Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors - Test2 - elhamkhani - TriplyDB

Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors

Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors

http://www.wikidata.org/entity/Q27642313

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Effect of nitroxoline on angiogenesis and growth of human bladder cancer Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression Inhibition of Monometalated Methionine Aminopeptidase: Inhibitor Discovery and Crystallographic Analysis †Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes Inhibition of Mycobacterium tuberculosis Methionine Aminopeptidases by Bengamide Derivatives Structural Analysis of Bengamide Derivatives as Inhibitors of Methionine Aminopeptidases Pyridinylpyrimidines selectively inhibit human methionine aminopeptidase-1 Pyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1 in Cells Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases.The dietary bioflavonoid, quercetin, selectively induces apoptosis of prostate cancer cells by down-regulating the expression of heat shock protein 90.A selective account of effective paradigms and significant outcomes in the discovery of inspirational marine natural products.Identifying compound-target associations by combining bioactivity profile similarity search and public databases mining.Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity.Myxobacteria versus sponge-derived alkaloids: the bengamide family identified as potent immune modulating agents by scrutiny of LC-MS/ELSD libraries Target identification of small molecules based on chemical biology approaches.An array of bengamide E analogues modified at the terminal olefinic position: synthesis and antitumor properties.Structural basis of catalysis by monometalated methionine aminopeptidase Two methionine aminopeptidases from Acinetobacter baumannii are functional enzymes.Production of the Bengamide Class of Marine Natural Products in Myxobacteria: Biosynthesis and Structure-Activity Relationships.Functional genomics to new drug targets.Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives.Kinase selectivity profiling by inhibitor affinity chromatography.Drug target identification using network analysis: Taking active components in Sini decoction as an example.A chemical and genetic approach to the mode of action of fumagillin Marine-derived angiogenesis inhibitors for cancer therapy.The Bengamides: A Mini-Review of Natural Sources, Analogues, Biological Properties, Biosynthetic Origins, and Future Prospects.The future of microfluidic assays in drug development.Chemistry and biology of bengamides and bengazoles, bioactive natural products from Jaspis sponges.Regulation of c-Src nonreceptor tyrosine kinase activity by bengamide A through inhibition of methionine aminopeptidases An endothelial cell genetic screen identifies the GTPase Rem2 as a suppressor of p19ARF expression that promotes endothelial cell proliferation and angiogenesis.FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis.Yeast glutamine-fructose-6-phosphate aminotransferase (Gfa1) requires methionine aminopeptidase activity for proper function.Omics assisted N-terminal proteoform and protein expression profiling upon methionine aminopeptidase 1 (MetAP1) deletion.Concepts and Methods to Access Novel Antibiotics from Actinomycetes.

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Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors

http://www.wikidata.org/entity/Q27642313

description

2003 nî lūn-bûn

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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Journal of Biological Chemistry

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Proteomics-based target identi ...... nine aminopeptidase inhibitors

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Anthony Morollo

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Dieter R Mueller

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Frederick R Kinder

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Hans Voshol

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Harry Towbin

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James A DeCaprio

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Jan van Oostrum

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Jeanette Wood

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Kenneth W Bair

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Michael J Eck

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P2860

Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase

The N-end rule: functions, mysteries, uses

Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2

The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis

Structure of human methionine aminopeptidase-2 complexed with fumagillin

Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells

The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae.

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52964-52971

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2207008

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10.1074/JBC.M309039200

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52

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278

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2003-10-08T00:00:00Z

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14534293

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