructure
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    Extrusion of cells with inappropriate Dpp signaling from Drosophila wing disc epithelia (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: Decapentaplegic (Dpp) is a signaling molecule that controls growth and patterning of the developing Drosophila wing. Mutant cells lacking Dpp signal transduction have been shown to activate c-Jun amino-terminal kinase (JNK)-dependent apoptosis and to be lost from the wing disc epithelium. These observations have led to the hypothesis that Dpp promotes cell survival by preventing apoptosis. Here, we show that in the absence of JNK-dependent apoptosis, mutant cells lacking Dpp signal transduction can survive; however, they are still lost from the wing disc epithelium. This loss correlates with extensive cytoskeletal changes followed by basal epithelial extrusion. We propose that Dpp promotes cell survival within disc epithelia by affecting cytoskeletal organization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shen, Jie -- Dahmann, Christian -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1789-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774763" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/analysis ; Animals ; Apoptosis ; Cell Shape ; Cell Survival ; Clone Cells/cytology/physiology ; Cytoskeleton/ultrastructure ; Drosophila Proteins/genetics/*metabolism ; Drosophila melanogaster/*cytology/genetics/growth & development/physiology ; Epithelial Cells/cytology/*physiology/ultrastructure ; Genes, Insect ; Intercellular Junctions/ultrastructure ; Larva/cytology/growth & development/metabolism ; Microtubules/ultrastructure ; Mutation ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Receptors, Cell Surface/genetics/metabolism ; *Signal Transduction ; Transforming Growth Factor beta/metabolism ; Wings, Animal/*cytology/growth & development/metabolism
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    Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the substrate) and ubiquitin. MIR1 and MIR2 are two E3 ubiquitin ligases encoded by Kaposi's sarcoma-associated herpesvirus that mediate the ubiquitination of major histocompatibility complex class I (MHC I) molecules and subsequent internalization. Here, we found that MIR1, but not MIR2, promoted down-regulation of MHC I molecules lacking lysine residues in their intracytoplasmic domain. In the presence of MIR1, these MHC I molecules were ubiquitinated, and their association with ubiquitin was sensitive to beta2-mercaptoethanol, unlike lysine-ubiquitin bonds. This form of ubiquitination required a cysteine residue in the intracytoplasmic tail of MHC I molecules. An MHC I molecule containing a single cysteine residue in an artificial glycine and alanine intracytoplasmic domain was endocytosed and degraded in the presence of MIR1. Thus, ubiquitination can occur on proteins lacking accessible lysines or an accessible N terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cadwell, Ken -- Coscoy, Laurent -- 1R01CA108447-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):127-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, 142 Life Sciences Addition Room 3200, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; CHO Cells ; Cell Line ; Cricetinae ; Cysteine/chemistry/metabolism ; Down-Regulation ; Endocytosis ; HLA-B7 Antigen/chemistry/genetics/*metabolism ; Herpesvirus 8, Human/*enzymology ; Humans ; Lysine/metabolism ; Mutation ; Protein Structure, Tertiary ; Serine/chemistry/metabolism ; Transduction, Genetic ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligases/*metabolism
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    NSP1 of the GRAS protein family is essential for rhizobial Nod factor-induced transcription (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-18
    Description: Rhizobial Nod factors induce in their legume hosts the expression of many genes and set in motion developmental processes leading to root nodule formation. Here we report the identification of the Medicago GRAS-type protein Nodulation signaling pathway 1 (NSP1), which is essential for all known Nod factor-induced changes in gene expression. NSP1 is constitutively expressed, and so it acts as a primary transcriptional regulator mediating all known Nod factor-induced transcriptional responses, and therefore, we named it a Nod factor response factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smit, Patrick -- Raedts, John -- Portyanko, Vladimir -- Debelle, Frederic -- Gough, Clare -- Bisseling, Ton -- Geurts, Rene -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Science, Laboratory of Molecular Biology, Wageningen University, Wageningen 6703 HA, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961669" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/metabolism ; Cell Nucleus/metabolism ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/*metabolism ; Medicago/*genetics/metabolism/*microbiology ; Molecular Sequence Data ; Mutation ; Plant Proteins/chemistry/genetics/*metabolism ; Plant Roots/metabolism/microbiology ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; Signal Transduction ; Sinorhizobium meliloti/*physiology ; Symbiosis ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic
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    Cell biology. Of grainy heads and broken skins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harden, Nicholas -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):364-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, V5A 1S6 Canada. nharden@sfu.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831745" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biological Evolution ; DNA-Binding Proteins/chemistry/*metabolism ; Dopa Decarboxylase/genetics/metabolism ; Drosophila/*embryology/genetics/metabolism ; Drosophila Proteins/genetics/metabolism ; Embryo, Mammalian/physiology ; Embryo, Nonmammalian/physiology ; Enhancer Elements, Genetic ; Epidermis/cytology/*embryology/physiology ; Epithelium/physiology ; Extracellular Signal-Regulated MAP Kinases/metabolism ; *Gene Expression Regulation ; Genes, Reporter ; JNK Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Signaling System ; Mice ; Mutation ; Nuclear Proteins ; *Signal Transduction ; Transcription Factor AP-1/metabolism ; Transcription Factors/chemistry/*metabolism ; Transcription, Genetic ; Transglutaminases/metabolism ; Tyrosine 3-Monooxygenase/genetics/metabolism ; *Wound Healing
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    Arabidopsis H+-PPase AVP1 regulates auxin-mediated organ development (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-08
    Description: The transport of auxin controls developmental events in plants. Here, we report that in addition to maintaining vacuolar pH, the H+-pyrophosphatase, AVP1, controls auxin transport and consequently auxin-dependent development. AVP1 overexpression results in increased cell division at the onset of organ formation, hyperplasia, and increased auxin transport. In contrast, avp1-1 null mutants have severely disrupted root and shoot development and reduced auxin transport. Changes in the expression of AVP1 affect the distribution and abundance of the P-adenosine triphosphatase and Pinformed 1 auxin efflux facilitator, two proteins implicated in auxin distribution. Thus, AVP1 facilitates the auxin fluxes that regulate organogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Jisheng -- Yang, Haibing -- Peer, Wendy Ann -- Richter, Gregory -- Blakeslee, Joshua -- Bandyopadhyay, Anindita -- Titapiwantakun, Boosaree -- Undurraga, Soledad -- Khodakovskaya, Mariya -- Richards, Elizabeth L -- Krizek, Beth -- Murphy, Angus S -- Gilroy, Simon -- Gaxiola, Roberto -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Science, University of Connecticut, Storrs, CT 06268, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210544" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Arabidopsis/cytology/genetics/*growth & development/*metabolism ; Arabidopsis Proteins/metabolism ; Biological Transport ; Cell Count ; Cell Proliferation ; Cell Shape ; Cell Wall/metabolism ; Hydrogen-Ion Concentration ; In Situ Hybridization ; Indoleacetic Acids/*metabolism/pharmacology ; Inorganic Pyrophosphatase/genetics/*metabolism ; Membrane Transport Proteins/metabolism ; Meristem/metabolism ; Microsomes/metabolism ; Mutation ; Plant Leaves/cytology/growth & development/metabolism ; Plant Roots/cytology/growth & development/metabolism ; Proton Pumps/genetics/*metabolism ; RNA Interference ; Signal Transduction ; Transformation, Genetic
