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  • Amino Acid Sequence  (2)
  • Cell Differentiation  (2)
  • Gene Expression Regulation  (2)
  • American Association for the Advancement of Science (AAAS)  (6)
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  • American Association for the Advancement of Science (AAAS)  (6)
  • 1
    Publication Date: 2002-08-24
    Description: Polyketide synthases (PKSs) assemble the polyketide carbon backbone by sequential decarboxylative condensation of acyl coenzyme A (CoA) precursors, and the C-C bond-forming step in this process is catalyzed by the beta-ketoacyl synthase (KS) domain or subunit. Genetic and biochemical characterization of the nonactin biosynthesis gene cluster from Streptomyces griseus revealed two KSs, NonJ and NonK, that are highly homologous to known KSs but catalyze sequential condensation of the acyl CoA substrates by forming C-O rather than C-C bonds. This chemistry can be used in PKS engineering to increase the scope and diversity of polyketide biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwon, Hyung-Jin -- Smith, Wyatt C -- Scharon, A Janelle -- Hwang, Sung Hee -- Kurth, Mark J -- Shen, Ben -- AI51689/AI/NIAID NIH HHS/ -- T32 GM08505/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1327-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Pharmaceutical Sciences and, Department of Chemistry, University of Wisconsin, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193782" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*chemistry/*metabolism ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalysis ; Chromatography, High Pressure Liquid ; Genes, Bacterial ; Macrolides/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/*metabolism ; Multigene Family ; Mutation ; Protein Engineering ; Protein Subunits ; Sequence Alignment ; Spectrometry, Mass, Electrospray Ionization ; Streptomyces/genetics ; Streptomyces griseus/*enzymology/genetics ; Transformation, Bacterial
    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
    Publication Date: 1989-04-28
    Description: Mice transgenic for a hybrid gene containing the liver promoter of the mouse amylase gene (Amy-1a) fused to the SV40 tumor antigen coding region unexpected developed malignant brown adipose tissue tumors (malignant hibernomas). Expression of the alpha-amylase gene had previously been thought to be confined to the liver parotid, and pancreas; however, analysis of white and brown adipose tissue from nontransgenic mice revealed expression of the endogenous Amy-1a gene in these tissues. Gene constructs driven by the Amy-1a liver promoter thus provide a means of targeting gene expression to the adipocyte cell lineage in transgenic mice. Moreover the high frequency of metastases in the liver, lungs, spleen, heart, and adrenals of these mice provides an experimental system in which to study the development of disseminated malignancy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, N -- Crooke, R -- Hwang, L H -- Schibler, U -- Knowles, B B -- Solter, D -- CA-10815/CA/NCI NIH HHS/ -- CA-18470/CA/NCI NIH HHS/ -- CA-21124/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Apr 28;244(4903):460-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wistar Institute, Philadelphia, PA 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2785714" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism/pathology ; *Adipose Tissue, Brown/metabolism/pathology ; Animals ; Antigens, Polyomavirus Transforming/*genetics ; Cloning, Molecular ; Gene Expression Regulation ; Liver/metabolism ; Mice ; Mice, Transgenic ; Neoplasm Metastasis ; Neoplasms, Experimental/*genetics/pathology ; Nucleic Acid Hybridization ; Promoter Regions, Genetic ; RNA, Messenger/metabolism ; Tissue Distribution ; Transcription, Genetic ; alpha-Amylases/*genetics
    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
    Publication Date: 1998-03-07
