ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Molecular Sequence Data  (59)
  • 2000-2004  (59)
  • 2001  (59)
  • 1
    facet.materialart.
    Unknown
    The genome of the natural genetic engineer Agrobacterium tumefaciens C58 (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: The 5.67-megabase genome of the plant pathogen Agrobacterium tumefaciens C58 consists of a circular chromosome, a linear chromosome, and two plasmids. Extensive orthology and nucleotide colinearity between the genomes of A. tumefaciens and the plant symbiont Sinorhizobium meliloti suggest a recent evolutionary divergence. Their similarities include metabolic, transport, and regulatory systems that promote survival in the highly competitive rhizosphere; differences are apparent in their genome structure and virulence gene complement. Availability of the A. tumefaciens sequence will facilitate investigations into the molecular basis of pathogenesis and the evolutionary divergence of pathogenic and symbiotic lifestyles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wood, D W -- Setubal, J C -- Kaul, R -- Monks, D E -- Kitajima, J P -- Okura, V K -- Zhou, Y -- Chen, L -- Wood, G E -- Almeida, N F Jr -- Woo, L -- Chen, Y -- Paulsen, I T -- Eisen, J A -- Karp, P D -- Bovee, D Sr -- Chapman, P -- Clendenning, J -- Deatherage, G -- Gillet, W -- Grant, C -- Kutyavin, T -- Levy, R -- Li, M J -- McClelland, E -- Palmieri, A -- Raymond, C -- Rouse, G -- Saenphimmachak, C -- Wu, Z -- Romero, P -- Gordon, D -- Zhang, S -- Yoo, H -- Tao, Y -- Biddle, P -- Jung, M -- Krespan, W -- Perry, M -- Gordon-Kamm, B -- Liao, L -- Kim, S -- Hendrick, C -- Zhao, Z Y -- Dolan, M -- Chumley, F -- Tingey, S V -- Tomb, J F -- Gordon, M P -- Olson, M V -- Nester, E W -- GM19642/GM/NIGMS NIH HHS/ -- GM32618/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2317-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Washington, 1959 NE Pacific Street, Box 357242, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743193" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/classification/*genetics/pathogenicity/physiology ; Bacterial Adhesion/genetics ; Bacterial Proteins/genetics/metabolism ; Carrier Proteins/genetics/metabolism ; Chromosomes, Bacterial/genetics ; Conjugation, Genetic ; DNA Replication ; Genes, Bacterial ; Genes, Regulator ; *Genome, Bacterial ; Membrane Proteins/genetics/metabolism ; Molecular Sequence Data ; Phylogeny ; Plants/microbiology ; Plasmids ; Replicon ; Rhizobiaceae/genetics/physiology ; *Sequence Analysis, DNA ; Sinorhizobium meliloti/genetics/physiology ; Symbiosis ; Virulence/genetics
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Biogeography and ecological setting of Indian Ocean hydrothermal vents (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-15
    Description: Within the endemic invertebrate faunas of hydrothermal vents, five biogeographic provinces are recognized. Invertebrates at two Indian Ocean vent fields (Kairei and Edmond) belong to a sixth province, despite ecological settings and invertebrate-bacterial symbioses similar to those of both western Pacific and Atlantic vents. Most organisms found at these Indian Ocean vent fields have evolutionary affinities with western Pacific vent faunas, but a shrimp that ecologically dominates Indian Ocean vents closely resembles its Mid-Atlantic counterpart. These findings contribute to a global assessment of the biogeography of chemosynthetic faunas and indicate that the Indian Ocean vent community follows asymmetric assembly rules biased toward Pacific evolutionary alliances.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Dover, C L -- Humphris, S E -- Fornari, D -- Cavanaugh, C M -- Collier, R -- Goffredi, S K -- Hashimoto, J -- Lilley, M D -- Reysenbach, A L -- Shank, T M -- Von Damm, K L -- Banta, A -- Gallant, R M -- Gotz, D -- Green, D -- Hall, J -- Harmer, T L -- Hurtado, L A -- Johnson, P -- McKiness, Z P -- Meredith, C -- Olson, E -- Pan, I L -- Turnipseed, M -- Won, Y -- Young, C R 3rd -- Vrijenhoek, R C -- New York, N.Y. -- Science. 2001 Oct 26;294(5543):818-23. Epub 2001 Sep 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, College of William & Mary, Williamsburg, VA 23187, USA. cindy_vandover@wm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11557843" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/classification/isolation & purification ; *Bacterial Physiological Phenomena ; Biological Evolution ; Biomass ; Decapoda (Crustacea)/classification/physiology ; *Ecosystem ; Euryarchaeota/classification/isolation & purification/physiology ; Geography ; *Geologic Sediments/microbiology ; Hot Temperature ; Invertebrates/classification/microbiology/*physiology ; Molecular Sequence Data ; Mollusca/classification/physiology ; Oceans and Seas ; Seawater ; Symbiosis
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    A transcriptional switch mediated by cofactor methylation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-10