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    Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: The structure of a synaptic intermediate of the site-specific recombinase gammadelta resolvase covalently linked through Ser10 to two cleaved duplex DNAs has been determined at 3.4 angstrom resolution. This resolvase, activated for recombination by mutations, forms a tetramer whose structure is substantially changed from that of a presynaptic complex between dimeric resolvase and the cleavage site DNA. Because the two cleaved DNA duplexes that are to be recombined lie on opposite sides of the core tetramer, large movements of both protein and DNA are required to achieve strand exchange. The two dimers linked to the DNAs that are to be recombined are held together by a flat interface. This may allow a 180 degrees rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Weikai -- Kamtekar, Satwik -- Xiong, Yong -- Sarkis, Gary J -- Grindley, Nigel D F -- Steitz, Thomas A -- GM28470/GM/NIGMS NIH HHS/ -- GM57510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1210-5. Epub 2005 Jun 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994378" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites ; Catalytic Domain ; Computer Simulation ; Crystallography, X-Ray ; DNA/*chemistry/*metabolism ; Dimerization ; Models, Molecular ; Mutation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombination, Genetic ; Transposon Resolvases/*chemistry/genetics/metabolism
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    Signal transduction. Signaling specificity in yeast (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elion, Elaine A -- Qi, Maosong -- Chen, Weidong -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):687-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. elaine_elion@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692041" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/metabolism ; Cyclin-Dependent Kinase Inhibitor Proteins ; DNA-Binding Proteins/genetics/metabolism ; Down-Regulation ; F-Box Proteins/metabolism ; Genes, Fungal ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*metabolism ; Mutation ; Peptides/pharmacology ; Pheromones/pharmacology ; Phosphorylation ; Repressor Proteins/metabolism ; SKP Cullin F-Box Protein Ligases/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism/physiology ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Transcription Factors/genetics/metabolism ; Ubiquitin-Protein Ligases/metabolism
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    Immunology. Decoding calcium signaling (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winslow, Monte M -- Crabtree, Gerald R -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):56-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunology Program, Stanford University, Stanford, CA 94305, USA〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637261" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium Channels/metabolism ; Calcium Channels, L-Type/genetics/*metabolism ; *Calcium Signaling ; Cation Transport Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Lymphocyte Activation ; Membrane Potentials ; Mice ; Models, Biological ; Mutation ; NFATC Transcription Factors ; Nuclear Proteins/metabolism ; Phosphorylation ; Potassium/metabolism ; Potassium Channels/metabolism ; Protein Subunits/metabolism ; Receptors, Antigen, T-Cell/metabolism ; T-Lymphocytes/*immunology/metabolism ; TRPM Cation Channels ; Transcription Factors/metabolism
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    An open letter to cancer researchers (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elledge, Stephen J -- Hannon, Gregory J -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):439-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239460" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/therapeutic use ; Biomarkers, Tumor ; Genes, Neoplasm ; Genetic Testing ; *Genome, Human ; Humans ; Mutation ; National Institutes of Health (U.S.) ; Neoplasms/drug therapy/*genetics/therapy ; Research Support as Topic ; *Sequence Analysis, DNA ; United States
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    The effects of artificial selection on the maize genome (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-28
    Description: Domestication promotes rapid phenotypic evolution through artificial selection. We investigated the genetic history by which the wild grass teosinte (Zea mays ssp. parviglumis) was domesticated into modern maize (Z. mays ssp. mays). Analysis of single-nucleotide polymorphisms in 774 genes indicates that 2 to 4% of these genes experienced artificial selection. The remaining genes retain evidence of a population bottleneck associated with domestication. Candidate selected genes with putative function in plant growth are clustered near quantitative trait loci that contribute to phenotypic differences between maize and teosinte. If we assume that our sample of genes is representative, approximately 1200 genes throughout the maize genome have been affected by artificial selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, Stephen I -- Bi, Irie Vroh -- Schroeder, Steve G -- Yamasaki, Masanori -- Doebley, John F -- McMullen, Michael D -- Gaut, Brandon S -- New York, N.Y. -- Science. 2005 May 27;308(5726):1310-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of California, Irvine, CA 92697, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919994" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/biosynthesis ; Biological Evolution ; Computer Simulation ; Genes, Plant ; Genetic Variation ; *Genome, Plant ; Inbreeding ; Likelihood Functions ; Linkage Disequilibrium ; Models, Genetic ; Mutation ; Phenotype ; *Polymorphism, Single Nucleotide ; Probability ; Quantitative Trait Loci ; Recombination, Genetic ; *Selection, Genetic ; Zea mays/*genetics/growth & development/metabolism
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    Requirement of voltage-gated calcium channel beta4 subunit for T lymphocyte functions (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: Calcium is known to play vital roles in diverse physiological processes, and it is known that voltage-gated calcium channels (Cav) mediate calcium influx in excitable cells. However, no consensus exists on the molecular identity of the calcium channels present in nonexcitable cells such as T lymphocytes. Here, we demonstrate that T lymphocytes express both regulatory beta4 and poreforming Cav1 alpha1 subunits of Cav channels. Cav beta4-mutant T lymphocytes fail to acquire normal functions and display impairment in the calcium response, activation of the transcription factor NFAT, and cytokine production. Although Cav1 channels of lymphocytes retain their voltage dependency, T cell receptor stimulation dramatically increases channel opening, providing a new mechanism for calcium entry in lymphocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Badou, Abdallah -- Basavappa, Srisaila -- Desai, Rooma -- Peng, You-Qing -- Matza, Didi -- Mehal, Wajahat Z -- Kaczmarek, Leonard K -- Boulpaep, Emile L -- Flavell, Richard A -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):117-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/*immunology/*metabolism ; Calcium/*metabolism ; Calcium Channels, L-Type/*metabolism ; *Calcium Signaling ; Cytokines/biosynthesis ; DNA-Binding Proteins/metabolism ; Ion Channel Gating ; Lymphocyte Activation ; Membrane Potentials ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mutation ; NFATC Transcription Factors ; Nuclear Proteins/metabolism ; Patch-Clamp Techniques ; Phosphorylation ; Protein Subunits/metabolism ; Receptors, Antigen, T-Cell/metabolism ; T-Lymphocytes/immunology/metabolism ; Transcription Factors/metabolism
