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  • Humans  (6)
  • Chemistry
  • Surface physics, nanoscale physics, low-dimensional systems
  • American Association for the Advancement of Science (AAAS)  (7)
  • 1
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    A phosphatase associated with metastasis of colorectal cancer (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-13
    Description: To gain insights into the molecular basis for metastasis, we compared the global gene expression profile of metastatic colorectal cancer with that of primary cancers, benign colorectal tumors, and normal colorectal epithelium. Among the genes identified, the PRL-3 protein tyrosine phosphatase gene was of particular interest. It was expressed at high levels in each of 18 cancer metastases studied but at lower levels in nonmetastatic tumors and normal colorectal epithelium. In 3 of 12 metastases examined, multiple copies of the PRL-3 gene were found within a small amplicon located at chromosome 8q24.3. These data suggest that the PRL-3 gene is important for colorectal cancer metastasis and provide a new therapeutic target for these intractable lesions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saha, S -- Bardelli, A -- Buckhaults, P -- Velculescu, V E -- Rago, C -- St Croix, B -- Romans, K E -- Choti, M A -- Lengauer, C -- Kinzler, K W -- Vogelstein, B -- CA 62924/CA/NCI NIH HHS/ -- CA43460/CA/NCI NIH HHS/ -- CA57345/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Nov 9;294(5545):1343-6. Epub 2001 Oct 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, The Oncology Center, Department of Surgery, Johns Hopkins Medical Institutions, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11598267" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/enzymology/genetics/pathology ; Chromosome Mapping ; Chromosomes, Human, Pair 8 ; Colon/enzymology ; Colorectal Neoplasms/*enzymology/*genetics/pathology ; Gene Amplification ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic ; Gene Library ; Humans ; Immediate-Early Proteins/*genetics/metabolism ; Intestinal Mucosa/enzymology ; Neoplasm Metastasis/*genetics ; Neoplasm Proteins ; Neoplasm Staging ; Polymerase Chain Reaction ; Protein Tyrosine Phosphatases/*genetics/metabolism ; Rectum/enzymology
    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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  • 2
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    Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-09-18
    Description: The mammalian cytoskeletal proteins beta- and gamma-actin are highly homologous, but only beta-actin is amino-terminally arginylated in vivo, which regulates its function. We examined the metabolic fate of exogenously expressed arginylated and nonarginylated actin isoforms. Arginylated gamma-actin, unlike beta-, was highly unstable and was selectively ubiquitinated and degraded in vivo. This instability was regulated by the differences in the nucleotide coding sequence between the two actin isoforms, which conferred different translation rates. gamma-actin was translated more slowly than beta-actin, and this slower processing resulted in the exposure of a normally hidden lysine residue for ubiquitination, leading to the preferential degradation of gamma-actin upon arginylation. This degradation mechanism, coupled to nucleotide coding sequence, may regulate protein arginylation in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2941909/" 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/PMC2941909/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Fangliang -- Saha, Sougata -- Shabalina, Svetlana A -- Kashina, Anna -- 5R01HL084419/HL/NHLBI NIH HHS/ -- R01 HL084419/HL/NHLBI NIH HHS/ -- R01 HL084419-03/HL/NHLBI NIH HHS/ -- R01 HL084419-03S1/HL/NHLBI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2010 Sep 17;329(5998):1534-7. doi: 10.1126/science.1191701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20847274" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry/genetics/*metabolism ; Amino Acid Sequence ; Animals ; Arginine/*metabolism ; Cell Line ; Cell Line, Tumor ; *Codon ; Humans ; Lysine/metabolism ; Mice ; Nucleic Acid Conformation ; Proteasome Endopeptidase Complex/metabolism ; Protein Biosynthesis ; Protein Folding ; Protein Isoforms/chemistry/genetics/metabolism ; *Protein Modification, Translational ; Protein Stability ; RNA, Messenger/chemistry/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Ubiquitination
    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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    Mutational analysis of the tyrosine kinome in colorectal cancers (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bardelli, Alberto -- Parsons, D Williams -- Silliman, Natalie -- Ptak, Janine -- Szabo, Steve -- Saha, Saurabh -- Markowitz, Sanford -- Willson, James K V -- Parmigiani, Giovanni -- Kinzler, Kenneth W -- Vogelstein, Bert -- Velculescu, Victor E -- CA43460/CA/NCI NIH HHS/ -- CA57345/CA/NCI NIH HHS/ -- CA62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 May 9;300(5621):949.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Howard Hughes Medical Institute and The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738854" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Colorectal Neoplasms/*enzymology/*genetics ; Computational Biology ; *DNA Mutational Analysis ; Exons ; Fusion Proteins, gag-onc/genetics ; Guanylate Cyclase/genetics ; Humans ; Molecular Sequence Data ; Mutation ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/chemistry/*genetics/metabolism ; Receptor, EphA3/genetics ; Receptor, trkB/genetics ; Receptor, trkC/genetics ; Sequence Analysis, DNA ; Vascular Endothelial Growth Factor Receptor-2/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)