    Description: We describe a molecular switch based on the controlled methylation of nucleosome and the transcriptional cofactors, the CREB-binding proteins (CBP)/p300. The CBP/p300 methylation site is localized to an arginine residue that is essential for stabilizing the structure of the KIX domain, which mediates CREB recruitment. Methylation of KIX by coactivator-associated arginine methyltransferase 1 (CARM1) blocks CREB activation by disabling the interaction between KIX and the kinase inducible domain (KID) of CREB. Thus, CARM1 functions as a corepressor in cyclic adenosine monophosphate signaling pathway via its methyltransferase activity while acting as a coactivator for nuclear hormones. These results provide strong in vivo and in vitro evidence that histone methylation plays a key role in hormone-induced gene activation and define cofactor methylation as a new regulatory mechanism in hormone signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, W -- Chen, H -- Du, K -- Asahara, H -- Tini, M -- Emerson, B M -- Montminy, M -- Evans, R M -- 9R01DK57978/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Department of Biological Chemistry, University of California Davis Cancer Center/Basic Science, Sacramento, CA 95817, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701890" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Apoptosis ; Cell Line ; Cyclic AMP Response Element-Binding Protein/metabolism ; Dimerization ; E1A-Associated p300 Protein ; *Gene Expression Regulation ; Genes, Reporter ; Histone Acetyltransferases ; Histones/metabolism ; Methylation ; Molecular Sequence Data ; Nerve Growth Factor/pharmacology ; Nuclear Proteins/chemistry/*metabolism ; PC12 Cells ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/*metabolism ; Rats ; Receptors, Retinoic Acid/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Somatostatin/genetics ; Trans-Activators/chemistry/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Transfection ; Tretinoin/metabolism/pharmacology
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58 (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: Agrobacterium tumefaciens is a plant pathogen capable of transferring a defined segment of DNA to a host plant, generating a gall tumor. Replacing the transferred tumor-inducing genes with exogenous DNA allows the introduction of any desired gene into the plant. Thus, A. tumefaciens has been critical for the development of modern plant genetics and agricultural biotechnology. Here we describe the genome of A. tumefaciens strain C58, which has an unusual structure consisting of one circular and one linear chromosome. We discuss genome architecture and evolution and additional genes potentially involved in virulence and metabolic parasitism of host plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodner, B -- Hinkle, G -- Gattung, S -- Miller, N -- Blanchard, M -- Qurollo, B -- Goldman, B S -- Cao, Y -- Askenazi, M -- Halling, C -- Mullin, L -- Houmiel, K -- Gordon, J -- Vaudin, M -- Iartchouk, O -- Epp, A -- Liu, F -- Wollam, C -- Allinger, M -- Doughty, D -- Scott, C -- Lappas, C -- Markelz, B -- Flanagan, C -- Crowell, C -- Gurson, J -- Lomo, C -- Sear, C -- Strub, G -- Cielo, C -- Slater, S -- R15 GM61690-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2323-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Hiram College, Hiram, OH 44234, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743194" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/classification/*genetics/pathogenicity/physiology ; Bacterial Proteins/chemistry/genetics/metabolism ; Carrier Proteins/chemistry/genetics/metabolism ; Cell Cycle ; Chromosomes, Bacterial/genetics ; DNA Replication ; Genes, Bacterial ; *Genome, Bacterial ; Molecular Sequence Data ; Phylogeny ; Plant Tumors/microbiology ; Plants/microbiology ; Plasmids ; Replicon ; Rhizobiaceae/genetics ; *Sequence Analysis, DNA ; Signal Transduction ; Sinorhizobium meliloti/genetics ; Synteny ; Telomere ; Virulence/genetics
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    A sperm cytoskeletal protein that signals oocyte meiotic maturation and ovulation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-17