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    Control of excitatory and inhibitory synapse formation by neuroligins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-01
    Description: The normal function of neural networks depends on a delicate balance between excitatory and inhibitory synaptic inputs. Synapse formation is thought to be regulated by bidirectional signaling between pre- and postsynaptic cells. We demonstrate that members of the Neuroligin family promote postsynaptic differentiation in cultured rat hippocampal neurons. Down-regulation of neuroligin isoform expression by RNA interference results in a loss of excitatory and inhibitory synapses. Electrophysiological analysis revealed a predominant reduction of inhibitory synaptic function. Thus, neuroligins control the formation and functional balance of excitatory and inhibitory synapses in hippocampal neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chih, Ben -- Engelman, Holly -- Scheiffele, Peter -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1324-8. Epub 2005 Jan 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Cellular Biophysics, Center for Neurobiology and Behavior, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681343" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Cell Adhesion Molecules, Neuronal ; Cell Line ; Cells, Cultured ; Dendrites/physiology/ultrastructure ; Down-Regulation ; Evoked Potentials ; Excitatory Postsynaptic Potentials ; Hippocampus/cytology ; Membrane Proteins/genetics/*metabolism ; Membrane Transport Proteins/metabolism ; Mutation ; Nerve Tissue Proteins/genetics/*metabolism ; Neural Inhibition ; Neurons/physiology ; Presynaptic Terminals/*physiology ; Protein Isoforms ; RNA Interference ; Rats ; Receptors, AMPA/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/*physiology ; Synaptic Membranes/*physiology ; Synaptic Transmission ; Transfection ; Vesicular Glutamate Transport Protein 1 ; Vesicular Inhibitory Amino Acid Transport Proteins
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    The biochemical architecture of an ancient adaptive landscape (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-10-22
    Description: Molecular evolution is moving from statistical descriptions of adaptive molecular changes toward predicting the fitness effects of mutations. Here, we characterize the fitness landscape of the six amino acids controlling coenzyme use in isopropylmalate dehydrogenase (IMDH). Although all natural IMDHs use nicotinamide adenine dinucleotide (NAD) as a coenzyme, they can be engineered to use nicotinamide adenine dinucleotide phosphate (NADP) instead. Intermediates between these two phenotypic extremes show that each amino acid contributes additively to enzyme function, with epistatic contributions confined to fitness. The genotype-phenotype-fitness map shows that NAD use is a global optimum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lunzer, Mark -- Miller, Stephen P -- Felsheim, Roderick -- Dean, Antony M -- GM060611/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):499-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BioTechnology Institute, Evolution and Behavior, University of Minnesota, St. Paul, MN 55108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239478" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Isopropylmalate Dehydrogenase/*chemistry/genetics/*metabolism ; Amino Acid Substitution ; Analysis of Variance ; Catalysis ; Epistasis, Genetic ; Escherichia coli/enzymology ; *Evolution, Molecular ; Genotype ; Kinetics ; Leucine/biosynthesis ; Mathematics ; Models, Chemical ; Mutation ; NAD/*metabolism ; NADP/*metabolism ; Oxidation-Reduction ; Phenotype ; Protein Engineering ; Selection, Genetic ; Thermodynamics
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    Genetics. Zebrafish researchers hook gene for human skin color (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1754-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357234" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; African Continental Ancestry Group/genetics ; Alanine/genetics ; Alleles ; Animals ; Antiporters/chemistry/*genetics/physiology ; Asian Continental Ancestry Group/genetics ; European Continental Ancestry Group/genetics ; Genes ; Genetic Variation ; Humans ; Mutation ; Selection, Genetic ; Skin Pigmentation/*genetics ; Threonine/genetics ; Zebrafish/*genetics ; Zebrafish Proteins/chemistry/*genetics/physiology
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    Retrograde signaling by Syt 4 induces presynaptic release and synapse-specific growth (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-08
    Description: The molecular pathways involved in retrograde signal transduction at synapses and the function of retrograde communication are poorly understood. Here, we demonstrate that postsynaptic calcium 2+ ion (Ca2+) influx through glutamate receptors and subsequent postsynaptic vesicle fusion trigger a robust induction of presynaptic miniature release after high-frequency stimulation at Drosophila neuromuscular junctions. An isoform of the synaptotagmin family, synaptotagmin 4 (Syt 4), serves as a postsynaptic Ca2+ sensor to release retrograde signals that stimulate enhanced presynaptic function through activation of the cyclic adenosine monophosphate (cAMP)-cAMP-dependent protein kinase pathway. Postsynaptic Ca2+ influx also stimulates local synaptic differentiation and growth through Syt 4-mediated retrograde signals in a synapse-specific manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshihara, Motojiro -- Adolfsen, Bill -- Galle, Kathleen T -- Littleton, J Troy -- R01 NS040296/NS/NINDS NIH HHS/ -- R01 NS040296-06/NS/NINDS NIH HHS/ -- R01 NS043244/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 4;310(5749):858-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Picower Institute for Learning and Memory, Department of Biology, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. motojiro@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16272123" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Calcium/metabolism ; Cell Differentiation/genetics/physiology ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Drosophila/embryology/growth & development/*physiology ; Egtazic Acid/analogs & derivatives/pharmacology ; Embryo, Nonmammalian/cytology/physiology ; Excitatory Postsynaptic Potentials ; Feedback, Physiological ; Models, Neurological ; Mutation ; Neuromuscular Junction/*physiology ; Neuronal Plasticity ; Presynaptic Terminals/physiology ; Receptors, Glutamate/metabolism ; *Signal Transduction ; Synapses/*physiology/ultrastructure ; Synaptic Membranes/physiology ; Synaptic Transmission ; Synaptic Vesicles/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Immunity, inflammation, and allergy in the gut (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: The gut immune system has the challenge of responding to pathogens while remaining relatively unresponsive to food antigens and the commensal microflora. In the developed world, this ability appears to be breaking down, with chronic inflammatory diseases of the gut commonplace in the apparent absence of overt infections. In both mouse and man, mutations in genes that control innate immune recognition, adaptive immunity, and epithelial permeability are all associated with gut inflammation. This suggests that perturbing homeostasis between gut antigens and host immunity represents a critical determinant in the development of gut inflammation and allergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macdonald, Thomas T -- Monteleone, Giovanni -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1920-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infection, Inflammation, and Repair, University of Southampton School of Medicine, Southampton General Hospital, Southampton, SO16 6YD, UK. t.t.macdonald@qmul.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790845" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Bacterial/immunology ; Bacteria/*immunology ; Bacterial Physiological Phenomena ; Celiac Disease/*immunology/pathology/physiopathology ; *Food Hypersensitivity ; Glutens/immunology ; Homeostasis ; Humans ; *Immunity, Mucosal ; Inflammatory Bowel Diseases/*immunology/pathology/physiopathology/therapy ; Intestinal Mucosa/*immunology/physiology ; Intestines/*immunology/microbiology/physiology ; Mutation ; Permeability ; T-Lymphocytes/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Nod2 mutation in Crohn's disease potentiates NF-kappaB activity and IL-1beta processing (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-05