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  • 4
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    Arsenic poisoning in West Bengal (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saha, D P -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1287.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966592" target="_blank"〉PubMed〈/a〉
    Keywords: *Arsenic Poisoning ; Humans ; India ; Keratosis/chemically induced ; Skin Diseases/*chemically induced
    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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  • 5
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    Access to stem cells and data: persons, property rights, and scientific progress (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-12
    Description: Many fields have struggled to develop strategies, policies, or structures to optimally manage data, materials, and intellectual property rights (IPRs). There is growing recognition that the field of stem cell science, in part because of its complex IPRs landscape and the importance of cell line collections, may require collective action to facilitate basic and translational research. Access to pluripotent stem cell lines and the information associated with them is critical to the progress of stem cell science, but simple notions of access are substantially complicated by shifting boundaries between what is considered information versus material, person versus artifact, and private property versus the public domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathews, Debra J H -- Graff, Gregory D -- Saha, Krishanu -- Winickoff, David E -- New York, N.Y. -- Science. 2011 Feb 11;331(6018):725-7. doi: 10.1126/science.1201382.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Berman Institute of Bioethics, Deering Hall, 208, 1809 Ashland Avenue, Baltimore, MD 21205, USA. dmathews@jhu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21311015" target="_blank"〉PubMed〈/a〉
    Keywords: *Access to Information ; Biological Specimen Banks ; Confidentiality ; Humans ; Informed Consent ; *Intellectual Property ; *Ownership ; Public Sector ; *Stem Cell Research ; *Stem Cells ; Tissue Donors
    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
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    Metal-catalyzed electrochemical diazidation of alkenes (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-08-11
    Description: Vicinal diamines are a common structural motif in bioactive natural products, therapeutic agents, and molecular catalysts, motivating the continuing development of efficient, selective, and sustainable technologies for their preparation. We report an operationally simple and environmentally friendly protocol that converts alkenes and sodium azide—both readily available feedstocks—to 1,2-diazides. Powered by electricity and catalyzed by Earth-abundant manganese, this transformation proceeds under mild conditions and exhibits exceptional substrate generality and functional group compatibility. Using standard protocols, the resultant 1,2-diazides can be smoothly reduced to vicinal diamines in a single step, with high chemoselectivity. Mechanistic studies are consistent with metal-mediated azidyl radical transfer as the predominant pathway, enabling dual carbon-nitrogen bond formation.
    Keywords: Chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Digoxin-inactivating bacteria: identification in human gut flora (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-04-15
    Description: Digoxin, the most widely used cardiac glycoside, undergoes significant metabolic conversion in many patients to cardioinactive metabolites in which the lactone ring is reduced. This appears to occur within the gastrointestinal tract. An attempt was made to isolate and identify the organisms capable of reducing digoxin from stool cultures obtained from human volunteers. Of hundreds of isolates studied, only Eubacterium lentum, a common anaerobe of the human colonic flora, converted digoxin to reduced derivatives. Such organisms were also isolated in high concentrations from the stools of individuals who did not excrete these metabolites when given digoxin in vivo. When the growth of E. lentum was stimulated by arginine, inactivation of digoxin was inhibited. Neither the presence of these organisms alone nor their concentration within the gut flora appeared to determine whether digoxin would be inactivated by this pathway in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saha, J R -- Butler, V P Jr -- Neu, H C -- Lindenbaum, J -- AA 00249/AA/NIAAA NIH HHS/ -- HL 10608/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):325-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836275" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/pharmacology ; Colon/microbiology ; Digoxin/*metabolism ; Eubacterium/drug effects/*metabolism ; Feces/microbiology ; Humans ; Oxidation-Reduction
    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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