    Description: Caenorhabditis elegans oocytes, like those of most animals, arrest during meiotic prophase. Sperm promote the resumption of meiosis (maturation) and contraction of smooth muscle-like gonadal sheath cells, which are required for ovulation. We show that the major sperm cytoskeletal protein (MSP) is a bipartite signal for oocyte maturation and sheath contraction. MSP also functions in sperm locomotion, playing a role analogous to actin. Thus, during evolution, MSP has acquired extracellular signaling and intracellular cytoskeletal functions for reproduction. Proteins with MSP-like domains are found in plants, fungi, and other animals, suggesting that related signaling functions may exist in other phyla.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, M A -- Nguyen, V Q -- Lee, M H -- Kosinski, M -- Schedl, T -- Caprioli, R M -- Greenstein, D -- CA09592/CA/NCI NIH HHS/ -- GM57173/GM/NIGMS NIH HHS/ -- GM58008/GM/NIGMS NIH HHS/ -- HD07043/HD/NICHD NIH HHS/ -- HD25614/HD/NICHD NIH HHS/ -- R01 GM057173/GM/NIGMS NIH HHS/ -- R01 HD025614/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 16;291(5511):2144-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11251118" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/*physiology ; Carrier Proteins/chemistry/physiology ; Cytoskeleton/chemistry/physiology ; Disorders of Sex Development ; Enzyme Activation ; Evolution, Molecular ; Female ; Gonads/cytology/physiology ; Helminth Proteins/chemistry/immunology/pharmacology/*physiology ; MAP Kinase Signaling System ; Male ; *Meiosis ; Membrane Proteins/chemistry/physiology ; Microinjections ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; Oocytes/*physiology ; Ovulation ; Phylogeny ; Protein Folding ; Protein Structure, Tertiary ; Pseudopodia/physiology ; Recombinant Proteins/pharmacology ; Signal Transduction ; Sperm Motility ; Spermatozoa/chemistry/*physiology
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    facet.materialart.
    Unknown
    HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-09
    Description: HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). We found that human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. Because proline hydroxylation requires molecular oxygen and Fe(2+), this protein modification may play a key role in mammalian oxygen sensing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivan, M -- Kondo, K -- Yang, H -- Kim, W -- Valiando, J -- Ohh, M -- Salic, A -- Asara, J M -- Lane, W S -- Kaelin , W G Jr -- New York, N.Y. -- Science. 2001 Apr 20;292(5516):464-8. Epub 2001 Apr 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Brigham and Women's Hospital, Howard Hughes Medical Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292862" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Cell Hypoxia ; Cell Line ; Cobalt/pharmacology ; Deferoxamine/pharmacology ; Humans ; Hydroxylation ; Hydroxyproline/*metabolism ; *Ligases ; Mass Spectrometry ; Mice ; Molecular Sequence Data ; Oxygen/*physiology ; Protein Structure, Tertiary ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/*metabolism ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; Von Hippel-Lindau Tumor Suppressor Protein
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    Human hypertension caused by mutations in WNK kinases (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-11
    Description: Hypertension is a major public health problem of largely unknown cause. Here, we identify two genes causing pseudohypoaldosteronism type II, a Mendelian trait featuring hypertension, increased renal salt reabsorption, and impaired K+ and H+ excretion. Both genes encode members of the WNK family of serine-threonine kinases. Disease-causing mutations in WNK1 are large intronic deletions that increase WNK1 expression. The mutations in WNK4 are missense, which cluster in a short, highly conserved segment of the encoded protein. Both proteins localize to the distal nephron, a kidney segment involved in salt, K+, and pH homeostasis. WNK1 is cytoplasmic, whereas WNK4 localizes to tight junctions. The WNK kinases and their associated signaling pathway(s) may offer new targets for the development of antihypertensive drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, F H -- Disse-Nicodeme, S -- Choate, K A -- Ishikawa, K -- Nelson-Williams, C -- Desitter, I -- Gunel, M -- Milford, D V -- Lipkin, G W -- Achard, J M -- Feely, M P -- Dussol, B -- Berland, Y -- Unwin, R J -- Mayan, H -- Simon, D B -- Farfel, Z -- Jeunemaitre, X -- Lifton, R P -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1107-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute; Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06510 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498583" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 12/genetics ; Chromosomes, Human, Pair 17/genetics ; Cytoplasm/enzymology ; Female ; Gene Expression Regulation, Enzymologic ; Genetic Linkage ; Humans ; Hypertension/enzymology/*genetics/physiopathology ; Intercellular Junctions/enzymology ; Intracellular Signaling Peptides and Proteins ; Introns ; Kidney Tubules, Collecting/enzymology/ultrastructure ; Kidney Tubules, Distal/enzymology/ultrastructure ; Male ; Membrane Proteins/metabolism ; Microscopy, Fluorescence ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Pedigree ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Pseudohypoaldosteronism/enzymology/*genetics/physiopathology ; Sequence Deletion ; Signal Transduction ; Zonula Occludens-1 Protein
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 8
    facet.materialart.