    Description: Variants of NOD2, an intracellular sensor of bacteria-derived muramyl dipeptide (MDP), increase susceptibility to Crohn's disease (CD). These variants are thought to be defective in activation of nuclear factor kappaB (NF-kappaB) and antibacterial defenses, but CD clinical specimens display elevated NF-kappaB activity. To illuminate the pathophysiological function of NOD2, we introduced such a variant to the mouse Nod2 locus. Mutant mice exhibited elevated NF-kappaB activation in response to MDP and more efficient processing and secretion of the cytokine interleukin-1beta (IL-1beta). These effects are linked to increased susceptibility to bacterial-induced intestinal inflammation and identify NOD2 as a positive regulator of NF-kappaB activation and IL-1beta secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maeda, Shin -- Hsu, Li-Chung -- Liu, Hongjun -- Bankston, Laurie A -- Iimura, Mitsutoshi -- Kagnoff, Martin F -- Eckmann, Lars -- Karin, Michael -- AI43477/AI/NIAID NIH HHS/ -- AI56075/AI/NIAID NIH HHS/ -- DK07202/DK/NIDDK NIH HHS/ -- DK35108/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):734-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0723, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692052" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylmuramyl-Alanyl-Isoglutamine/immunology ; Animals ; Anti-Bacterial Agents/pharmacology ; Apoptosis ; Bacteria/immunology ; Cells, Cultured ; Colitis/immunology/pathology ; Colon/*immunology/microbiology ; Crohn Disease/genetics/*immunology ; Cytokines/biosynthesis/genetics ; Dextran Sulfate/pharmacology ; Interleukin-1/*metabolism ; Intestinal Mucosa/immunology ; Intracellular Signaling Peptides and Proteins/*genetics/*physiology ; Lipopolysaccharides/immunology ; Macrophage Activation ; Macrophages/*immunology/metabolism ; Mice ; Mutation ; NF-kappa B/*metabolism ; Nod2 Signaling Adaptor Protein ; Peptidoglycan/immunology ; Signal Transduction
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    NMR structure of Mistic, a membrane-integrating protein for membrane protein expression (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-26
    Description: Although structure determination of soluble proteins has become routine, our understanding of membrane proteins has been limited by experimental bottlenecks in obtaining both sufficient yields of protein and ordered crystals. Mistic is an unusual Bacillus subtilis integral membrane protein that folds autonomously into the membrane, bypassing the cellular translocon machinery. Using paramagnetic probes, we determined by nuclear magnetic resonance (NMR) spectroscopy that the protein forms a helical bundle with a surprisingly polar lipid-facing surface. Additional experiments suggest that Mistic can be used for high-level production of other membrane proteins in their native conformations, including many eukaryotic proteins that have previously been intractable to bacterial expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roosild, Tarmo P -- Greenwald, Jason -- Vega, Mark -- Castronovo, Samantha -- Riek, Roland -- Choe, Senyon -- GM056653/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1317-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Laboratory, Salk Institute, San Diego, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731457" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/*chemistry ; Bacterial Proteins/*chemistry/*metabolism ; Cell Membrane/chemistry ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli ; Hydrogen Bonding ; Lipid Bilayers ; Membrane Proteins/*chemistry/*metabolism ; Micelles ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Transforming Growth Factor beta/chemistry/metabolism ; Recombinant Proteins/chemistry/metabolism
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    Structural biology. Adaptation of SARS coronavirus to humans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, Kathryn V -- AI59578/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Colorado Health Sciences Center, Mail Stop 8333, Post Office Box 6211, Aurora, CO 80045, USA. kathryn.holmes@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166506" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Substitution ; Animals ; Binding Sites ; Carboxypeptidases/*chemistry/metabolism ; Disease Outbreaks ; Genes, Viral ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/*chemistry/genetics/metabolism ; Mutation ; Peptidyl-Dipeptidase A ; Protein Structure, Tertiary ; RNA, Viral/genetics ; Receptors, Virus/*chemistry/metabolism ; Recombination, Genetic ; SARS Virus/*chemistry/*genetics/physiology ; Severe Acute Respiratory Syndrome/epidemiology/prevention & control/*virology ; Species Specificity ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/*chemistry/genetics/metabolism ; Viral Vaccines ; Virus Replication ; Viverridae/virology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    GDF11 controls the timing of progenitor cell competence in developing retina (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-06-25
    Description: The orderly generation of cell types in the developing retina is thought to be regulated by changes in the competence of multipotent progenitors. Here, we show that a secreted factor, growth and differentiation factor 11 (GDF11), controls the numbers of retinal ganglion cells (RGCs), as well as amacrine and photoreceptor cells, that form during development. GDF11 does not affect proliferation of progenitors-a major mode of GDF11 action in other tissues-but instead controls duration of expression of Math5, a gene that confers competence for RGC genesis, in progenitor cells. Thus, GDF11 governs the temporal windows during which multipotent progenitors retain competence to produce distinct neural progeny.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Joon -- Wu, Hsiao-Huei -- Lander, Arthur D -- Lyons, Karen M -- Matzuk, Martin M -- Calof, Anne L -- AR44528/AR/NIAMS NIH HHS/ -- DC03583/DC/NIDCD NIH HHS/ -- HD32067/HD/NICHD NIH HHS/ -- HD38761/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1927-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, University of California, Irvine, CA 92697, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976303" target="_blank"〉PubMed〈/a〉
    Keywords: Amacrine Cells/*cytology ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Bone Morphogenetic Proteins/genetics/*physiology ; Cell Count ; Cell Differentiation ; Cell Proliferation ; DNA-Binding Proteins/genetics/metabolism ; Feedback, Physiological ; Gene Expression Regulation, Developmental ; Growth Differentiation Factors ; Mice ; Mice, Inbred C57BL ; Multipotent Stem Cells/cytology/*physiology ; Mutation ; Nerve Tissue Proteins/genetics/metabolism/physiology ; Retina/*cytology/*embryology ; Retinal Ganglion Cells/*cytology ; Retinal Rod Photoreceptor Cells/*cytology/embryology ; Transcription Factors/genetics/metabolism/physiology
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    tRNA actively shuttles between the nucleus and cytosol in yeast (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-21
