L2′ loop is critical for caspase-7 active site formation
about
Substrate-Induced Conformational Changes Occur in All Cleaved Forms of Caspase-6Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.A designed redox-controlled caspaseZinc-mediated Allosteric Inhibition of Caspase-6Structural and Enzymatic Insights into Caspase-2 Protein Substrate Recognition and CatalysisHydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 ProteasePhosphorylation regulates assembly of the caspase-6 substrate-binding groove.Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulationAllosteric modulation of caspase 3 through mutagenesisTunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selectionAllosteric regulation of protease activity by small molecules.A bifunctional allosteric site in the dimer interface of procaspase-3Small Molecule Active Site Directed Tools for Studying Human CaspasesBioinformatics and variability in drug response: a protein structural perspective.Inhibition of caspase-9 by stabilized peptides targeting the dimerization interface.Impact of mutations on the allosteric conformational equilibrium.In-silico analysis of caspase-3 and -7 proteases from blood-parasitic Schistosoma species (Trematoda) and their human host.Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.Molecular determinants involved in activation of caspase 7Cacidases: caspases can cleave after aspartate, glutamate and phosphoserine residues.Caspase-6 latent state stability relies on helical propensity.Studies of the molecular mechanism of caspase-8 activation by solution NMR.Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.Dual Site Phosphorylation of Caspase-7 by PAK2 Blocks Apoptotic Activity by Two Distinct Mechanisms.Active site-adjacent phosphorylation at Tyr-397 by c-Abl kinase inactivates caspase-9.Utilizing Inverse Emulsion Polymerization To Generate Responsive Nanogels for Cytosolic Protein Delivery.Multiple mechanisms of zinc-mediated inhibition for the apoptotic caspases -3, -6, -7, & -8.Modulation of procaspase-7 self-activation by PEST amino acid residues of the N-terminal prodomain and intersubunit linker.Caspase-9 CARD : core domain interactions require a properly formed active site.
P2860
Q27666081-0F67E9BF-B594-4159-B0B8-08D233CB7827Q27666723-AC540B7B-77E2-4343-84CD-1F4E5D53EA1AQ27670443-7AF7BA2A-3842-4EF4-838E-F55FF473412AQ27671521-ED59D015-AD47-43F2-BF3F-9F033857C8DFQ27671643-EFD433AB-87D6-4E24-B5DB-8490C5C551D5Q27676981-F2ED5E59-9FD3-4E1C-B930-C92BF0EAD85BQ27678364-89080758-58A3-478E-B12D-C8063DBDE815Q27678659-C81473E8-6481-45B3-B350-3794D456263BQ27679175-78EF4C44-C999-457C-B075-059E83A2E94AQ27728138-15FC1A8D-AD5E-4DA5-BC30-E9CB5E6122A1Q33601580-1D21080D-7DF6-4BC9-A992-68881B5C4361Q33924838-19A1586C-1C37-456C-A157-15C4C9257D08Q35836079-62E7EB80-5688-4D03-A3D3-427C7AF9CBF5Q36009999-EF05A0E5-3E74-4201-ACB1-DAB722A50687Q36529717-B8208FC8-57D5-4C7A-84A8-7930A47EBD16Q36570126-96A052F4-59C9-4831-A19B-571974F193F5Q36994827-5576E961-8900-495D-802F-BE40DE807EE4Q37017201-8E36118E-621F-49C8-988B-F323CECF61F6Q41588503-FA16AB74-7A17-4428-A262-1A115197967AQ41636957-37159078-C291-4C0C-AB35-1B52272C1AFAQ42725779-AE4EDE8F-BD20-47FF-ACDF-DCAF31171B47Q43256262-848D838A-AE9E-4443-A25A-87D3BA59BCFDQ46549661-9CB02AFD-129F-40E7-8178-B4E5434C3C45Q47143415-CDC99933-8264-4838-BC71-E80E3444633FQ47608162-C4CDB09D-CA5F-47E7-92D9-E2B69F3CB733Q47624521-4290C833-8DF2-4A5B-88B0-A85AF36322C2Q49822760-F77D868C-62E9-4309-B74F-5673840B3AECQ50918511-D4CC03E4-DCBA-4BEB-92C2-76FEDD7B8797Q52676492-4249398C-A7C3-4A32-B91F-412D23EF0A77
P2860
L2′ loop is critical for caspase-7 active site formation
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
L2′ loop is critical for caspase-7 active site formation
@ast
L2′ loop is critical for caspase-7 active site formation
@en
L2′ loop is critical for caspase-7 active site formation
@nl
type
label
L2′ loop is critical for caspase-7 active site formation
@ast
L2′ loop is critical for caspase-7 active site formation
@en
L2′ loop is critical for caspase-7 active site formation
@nl
prefLabel
L2′ loop is critical for caspase-7 active site formation
@ast
L2′ loop is critical for caspase-7 active site formation
@en
L2′ loop is critical for caspase-7 active site formation
@nl
P2860
P356
P1433
P1476
L2′ loop is critical for caspase-7 active site formation
@en
P2093
Jeanne A Hardy
Witold A Witkowski
P2860
P304
P356
10.1002/PRO.151
P577
2009-07-01T00:00:00Z