    Unknown
    Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-09
    Description: Hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. Here we show that the interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by an enzyme we have termed HIF-alpha prolyl-hydroxylase (HIF-PH). An absolute requirement for dioxygen as a cosubstrate and iron as cofactor suggests that HIF-PH functions directly as a cellular oxygen sensor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaakkola, P -- Mole, D R -- Tian, Y M -- Wilson, M I -- Gielbert, J -- Gaskell, S J -- von Kriegsheim, A -- Hebestreit, H F -- Mukherji, M -- Schofield, C J -- Maxwell, P H -- Pugh, C W -- Ratcliffe, P J -- New York, N.Y. -- Science. 2001 Apr 20;292(5516):468-72. Epub 2001 Apr 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Henry Wellcome Building of Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292861" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ascorbic Acid/pharmacology ; Cell Hypoxia ; DNA-Binding Proteins/chemistry/*metabolism ; Deferoxamine/pharmacology ; Ferrous Compounds/pharmacology ; Humans ; Hydroxylation ; Hydroxyproline/*metabolism ; Hypoxia-Inducible Factor 1 ; Hypoxia-Inducible Factor 1, alpha Subunit ; *Ligases ; Molecular Sequence Data ; Nuclear Proteins/chemistry/*metabolism ; Oxygen/*physiology ; Point Mutation ; Procollagen-Proline Dioxygenase/antagonists & inhibitors/*metabolism ; Protein Structure, Tertiary ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Transcription Factors/chemistry/*metabolism ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; Von Hippel-Lindau Tumor Suppressor Protein
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    Global analysis of protein activities using proteome chips (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-28
    Description: To facilitate studies of the yeast proteome, we cloned 5800 open reading frames and overexpressed and purified their corresponding proteins. The proteins were printed onto slides at high spatial density to form a yeast proteome microarray and screened for their ability to interact with proteins and phospholipids. We identified many new calmodulin- and phospholipid-interacting proteins; a common potential binding motif was identified for many of the calmodulin-binding proteins. Thus, microarrays of an entire eukaryotic proteome can be prepared and screened for diverse biochemical activities. The microarrays can also be used to screen protein-drug interactions and to detect posttranslational modifications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, H -- Bilgin, M -- Bangham, R -- Hall, D -- Casamayor, A -- Bertone, P -- Lan, N -- Jansen, R -- Bidlingmaier, S -- Houfek, T -- Mitchell, T -- Miller, P -- Dean, R A -- Gerstein, M -- Snyder, M -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2101-5. Epub 2001 Jul 26.〈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/11474067" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Calmodulin/metabolism ; Calmodulin-Binding Proteins/metabolism ; Cell Membrane/metabolism ; Cloning, Molecular ; Fungal Proteins/chemistry/genetics/*metabolism ; Glucose/metabolism ; Liposomes/metabolism ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Open Reading Frames ; Peptide Library ; Phosphatidylcholines/metabolism ; Phosphatidylinositols/metabolism ; Phospholipids/metabolism ; Protein Binding ; *Proteome ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Signal Transduction ; Streptavidin/metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-28
    Description: Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin. Like some syntaxins, Ykt6p adopted a folded back conformation in which Ykt6pN bound to its COOH-terminal core domain. The NH2-terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tochio, H -- Tsui, M M -- Banfield, D K -- Zhang, M -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):698-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Carrier Proteins/*chemistry/metabolism ; *Contractile Proteins ; Membrane Proteins/*chemistry/metabolism ; Microfilament Proteins/chemistry ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis ; Nuclear Magnetic Resonance, Biomolecular ; Profilins ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Qa-SNARE Proteins ; Qc-SNARE Proteins ; R-SNARE Proteins ; Recombinant Fusion Proteins/chemistry/metabolism ; SNARE Proteins ; *Saccharomyces cerevisiae Proteins ; *Vesicular Transport Proteins
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...