    Description: Previous evidence suggested that transfer RNAs (tRNAs) cross the nuclear envelope to the cytosol only once after maturing in the nucleus. We now present evidence for nuclear import of tRNAs in yeast. Several export mutants accumulate mature tRNAs in the nucleus even in the absence of transcription. Import requires energy but not the Ran cycle. These results indicate that tRNAs shuttle between the nucleus and cytosol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takano, Akira -- Endo, Toshiya -- Yoshihisa, Tohru -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):140-2. Epub 2005 May 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Graduate School of Science, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905365" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Adenosine Triphosphate/metabolism ; Cell Nucleus/genetics/*metabolism ; Cytosol/*metabolism ; Introns ; Mutation ; RNA Precursors/metabolism ; RNA, Fungal/*metabolism ; RNA, Transfer/genetics/*metabolism ; RNA, Transfer, Amino Acid-Specific/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; RNA, Transfer, Ile/metabolism ; RNA, Transfer, Pro/metabolism ; RNA, Transfer, Tyr/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism ; Transcription, Genetic ; ran GTP-Binding Protein/metabolism
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    Cell biology. Wnt signaling glows with RNAi (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fearon, Eric R -- Cadigan, Ken M -- New York, N.Y. -- Science. 2005 May 6;308(5723):801-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA. fearon@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879199" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cytoskeletal Proteins/metabolism ; Drosophila Proteins/*metabolism ; Drosophila melanogaster/*genetics/metabolism ; *Gene Expression Regulation ; Genes, Insect ; Genes, Reporter ; *Genomics ; Intercellular Signaling Peptides and Proteins/metabolism ; Models, Biological ; Mutation ; Phosphorylation ; Proto-Oncogene Proteins/*metabolism ; *RNA Interference ; RNA, Double-Stranded/genetics/metabolism ; *Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors/genetics/metabolism ; Wings, Animal/metabolism ; Wnt Proteins ; Wnt1 Protein ; beta Catenin
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    An active role for tRNA in decoding beyond codon:anticodon pairing (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-21
    Description: During transfer RNA (tRNA) selection, a cognate codon:anticodon interaction triggers a series of events that ultimately results in the acceptance of that tRNA into the ribosome for peptide-bond formation. High-fidelity discrimination between the cognate tRNA and near- and noncognate ones depends both on their differential dissociation rates from the ribosome and on specific acceleration of forward rate constants by cognate species. Here we show that a mutant tRNA(Trp) carrying a single substitution in its D-arm achieves elevated levels of miscoding by accelerating these forward rate constants independent of codon:anticodon pairing in the decoding center. These data provide evidence for a direct role for tRNA in signaling its own acceptance during decoding and support its fundamental role during the evolution of protein synthesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1687177/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1687177/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochella, Luisa -- Green, Rachel -- R01 GM059425/GM/NIGMS NIH HHS/ -- R01GM059425/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 20;308(5725):1178-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905403" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Base Pairing ; Codon ; Codon, Terminator ; Dipeptides/biosynthesis ; GTP Phosphohydrolases/metabolism ; Guanosine Triphosphate/metabolism ; Hydrolysis ; Kinetics ; Mutation ; Nucleic Acid Conformation ; Peptide Elongation Factor Tu/metabolism ; *Protein Biosynthesis ; RNA, Messenger/metabolism ; RNA, Transfer, Trp/*chemistry/genetics/*metabolism ; Ribosomes/*metabolism
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    Developmental biology. Combing over the Polycomb group proteins (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-04-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):624-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860605" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/metabolism/ultrastructure ; DNA-Directed RNA Polymerases/metabolism ; Dosage Compensation, Genetic ; Drosophila/genetics ; Drosophila Proteins/chemistry/genetics/*physiology ; *Gene Expression Regulation, Developmental ; *Gene Silencing ; Histones/metabolism ; Humans ; Male ; Methylation ; Mutation ; Neoplasms/etiology/genetics ; Nucleosomes/ultrastructure ; Pluripotent Stem Cells/physiology ; Polycomb Repressive Complex 1 ; Polycomb-Group Proteins ; Prostatic Neoplasms/genetics/metabolism/pathology ; Proteins/genetics/metabolism ; Repressor Proteins/chemistry/genetics/*physiology ; Transcription, Genetic ; Ubiquitin/metabolism
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    Genetic factors in type 2 diabetes: the end of the beginning? (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-01-22
    Description: The intensive search for genetic variants that predispose to type 2 diabetes was launched with optimism, but progress has been slower than was hoped. Even so, major advances have been made in the understanding of monogenic forms of the disease which together represent a substantial health burden, and a few common gene variants that influence susceptibility have now been unequivocally identified. Armed with a better understanding of the tools needed to detect such genes, it seems inevitable that the rate of progress will increase and the relevance of genetic information to the diagnosis, treatment, and prevention of diabetes will become increasingly tangible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Rahilly, Stephen -- Barroso, Ines -- Wareham, Nicholas J -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Cambridge, Department of Clinical Biochemistry, Addenbrooke's Hospital, Cambridge CB2 2QQ, UK. so104@medschl.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662000" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Diabetes Mellitus, Type 2/diagnosis/*genetics/therapy ; Disease Models, Animal ; *Genetic Predisposition to Disease ; Genetic Techniques ; Genetic Variation ; Humans ; Life Style ; *Multifactorial Inheritance ; Mutation ; Risk Factors
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    A synaptonemal complex protein promotes homology-independent centromere coupling (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-10
    Description: We describe a process in meiotic cells of budding yeast in which chromosomes become joined together in pairs at their centromeres independent of chromosomal homology. These centromeric interactions depend on the synaptonemal complex component Zip1. During meiosis in wild-type diploids, centromere couples are initially nonhomologous and then undergo switching until all couples involve homologs. This transition to homologous coupling depends on Spo11, a protein required for the initiation of meiotic recombination. Regions of synaptonemal complex assembled early in meiosis are often centromere-associated. We propose that centromere coupling facilitates homolog pairing and promotes synapsis initiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsubouchi, Tomomi -- Roeder, G Shirleen -- GM28904/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 6;308(5723):870-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879219" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/genetics/metabolism ; Cell Nucleus/physiology ; Centromere/*physiology ; *Chromosome Pairing ; Chromosomes, Fungal/physiology ; Cytoskeletal Proteins/genetics/metabolism ; Endodeoxyribonucleases ; Esterases/genetics/metabolism ; Kinetochores ; *Meiosis ; Mutation ; Nuclear Proteins ; Recombination, Genetic ; Saccharomyces cerevisiae/genetics/*physiology ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Synaptonemal Complex/*physiology
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    MicroRNAs regulate brain morphogenesis in zebrafish (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-03-19
