About: TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087

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scientific article published on 01 September 2000

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 2000 (uk) article scientifique publié en 2000 (fr) im September 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en setiembre de 2000 (ast) scientific article published on 01 September 2000 (en)
publication date	wds:Q73250646-49ABD2BA-0E17-443E-B7B6-B8011175BF05
publication date	2000-01-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q73250646-0A67AB51-FFBB-4E2E-93F7-20776AF89BE0 wds:Q73250646-1EEC57FC-AA38-4678-86E9-E434E2CF3AEB wds:Q73250646-2E385AEE-3A03-4539-AF00-0CC01581D8F4 wds:Q73250646-90679A03-92E2-4BEA-90BA-F7DEBC92217B wds:Q73250646-97F19700-5448-4508-8D21-24E27B9E1AAE wds:Q73250646-BB7E505F-B6B9-472C-BC14-4B0FA7A842EA wds:Q73250646-CFFF3609-6DA7-4626-B268-E71223551CCE wds:Q73250646-E9F7B076-87D0-4424-B234-9946EA52A10F wds:Q73250646-ECE9CD9A-9363-497C-8A20-BE896148D886
cites work	Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities. Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death Structures of TMC-95A-D: novel proteasome inhibitors from Apiospora montagnei sacc. TC 1093 TMC-86A, B and TMC-96, new proteasome inhibitors from Streptomyces sp. TC 1084 and Saccharothrix sp. TC 1094. I. Taxonomy, fermentation, isolation, and biological activities. c-Fos degradation by the proteasome. An early, Bcl-2-regulated step in apoptosis TMC-86A, B and TMC-96, new proteasome inhibitors from Streptomyces sp. TC 1084 and Saccharothrix sp. TC 1094. II. Physico-chemical properties and structure determination
access restriction status	wds:Q73250646-2E45C987-D683-4090-AA80-609056D257B6
access restriction status	open access
author name string	wds:Q73250646-19C095E8-C6F8-47AD-A4D1-435E81EC61F1 wds:Q73250646-2866AF58-D95F-4DFD-AFA5-9B85667AE164 wds:Q73250646-31A8A0D2-781C-4467-A2DD-03DE39FE8662 wds:Q73250646-4B79E1AD-44F9-408C-B77B-0E5575CDA5CD wds:Q73250646-7556134F-409F-4E72-AFAE-5D17F9EB5EFE wds:Q73250646-D455C093-E21B-4506-AFD0-35F27B370AAE
author name string	K Takahashi M Nishio S Suzuki T Ohnuki S Komatsubara Y Koguchi
rdfs:label	TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (en) TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (nl)
skos:prefLabel	TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (en) TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (nl)
name	TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (en) TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (nl)
title	wds:Q73250646-34088DA7-7A9C-48CF-980C-90FC00A65375
title	TMC-89A and B, new proteasome inhibitors from streptomyces sp. TC 1087 (en)
page(s)	wds:Q73250646-2EC15019-8E78-4866-BA42-E6FE93F12598
page(s)	967-972
instance of	wds:Q73250646-68217E73-6477-497B-9DF1-64090ADAEC55
instance of	scholarly article
main subject	wds:Q73250646-2166675A-98ED-4C88-960F-B463FBE81AB7 wds:Q73250646-4BC8D7D7-821B-43A5-9E5E-5DC2555EE8DC wds:Q73250646-9D8218D3-D14C-422E-A196-9CCF6CED9B90 wds:Q73250646-A568173C-E189-4CC9-90C6-CC3C8F4D6B13 wds:Q73250646-F3B78195-79C2-4E33-8E00-A3DC732144C7
main subject	Streptomyces (2S)-N'-[(2S,3R)-3-hydroxy-1-[[(2S,3R)-3-hydroxy-1-[[(2R)-1-[(2R)-2-(hydroxymethyl)oxiran-2-yl]-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]amino]-1-oxobutan-2-yl]-2-methylpropanediamide (2R)-N'-[(2R,3R)-3-hydroxy-1-[[(2S,3R)-3-hydroxy-1-[[(2R)-1-[(2S)-2-(hydroxymethyl)oxiran-2-yl]-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]amino]-1-oxobutan-2-yl]-2-methylpropanediamide TMC-89B TMC-89A
PubMed ID	wds:Q73250646-3489D649-5FED-4F24-A651-90F06BF80806
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11099231
PubMed ID	11099231
published in	wds:Q73250646-FDC05109-C88A-4002-8513-91A4751ED20F
full work available at URL	wds:Q73250646-473FC517-048B-4A0F-BEEE-2D71E8C1A8FB
published in	The Journal of Antibiotics
full work available at URL	https://www.jstage.jst.go.jp/article/antibiotics1968/53/9/53_9_967/_pdf
issue	wds:Q73250646-DBB8D039-5F37-415A-A88F-91C7A0FCB631
volume	wds:Q73250646-0ED44CF5-6262-42B1-8442-0549CB08E2AB
issue	9
volume	53
DOI	wds:Q73250646-BC206ADD-10A7-4A5A-8447-9CCF280D7BD7
DOI	http://dx.doi.org/10.7164/ANTIBIOTICS.53.967
DOI	10.7164/ANTIBIOTICS.53.967
online access status	wds:Q73250646-A437A604-F795-43C1-BB34-D026418413D4
online access status	open access
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73250646
is cites work of	Development and characterization of proteasome inhibitors Proteasome regulators: activators and inhibitors. Irreversible inhibitors of serine, cysteine, and threonine proteases 20S proteasome and its inhibitors: crystallographic knowledge for drug development Peptides with anticancer use or potential. Natural product inhibitors of the ubiquitin-proteasome pathway The ubiquitin-proteasome pathway and proteasome inhibitors The proteasomal system. Proteasome inhibitors: recent advances and new perspectives in medicinal chemistry Immunoproteasome in cancer and neuropathologies: a new therapeutic target? Recent advances in the identification and development of 20S proteasome inhibitors Proteasome inhibitors as therapeutic agents: current and future strategies. Exploiting nature's rich source of proteasome inhibitors as starting points in drug development Stereocontrolled synthesis of the northern part of potent proteasome inhibitor TMC-95A. The therapeutic potential of microbial proteasome inhibitors. Macyranones: Structure, Biosynthesis, and Binding Mode of an Unprecedented Epoxyketone that Targets the 20S Proteasome Genetic basis for the biosynthesis of the pharmaceutically important class of epoxyketone proteasome inhibitors. Semi-high throughput method of measuring proteasome inhibition in vitro and in cultured cells. Built to bind: biosynthetic strategies for the formation of small-molecule protease inhibitors Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes

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