    Description: The spindle checkpoint regulates the cell division cycle by keeping cells with defective spindles from leaving mitosis. In the two-hybrid system, three proteins that are components of the checkpoint, Mad1, Mad2, and Mad3, were shown to interact with Cdc20, a protein required for exit from mitosis. Mad2 and Mad3 coprecipitated with Cdc20 at all stages of the cell cycle. The binding of Mad2 depended on Mad1 and that of Mad3 on Mad1 and Mad2. Overexpression of Cdc20 allowed cells with a depolymerized spindle or damaged DNA to leave mitosis but did not overcome the arrest caused by unreplicated DNA. Mutants in Cdc20 that were resistant to the spindle checkpoint no longer bound Mad proteins, suggesting that Cdc20 is the target of the spindle checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, L H -- Lau, L F -- Smith, D L -- Mistrot, C A -- Hardwick, K G -- Hwang, E S -- Amon, A -- Murray, A W -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1041-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California at San Francisco, San Francisco, CA 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461437" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cadherins ; Calcium-Binding Proteins/metabolism ; *Carrier Proteins ; Cdc20 Proteins ; Cdh1 Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; DNA Damage ; DNA Replication ; Fungal Proteins/chemistry/*metabolism ; Ligases/metabolism ; Mad2 Proteins ; *Mitosis ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/metabolism ; Phosphoproteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/*cytology/*metabolism ; *Saccharomyces cerevisiae Proteins ; Spindle Apparatus/*metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
    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
    Publication Date: 2004-02-14
    Description: Somatic cell nuclear transfer (SCNT) technology has recently been used to generate animals with a common genetic composition. In this study, we report the derivation of a pluripotent embryonic stem (ES) cell line (SCNT-hES-1) from a cloned human blastocyst. The SCNT-hES-1 cells displayed typical ES cell morphology and cell surface markers and were capable of differentiating into embryoid bodies in vitro and of forming teratomas in vivo containing cell derivatives from all three embryonic germ layers in severe combined immunodeficient mice. After continuous proliferation for more than 70 passages, SCNT-hES-1 cells maintained normal karyotypes and were genetically identical to the somatic nuclear donor cells. Although we cannot completely exclude the possibility that the cells had a parthenogenetic origin, imprinting analyses support a SCNT origin of the derived human ES cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, Woo Suk -- Ryu, Young June -- Park, Jong Hyuk -- Park, Eul Soon -- Lee, Eu Gene -- Koo, Ja Min -- Jeon, Hyun Yong -- Lee, Byeong Chun -- Kang, Sung Keun -- Kim, Sun Jong -- Ahn, Curie -- Hwang, Jung Hye -- Park, Ky Young -- Cibelli, Jose B -- Moon, Shin Yong -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1669-74. Epub 2004 Feb 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Veterinary Medicine, Seoul National University, Seoul 151-742, Korea. hwangws@snu.ac.kr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963337" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biomarkers/analysis ; Blastocyst/*cytology ; Cell Differentiation ; *Cell Line ; *Cloning, Organism ; Culture Media ; Culture Techniques ; DNA Fingerprinting ; Embryo, Mammalian/*cytology ; Female ; Genomic Imprinting ; Humans ; Karyotyping ; Male ; Mice ; Mice, SCID ; Nuclear Transfer Techniques ; Oocyte Donation ; Ovarian Follicle/cytology ; Parthenogenesis ; Pluripotent Stem Cells/chemistry/*cytology ; Reverse Transcriptase Polymerase Chain Reaction ; Tandem Repeat Sequences ; Teratoma/etiology/pathology ; Testicular Neoplasms/etiology/pathology
    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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  • 5
    Publication Date: 2005-05-21
    Description: Patient-specific, immune-matched human embryonic stem cells (hESCs) are anticipated to be of great biomedical importance for studies of disease and development and to advance clinical deliberations regarding stem cell transplantation. Eleven hESC lines were established by somatic cell nuclear transfer (SCNT) of skin cells from patients with disease or injury into donated oocytes. These lines, nuclear transfer (NT)-hESCs, grown on human feeders from the same NT donor or from genetically unrelated individuals, were established at high rates, regardless of NT donor sex or age. NT-hESCs were pluripotent, chromosomally normal, and matched the NT patient's DNA. The major histocompatibility complex identity of each NT-hESC when compared to the patient's