about
Proposal of Dual Inhibitor Targeting ATPase Domains of Topoisomerase II and Heat Shock Protein 90Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancersParalog-selective Hsp90 inhibitors define tumor-specific regulation of HER2An Organometallic Inhibitor for the Human Repair Enzyme 7,8-Dihydro-8-oxoguanosine TriphosphataseExploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of HSP70.Drugging the cancer kinome: progress and challenges in developing personalized molecular cancer therapeuticsRole of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complexProtein chaperones: a composition of matter review (2008 - 2013).Heat shock protein 90 inhibitors in the treatment of cancer: current status and future directionsThe generation of purinome-targeted libraries as a means to diversify ATP-mimetic chemical classes for lead finding.Conformational dynamics of ATP/Mg:ATP in motor proteins via data mining and molecular simulation.In Vitro Activity of Geldanamycin Derivatives against Schistosoma japonicum and Brugia malayiValidation of inhibitors of an ABC transporter required to transport lipopolysaccharide to the cell surface in Escherichia coli.A targeted quantitative proteomics strategy for global kinome profiling of cancer cells and tissues.An RNA aptamer specific to Hsp70-ATP conformation inhibits its ATPase activity independent of Hsp40.A Systematic Study on Structure and Function of ATPase of Wuchereria bancrofti.Zebrafish dead end possesses ATPase activity that is required for primordial germ cell development.Targeting chaperones in transformed systems--a focus on Hsp90 and cancer.Purine-scaffold Hsp90 inhibitors.The SMARCA2/4 ATPase Domain Surpasses the Bromodomain as a Drug Target in SWI/SNF-Mutant Cancers: Insights from cDNA Rescue and PFI-3 Inhibitor Studies.Hsp90 regulates the phosphorylation and activity of serum- and glucocorticoid-regulated kinase-1.Isotope-coded ATP probe for quantitative affinity profiling of ATP-binding proteins.Heat Shock Protein (HSP) Drug Discovery and Development: Targeting Heat Shock Proteins in Disease.Discovery and development of heat shock protein 90 inhibitors.OLA1, an Obg-like ATPase, suppresses antioxidant response via nontranscriptional mechanismsKnockdown of OLA1, a regulator of oxidative stress response, inhibits motility and invasion of breast cancer cells.HPLC method development, validation and impurity characterization for an antitumor Hsp90 inhibitor-PU-H71 (NSC 750424).Depleting Mycobacterium tuberculosis of the transcription termination factor Rho causes pervasive transcription and rapid deathTargeting the type III secretion system to treat bacterial infections.Mycobacterium tuberculosis P-type ATPases: possible targets for drug or vaccine development.Global discovery of protein kinases and other nucleotide-binding proteins by mass spectrometry.A novel SERCA inhibitor demonstrates synergy with classic SERCA inhibitors and targets multidrug-resistant AML.Synthesis and evaluation of cell-permeable biotinylated PU-H71 derivatives as tumor Hsp90 probesAntisense-mediated Inhibition of the plasma membrane calcium-ATPase suppresses proliferation of MCF-7 cells.Discovery of mono- and disubstituted 1H-pyrazolo[3,4]pyrimidines and 9H-purines as catalytic inhibitors of human DNA topoisomerase IIα.A genome-wide structure-based survey of nucleotide binding proteins in M. tuberculosis.N-N bond-forming cyclization for the one-pot synthesis of N-aryl[3,4-d]pyrazolopyrimidines.Targeting of nucleotide-binding proteins by HAMLET--a conserved tumor cell death mechanism.Fingerprinting differential active site constraints of ATPases
P2860
Q26997981-B7D03AAD-7B7E-4C70-A65A-46DBDF7F06A3Q27022514-521A9241-61A6-4E40-9FCD-A2F2E1AFAE83Q27679845-A9BFE6CD-6578-4E15-89AB-2EC26313B1E9Q27680660-E6BFE5A1-095B-43E2-9E07-8EA5F50817BBQ27704725-169A4CB7-EDBA-456B-83F5-C0B5908A5E6CQ28254233-A12A8A49-1626-42F7-A540-30675676CFACQ28566112-935006AA-25D0-415B-A5A5-A9279D156940Q34013266-80096134-E621-4174-94E9-261F97F0A843Q34164027-DC727F50-7DE5-4DE3-B6A2-09A9C54B143FQ34164591-1DB07C39-14CD-48D3-985A-A043D64B08F3Q34392699-C2D1006C-8CE4-4353-925E-AB70829EF4B1Q34495415-6A9D4B62-C564-4811-8F62-B82314AAF3FCQ34715492-73796A79-B556-44A0-ABF1-A1CCDC2FFA25Q35092533-29350A7A-5DF9-4BBD-8307-37CBA003D66CQ35224117-18D2D781-FE5F-4952-8E0C-3C602DA38FEBQ35549566-EEB8B344-A2BA-4CC5-A7D5-2B98A9418153Q35592123-8451132A-8452-4C70-99A8-2C3CC007AE6AQ36379365-14BC47A3-5795-47D3-8D32-4FD5639B5079Q36426208-43119DE7-B588-4AAB-8C88-00577C30AEC3Q36584337-CE62BF17-9B4F-41E1-82BC-D998B8043024Q36739599-8FCC53D6-F463-4E98-BB39-EEB908C31039Q37166849-37153973-BD30-4733-BC1E-E45DF5D3CCAEQ37198085-FED2CC61-8087-49E1-9B00-AC16D8668374Q37328728-31B1ABCC-658D-45AF-BF61-916C55DAEE90Q37340833-3590CCCD-D83E-4423-B04C-D6D64E66BC29Q37411015-3C488BA9-B5D3-45D4-B2CA-F154ADACF457Q37638066-FA3F603F-A090-4659-8E67-C5B5873D14E3Q37736367-5F3671FB-E739-4A9F-9253-48A651EDDD59Q38167861-A4D45319-CCD9-4620-B8F3-64700F98EA95Q38238758-E39FBA3C-6A48-4A37-9B03-B97C60ED8D94Q38265824-0132069B-3DE4-4EB0-AC69-250F8D834B1DQ39089915-D630FF20-A094-4366-82F5-F2CDF55C8D75Q39911066-3E92A420-4CD5-4B9B-96CB-68CA726CF0F9Q40418313-FD5832DC-8C08-443A-9A12-D08E627DB05DQ41672722-04948980-E373-4ED7-B891-3767141141CCQ42083154-1AA88666-768B-446F-8251-971594BC7155Q42227466-057BA701-4D49-456D-8B14-F0B2ECA03B92Q52307146-8C5FBF94-1A6B-433B-AC1A-D1B4F460066AQ58376396-4FADB2C8-7230-4F61-9B29-3319EB6B2296
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
ATPases as drug targets: learning from their structure.
@ast
ATPases as drug targets: learning from their structure.
@en
ATPases as drug targets: learning from their structure.
@nl
type
label
ATPases as drug targets: learning from their structure.
@ast
ATPases as drug targets: learning from their structure.
@en
ATPases as drug targets: learning from their structure.
@nl
prefLabel
ATPases as drug targets: learning from their structure.
@ast
ATPases as drug targets: learning from their structure.
@en
ATPases as drug targets: learning from their structure.
@nl
P2860
P356
P1476
ATPases as drug targets: learning from their structure.
@en
P2093
Patrick Chène
P2860
P2888
P304
P356
10.1038/NRD894
P577
2002-09-01T00:00:00Z