Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
about
A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosisThermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.Allosteric modulation of caspase 3 through mutagenesisTunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selectionProcaspase-3 activation as an anti-cancer strategy: structure-activity relationship of procaspase-activating compound 1 (PAC-1) and its cellular co-localization with caspase-3A bifunctional allosteric site in the dimer interface of procaspase-3Modifying caspase-3 activity by altering allosteric networks.Reassembly of active caspase-3 is facilitated by the propeptide.Targeting cell death in tumors by activating caspases.An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3.Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.The protein structures that shape caspase activity, specificity, activation and inhibition.Fibrils colocalize caspase-3 with procaspase-3 to foster maturation.pH effects on the stability and dimerization of procaspase-3.Genetic characterization of two gain-of-function alleles of the effector caspase DrICE in DrosophilaFolding and assembly kinetics of procaspase-3.Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3.The Apaf-1 apoptosome induces formation of caspase-9 homo- and heterodimers with distinct activities.Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.Modifications to a common phosphorylation network provide individualized control in caspases.In silico and in vivo analyses of the mutated human tissue plasminogen activator (mtPA) and the antithetical effects of P19 silencing suppressor on its expression in two Nicotiana species
P2860
Q24647033-76B62760-BF8B-4BD4-85A4-FA0649F4D626Q27666723-35A11936-B80F-4D30-8A0B-C7E5DAB856EAQ27679175-86313AA8-875B-4D36-BC23-006F95F25FA9Q27728138-0D2372BA-E878-43B4-9055-B2D7B1AF24FCQ28256422-6CDCA79F-8A49-4271-A37E-1ADFEF6833BBQ33924838-B8B25B8F-CE26-46C0-9075-387A28695080Q34680233-2C1E1BD0-F9A3-4349-A010-3C93DBFAD25DQ35058817-20EDC935-4163-4575-B4B5-F6541376BFB4Q35058822-B58C0B6C-0DCE-4A67-AD6A-DD8A397CE411Q35058831-753E8E79-4BC7-4E83-88F5-2D1A102473BBQ35058834-A0E1657C-0724-4213-944F-0A8098747777Q35902423-06DE1872-6DE2-4159-B124-F411AAED1E34Q36286189-BD2F9370-559F-4BD4-BA6D-F11695AF7527Q36476780-DA18AB26-DF30-47F8-B4A4-6209AEAFD9C6Q37179339-1C663F36-F328-49C5-AAE3-19C5518A614CQ41858306-D9CFD881-5328-4BD9-B59C-6FBC32591A6EQ42156615-CEB2219F-1609-4686-804A-8E0325986604Q42363495-CCB97727-5BD1-4AF0-8330-22186B17F5E0Q46549661-690EB195-40DF-4D52-9E2D-46193C6CE642Q50134152-E88E8523-08BA-4FD0-B618-3B797E6A5BD1Q58719633-D13E25A5-0DF0-4909-9CA0-DA8E9DA0A32C
P2860
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
description
2003 nî lūn-bûn
@nan
2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@ast
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@en
type
label
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@ast
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@en
prefLabel
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@ast
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@en
P2093
P2860
P356
P1433
P1476
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.
@en
P2093
A Clay Clark
Ashutosh Tripathy
Brett Feeney
Cristina Pop
P2860
P304
12311-12320
P356
10.1021/BI034999P
P407
P577
2003-10-01T00:00:00Z