    Description: MicroRNAs (miRNAs) are small RNAs that regulate gene expression posttranscriptionally. To block all miRNA formation in zebrafish, we generated maternal-zygotic dicer (MZdicer) mutants that disrupt the Dicer ribonuclease III and double-stranded RNA-binding domains. Mutant embryos do not process precursor miRNAs into mature miRNAs, but injection of preprocessed miRNAs restores gene silencing, indicating that the disrupted domains are dispensable for later steps in silencing. MZdicer mutants undergo axis formation and differentiate multiple cell types but display abnormal morphogenesis during gastrulation, brain formation, somitogenesis, and heart development. Injection of miR-430 miRNAs rescues the brain defects in MZdicer mutants, revealing essential roles for miRNAs during morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giraldez, Antonio J -- Cinalli, Ryan M -- Glasner, Margaret E -- Enright, Anton J -- Thomson, J Michael -- Baskerville, Scott -- Hammond, Scott M -- Bartel, David P -- Schier, Alexander F -- New York, N.Y. -- Science. 2005 May 6;308(5723):833-8. Epub 2005 Mar 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Genetics Program, Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA. giraldez@saturn.med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774722" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; Brain/*embryology ; Cell Differentiation ; Central Nervous System/embryology ; Gastrula/physiology ; Gene Silencing ; Heart/embryology ; MicroRNAs/genetics/metabolism/*physiology ; *Morphogenesis ; Mutation ; Neurons/cytology ; Phenotype ; RNA Processing, Post-Transcriptional ; RNA, Double-Stranded/metabolism ; Ribonuclease III/genetics/metabolism ; Signal Transduction ; Somites/cytology/physiology ; Spinal Cord/embryology ; Zebrafish/*embryology/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular biology. A renewed focus on transfer RNA (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daviter, Tina -- Murphy, Frank V 4th -- Ramakrishnan, V -- New York, N.Y. -- Science. 2005 May 20;308(5725):1123-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905389" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Base Pairing ; Codon ; GTP Phosphohydrolases/metabolism ; Guanosine Triphosphate/metabolism ; Mutation ; Nucleic Acid Conformation ; Peptide Elongation Factor Tu/metabolism ; *Protein Biosynthesis ; RNA, Transfer/*chemistry/genetics/*metabolism ; RNA, Transfer, Amino Acyl/chemistry/metabolism ; Ribosomes/chemistry/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    Accurate multiplex polony sequencing of an evolved bacterial genome (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-06
    Description: We describe a DNA sequencing technology in which a commonly available, inexpensive epifluorescence microscope is converted to rapid nonelectrophoretic DNA sequencing automation. We apply this technology to resequence an evolved strain of Escherichia coli at less than one error per million consensus bases. A cell-free, mate-paired library provided single DNA molecules that were amplified in parallel to 1-micrometer beads by emulsion polymerase chain reaction. Millions of beads were immobilized in a polyacrylamide gel and subjected to automated cycles of sequencing by ligation and four-color imaging. Cost per base was roughly one-ninth as much as that of conventional sequencing. Our protocols were implemented with off-the-shelf instrumentation and reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shendure, Jay -- Porreca, Gregory J -- Reppas, Nikos B -- Lin, Xiaoxia -- McCutcheon, John P -- Rosenbaum, Abraham M -- Wang, Michael D -- Zhang, Kun -- Mitra, Robi D -- Church, George M -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1728-32. Epub 2005 Aug 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA. shendure@alumni.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16081699" target="_blank"〉PubMed〈/a〉
    Keywords: Acrylic Resins ; Algorithms ; Automation ; Costs and Cost Analysis ; DNA Ligases/metabolism ; DNA Primers ; DNA, Bacterial/*genetics ; Escherichia coli/*genetics ; *Evolution, Molecular ; Fluorescent Dyes ; Gels ; Gene Library ; *Genome, Bacterial ; Microscopy, Fluorescence ; Microspheres ; Mutation ; Nucleic Acid Hybridization ; Point Mutation ; Polymerase Chain Reaction ; Sequence Analysis, DNA/economics/instrumentation/*methods
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    Stomatal patterning and differentiation by synergistic interactions of receptor kinases (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-09
    Description: Coordinated spacing and patterning of stomata allow efficient gas exchange between plants and the atmosphere. Here we report that three ERECTA (ER)-family leucine-rich repeat-receptor-like kinases (LRR-RLKs) together control stomatal patterning, with specific family members regulating the specification of stomatal stem cell fate and the differentiation of guard cells. Loss-of-function mutations in all three ER-family genes cause stomatal clustering. Genetic interactions with a known stomatal patterning mutant too many mouths (tmm) revealed stoichiometric epistasis and combination-specific neomorphism. Our findings suggest that the negative regulation of ER-family RLKs by TMM, which is an LRR receptor-like protein, is critical for proper stomatal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shpak, Elena D -- McAbee, Jessica Messmer -- Pillitteri, Lynn Jo -- Torii, Keiko U -- New York, N.Y. -- Science. 2005 Jul 8;309(5732):290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16002616" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/*enzymology/genetics/growth & development ; Arabidopsis Proteins/genetics/*metabolism ; Cell Communication ; Cell Differentiation ; Cell Division ; Cell Lineage ; Epistasis, Genetic ; Gene Expression ; Genes, Plant ; Meristem/cytology ; Mutation ; Plant Epidermis/*cytology/enzymology/growth & development ; Plant Leaves/*cytology/enzymology/growth & development ; Promoter Regions, Genetic ; Protein Kinases/genetics/*metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Signal Transduction ; Stem Cells/cytology/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
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    Suppressing cancer: the importance of being senescent (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Campisi, Judith -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):886-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lawrence Berkeley National Laboratory, Life Sciences Division, 1 Cyclotron Road, Berkeley, CA 94720 and Buck Institute for Age Research, 8001 Redwood Boulevard, Novato, CA 94945, USA. jcampisi@lbl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16081723" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/genetics ; Animals ; Biomarkers ; Biomarkers, Tumor ; *Cell Aging/genetics/physiology ; DNA Damage ; Disease Models, Animal ; Genes, p53 ; Genes, ras ; Humans ; Lung Neoplasms/genetics ; Methyltransferases/genetics/physiology ; Mice ; Mutation ; *Neoplasms/genetics ; Proto-Oncogene Proteins B-raf/genetics ; Repressor Proteins/genetics/physiology ; Telomere
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  • 92
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    ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: The ataxia-telangiectasia mutated (ATM) kinase signals the presence of DNA double-strand breaks in mammalian cells by phosphorylating proteins that initiate cell-cycle arrest, apoptosis, and DNA repair. We show that the Mre11-Rad50-Nbs1 (MRN) complex acts as a double-strand break sensor for ATM and recruits ATM to broken DNA molecules. Inactive ATM dimers were activated in vitro with DNA in the presence of MRN, leading to phosphorylation of the downstream cellular targets p53 and Chk2. ATM autophosphorylation was not required for monomerization of ATM by MRN. The unwinding of DNA ends by MRN was essential for ATM stimulation, which is consistent with the central role of single-stranded DNA as an evolutionarily conserved signal for DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Ji-Hoon -- Paull, Tanya T -- CA094008/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):551-4. Epub 2005 Mar 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, 1 University Station, A4800, Austin, TX 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790808" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Cell Line ; DNA/chemistry/*metabolism ; *DNA Damage ; DNA Repair ; DNA Repair Enzymes/genetics/*metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; Enzyme Activation ; Humans ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Nucleic Acid Conformation ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Recombinant Proteins/metabolism ; Serine ; Signal Transduction ; Transfection ; Tumor Suppressor Proteins/chemistry/*metabolism