own showed immunological compatibility, which is important for eventual transplantation. With the generation of these NT-hESCs, evaluations of genetic and epigenetic stability can be made. Additional work remains to be done regarding the development of reliable directed differentiation and the elimination of remaining animal components. Before clinical use of these cells can occur, preclinical evidence is required to prove that transplantation of differentiated NT-hESCs can be safe, effective, and tolerated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, Woo Suk -- Roh, Sung Il -- Lee, Byeong Chun -- Kang, Sung Keun -- Kwon, Dae Kee -- Kim, Sue -- Kim, Sun Jong -- Park, Sun Woo -- Kwon, Hee Sun -- Lee, Chang Kyu -- Lee, Jung Bok -- Kim, Jin Mee -- Ahn, Curie -- Paek, Sun Ha -- Chang, Sang Sik -- Koo, Jung Jin -- Yoon, Hyun Soo -- Hwang, Jung Hye -- Hwang, Youn Young -- Park, Ye Soo -- Oh, Sun Kyung -- Kim, Hee Sun -- Park, Jong Hyuk -- Moon, Shin Yong -- Schatten, Gerald -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1777-83. Epub 2005 May 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Veterinary Medicine, Seoul National University, Seoul 151-742, Korea. hwangws@snu.ac.kr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905366" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Agammaglobulinemia ; Blastocyst/*cytology ; Cell Differentiation ; *Cell Line ; Child ; Child, Preschool ; *Cloning, Organism ; DNA Fingerprinting ; Diabetes Mellitus, Type 1 ; Epigenesis, Genetic ; Ethics Committees, Research ; Female ; Fibroblasts ; HLA Antigens/analysis ; Humans ; Informed Consent ; Karyotyping ; Male ; *Nuclear Transfer Techniques ; Oocyte Donation ; Pluripotent Stem Cells/*cytology/immunology ; Spinal Cord Injuries ; Stem Cell Transplantation ; Tissue and Organ Procurement
    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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  • 6
    Publication Date: 2009-05-16
    Description: Long-term memory and synaptic plasticity require changes in gene expression and yet can occur in a synapse-specific manner. Messenger RNA localization and regulated translation at synapses are thus critical for establishing synapse specificity. Using live-cell microscopy of photoconvertible fluorescent protein translational reporters, we directly visualized local translation at synapses during long-term facilitation of Aplysia sensory-motor synapses. Translation of the reporter required multiple applications of serotonin, was spatially restricted to stimulated synapses, was transcript- and stimulus-specific, and occurred during long-term facilitation but not during long-term depression of sensory-motor synapses. Translational regulation only occurred in the presence of a chemical synapse and required calcium signaling in the postsynaptic motor neuron. Thus, highly regulated local translation occurs at synapses during long-term plasticity and requires trans-synaptic signals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2821090/" 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/PMC2821090/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Dan Ohtan -- Kim, Sang Mok -- Zhao, Yali -- Hwang, Hongik -- Miura, Satoru K -- Sossin, Wayne S -- Martin, Kelsey C -- 15121/Canadian Institutes of Health Research/Canada -- NS045324/NS/NINDS NIH HHS/ -- R01 NS045324/NS/NINDS NIH HHS/ -- R01 NS045324-08A2/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 19;324(5934):1536-40. doi: 10.1126/science.1173205. Epub 2009 May 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Biobehavioral Sciences, University of California-Los Angeles (UCLA), BSRB 390B, 615 Charles E. Young Drive South, Los Angeles, CA 90095-1737, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19443737" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia ; Biological Transport ; Calcium/physiology ; Cells, Cultured ; FMRFamide/physiology ; Gene Expression Regulation ; Genes, Reporter ; Luminescent Proteins/genetics ; Motor Neurons/physiology ; Neuronal Plasticity/genetics/*physiology ; Neuropeptides/genetics ; Neurotransmitter Agents/genetics ; *Protein Biosynthesis ; RNA, Messenger/metabolism ; Sensory Receptor Cells/physiology ; Serotonin/physiology ; Synapses/genetics/*physiology
    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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