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  • 93
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    Mathematical modeling of planar cell polarity to understand domineering nonautonomy (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-22
    Description: Planar cell polarity (PCP) signaling generates subcellular asymmetry along an axis orthogonal to the epithelial apical-basal axis. Through a poorly understood mechanism, cell clones that have mutations in some PCP signaling components, including some, but not all, alleles of the receptor frizzled, cause polarity disruptions of neighboring wild-type cells, a phenomenon referred to as domineering nonautonomy. Here, a contact-dependent signaling hypothesis, derived from experimental results, is shown by reaction-diffusion, partial differential equation modeling and simulation to fully reproduce PCP phenotypes, including domineering nonautonomy, in the Drosophila wing. The sufficiency of this model and the experimental validation of model predictions reveal how specific protein-protein interactions produce autonomy or domineering nonautonomy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amonlirdviman, Keith -- Khare, Narmada A -- Tree, David R P -- Chen, Wei-Shen -- Axelrod, Jeffrey D -- Tomlin, Claire J -- R01-GM59823/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):423-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Aeronautics and Astronautics, Stanford University, Stanford, CA 94305-4035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662015" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Alleles ; Animals ; Cell Membrane/metabolism ; *Cell Polarity ; Diffusion ; Drosophila/*cytology/genetics/metabolism ; Drosophila Proteins/genetics/metabolism ; Feedback, Physiological ; Frizzled Receptors ; Mathematics ; Membrane Proteins/genetics/metabolism ; *Models, Biological ; Mutation ; Phenotype ; Phosphoproteins/genetics/metabolism ; Protein Binding ; Receptors, G-Protein-Coupled ; *Signal Transduction ; Wings, Animal/*cytology/metabolism
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    Optimization of virulence functions through glucosylation of Shigella LPS (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-26
    Description: Shigella, the leading cause of bacillary dysentery, uses a type III secretion system (TTSS) to inject proteins into human cells, leading to bacterial invasion and a vigorous inflammatory response. The bacterium is protected against the response by the O antigen of lipopolysaccharide (LPS) on its surface. We show that bacteriophage-encoded glucosylation of Shigella O antigen, the basis of different serotypes, shortens the LPS molecule by around half. This enhances TTSS function without compromising the protective properties of the LPS. Thus, LPS glucosylation promotes bacterial invasion and evasion of innate immunity, which may have contributed to the emergence of serotype diversity in Shigella.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉West, Nicholas P -- Sansonetti, Philippe -- Mounier, Joelle -- Exley, Rachel M -- Parsot, Claude -- Guadagnini, Stephanie -- Prevost, Marie-Christine -- Prochnicka-Chalufour, Ada -- Delepierre, Muriel -- Tanguy, Myriam -- Tang, Christoph M -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1313-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Molecular Microbiology and Infection, Department of Infectious Diseases, Faculty of Medicine, Flowers Building, Imperial College London, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731456" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Adhesion ; Bacteriophages/genetics ; Carbohydrate Conformation ; Dysentery, Bacillary/immunology/*microbiology/pathology ; Glucose/*metabolism ; Glycosylation ; Hydrophobic and Hydrophilic Interactions ; Immunity, Innate ; Intestinal Mucosa/microbiology/pathology ; Lipopolysaccharides/chemistry/*metabolism ; Microscopy, Electron, Scanning ; Microscopy, Electron, Transmission ; Mutation ; Neutrophils ; O Antigens/chemistry/*metabolism ; Operon ; Rabbits ; Serotyping ; Shigella flexneri/classification/metabolism/*pathogenicity/ultrastructure ; Virulence
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  • 95
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    Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pufall, Miles A -- Lee, Gregory M -- Nelson, Mary L -- Kang, Hyun-Seo -- Velyvis, Algirdas -- Kay, Lewis E -- McIntosh, Lawrence P -- Graves, Barbara J -- GM08537/GM/NIGMS NIH HHS/ -- P01-CA24014/CA/NCI NIH HHS/ -- R01 GM38663/GM/NIGMS NIH HHS/ -- T32-CA93247/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):142-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Huntsman Cancer Institute, Department of Oncological Sciences, University of Utah, Salt Lake City, UT 84112-5550, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994560" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; DNA/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/*chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-ets ; Signal Transduction ; Transcription Factors/*chemistry/genetics/*metabolism
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    Immunology. Close to the edge: neutralizing the HIV-1 envelope (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nabel, Gary J -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1878-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center (VRC), National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. gnabel@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976295" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/therapeutic use ; Animals ; Antibodies, Monoclonal/immunology/therapeutic use ; Antibody Specificity ; Autoantigens/immunology ; Autoimmune Diseases/immunology ; Cardiolipins/*immunology ; Complementarity Determining Regions ; Epitopes ; Gene Products, env/chemistry/*immunology ; HIV Antibodies/chemistry/genetics/*immunology/therapeutic use ; HIV Envelope Protein gp41/chemistry/*immunology ; HIV Infections/*immunology/prevention & control/therapy ; HIV-1/*immunology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Immunization, Passive ; Models, Molecular ; Mutation ; Neutralization Tests ; Protein Structure, Tertiary
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    Bats are natural reservoirs of SARS-like coronaviruses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: Severe acute respiratory syndrome (SARS) emerged in 2002 to 2003 in southern China. The origin of its etiological agent, the SARS coronavirus (SARS-CoV), remains elusive. Here we report that species of bats are a natural host of coronaviruses closely related to those responsible for the SARS outbreak. These viruses, termed SARS-like coronaviruses (SL-CoVs), display greater genetic variation than SARS-CoV isolated from humans or from civets. The human and civet isolates of SARS-CoV nestle phylogenetically within the spectrum of SL-CoVs, indicating that the virus responsible for the SARS outbreak was a member of this coronavirus group.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Wendong -- Shi, Zhengli -- Yu, Meng -- Ren, Wuze -- Smith, Craig -- Epstein, Jonathan H -- Wang, Hanzhong -- Crameri, Gary -- Hu, Zhihong -- Zhang, Huajun -- Zhang, Jianhong -- McEachern, Jennifer -- Field, Hume -- Daszak, Peter -- Eaton, Bryan T -- Zhang, Shuyi -- Wang, Lin-Fa -- R01-TW05869/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):676-9. Epub 2005 Sep 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Zoology, Chinese Academy of Sciences (CAS), Beijing, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195424" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cercopithecus aethiops ; China/epidemiology ; Chiroptera/*virology ; Communicable Diseases, Emerging ; *Coronavirus/classification ; Disease Outbreaks ; *Disease Reservoirs ; Genetic Variation ; Genome, Viral ; Henipavirus/classification ; Humans ; Molecular Sequence Data ; Mutation ; Phylogeny ; Polymerase Chain Reaction ; *SARS Virus/classification ; Sequence Analysis, DNA ; Severe Acute Respiratory Syndrome/epidemiology/transmission/virology ; Vero Cells ; Viverridae/virology
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    Comparative genomics of trypanosomatid parasitic protozoa (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: A comparison of gene content and genome architecture of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major, three related pathogens with different life cycles and disease pathology, revealed a conserved core proteome of about 6200 genes in large syntenic polycistronic gene clusters. Many species-specific genes, especially large surface antigen families, occur at nonsyntenic chromosome-internal and subtelomeric regions. Retroelements, structural RNAs, and gene family expansion are often associated with syntenic discontinuities that-along with gene divergence, acquisition and loss, and rearrangement within the syntenic regions-have shaped the genomes of each parasite. Contrary to recent reports, our analyses reveal no evidence that these species are descended from an ancestor that contained a photosynthetic endosymbiont.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉El-Sayed, Najib M -- Myler, Peter J -- Blandin, Gaelle -- Berriman, Matthew -- Crabtree, Jonathan -- Aggarwal, Gautam -- Caler, Elisabet -- Renauld, Hubert -- Worthey, Elizabeth A -- Hertz-Fowler, Christiane -- Ghedin, Elodie -- Peacock, Christopher -- Bartholomeu, Daniella C -- Haas, Brian J -- Tran, Anh-Nhi -- Wortman, Jennifer R -- Alsmark, U Cecilia M -- Angiuoli, Samuel -- Anupama, Atashi -- Badger, Jonathan -- Bringaud, Frederic -- Cadag, Eithon -- Carlton, Jane M -- Cerqueira, Gustavo C -- Creasy, Todd -- Delcher, Arthur L -- Djikeng, Appolinaire -- Embley, T Martin -- Hauser, Christopher -- Ivens, Alasdair C -- Kummerfeld, Sarah K -- Pereira-Leal, Jose B -- Nilsson, Daniel -- Peterson, Jeremy -- Salzberg, Steven L -- Shallom, Joshua -- Silva, Joana C -- Sundaram, Jaideep -- Westenberger, Scott -- White, Owen -- Melville, Sara E -- Donelson, John E -- Andersson, Bjorn -- Stuart, Kenneth D -- Hall, Neil -- AI045039/AI/NIAID NIH HHS/ -- AI45038/AI/NIAID NIH HHS/ -- AI45061/AI/NIAID NIH HHS/ -- R01 AI043062/AI/NIAID NIH HHS/ -- U01 AI040599/AI/NIAID NIH HHS/ -- U01 AI043062/AI/NIAID NIH HHS/ -- U01 AI045038/AI/NIAID NIH HHS/ -- U01 AI045039/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):404-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA. nelsayed@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020724" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chromosomes/genetics ; Evolution, Molecular ; Gene Transfer, Horizontal ; Genes, Protozoan ; *Genome, Protozoan ; Genomics ; Leishmania major/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Mutation ; Phylogeny ; Plastids/genetics ; *Proteome ; Protozoan Proteins/chemistry/*genetics/physiology ; Recombination, Genetic ; Retroelements ; Species Specificity ; Symbiosis ; Synteny ; Telomere/genetics ; Trypanosoma brucei brucei/chemistry/*genetics/metabolism ; Trypanosoma cruzi/chemistry/*genetics/metabolism
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    BZR1 is a transcriptional repressor with dual roles in brassinosteroid homeostasis and growth responses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-01
    Description: Brassinosteroid (BR) homeostasis and signaling are crucial for normal growth and development of plants. BR signaling through cell-surface receptor kinases and intracellular components leads to dephosphorylation and accumulation of the nuclear protein BZR1. How BR signaling regulates gene expression, however, remains unknown. Here we show that BZR1 is a transcriptional repressor that has a previously unknown DNA binding domain and binds directly to the promoters of feedback-regulated BR biosynthetic genes. Microarray analyses identified additional potential targets of BZR1 and illustrated, together with physiological studies, that BZR1 coordinates BR homeostasis and signaling by playing dual roles in regulating BR biosynthesis and downstream growth responses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2925132/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2925132/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Jun-Xian -- Gendron, Joshua M -- Sun, Yu -- Gampala, Srinivas S L -- Gendron, Nathan -- Sun, Catherine Qing -- Wang, Zhi-Yong -- 5T32GM007276/GM/NIGMS NIH HHS/ -- R01 GM066258/GM/NIGMS NIH HHS/ -- R01 GM066258-04/GM/NIGMS NIH HHS/ -- R01 GM66258-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1634-8. Epub 2005 Jan 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681342" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/growth & development/physiology ; Arabidopsis Proteins/genetics/*metabolism ; Base Sequence ; Binding Sites ; Chromatin Immunoprecipitation ; DNA-Binding Proteins/genetics/*metabolism ; Feedback, Physiological ; *Gene Expression Regulation, Plant ; Genes, Plant ; Genes, Reporter ; Homeostasis ; Light ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Plant Growth Regulators/biosynthesis/*metabolism/pharmacology ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/metabolism ; *Signal Transduction ; Steroids/biosynthesis/*metabolism/pharmacology ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    Complete replication of hepatitis C virus in cell culture (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-11
    Description: Many aspects of the hepatitis C virus (HCV) life cycle have not been reproduced in cell culture, which has slowed research progress on this important human pathogen. Here, we describe a full-length HCV genome that replicates and produces virus particles that are infectious in cell culture (HCVcc). Replication of HCVcc was robust, producing nearly 10(5) infectious units per milliliter within 48 hours. Virus particles were filterable and neutralized with a monoclonal antibody against the viral glycoprotein E2. Viral entry was dependent on cellular expression of a putative HCV receptor, CD81. HCVcc replication was inhibited by interferon-alpha and by several HCV-specific antiviral compounds, suggesting that this in vitro system will aid in the search for improved antivirals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lindenbach, Brett D -- Evans, Matthew J -- Syder, Andrew J -- Wolk, Benno -- Tellinghuisen, Timothy L -- Liu, Christopher C -- Maruyama, Toshiaki -- Hynes, Richard O -- Burton, Dennis R -- McKeating, Jane A -- Rice, Charles M -- AI40034/AI/NIAID NIH HHS/ -- AI50798/AI/NIAID NIH HHS/ -- AI51820/AI/NIAID NIH HHS/ -- CA10702/CA/NCI NIH HHS/ -- CA57973/CA/NCI NIH HHS/ -- CA85883/CA/NCI NIH HHS/ -- DK70497/DK/NIDDK NIH HHS/ -- G0400802/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):623-6. Epub 2005 Jun 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for the Study of Hepatitis C, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947137" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology ; Antibodies, Viral/immunology ; Antigens, CD/metabolism ; Antigens, CD81 ; Antiviral Agents/pharmacology ; Cell Line, Tumor ; Centrifugation, Density Gradient ; Culture Media, Conditioned ; Genome, Viral ; Hepacivirus/genetics/immunology/*physiology ; Humans ; Interferon-alpha/pharmacology ; Mutation ; Neutralization Tests ; RNA, Viral/biosynthesis ; Replicon ; Serial Passage ; Transfection ; Viral Envelope Proteins/analysis/biosynthesis ; Viral Nonstructural Proteins/analysis/biosynthesis ; Virion/physiology ; *Virus Cultivation ; *Virus Replication
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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