Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain
about
Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulationsNMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional DynamicsSolution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plantsDynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain.Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations.A small molecule agonist of EphA2 receptor tyrosine kinase inhibits tumor cell migration in vitro and prostate cancer metastasis in vivo.Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulationsStructures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.Ligand-induced Dimerization of Middle East Respiratory Syndrome (MERS) Coronavirus nsp5 Protease (3CLpro): IMPLICATIONS FOR nsp5 REGULATION AND THE DEVELOPMENT OF ANTIVIRALS.Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.Why do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water.
P2860
Q28477745-BF9A8D58-A096-49BA-83D2-46176D317519Q28547136-0CB2EFB6-2C71-49C2-B21E-AA1292F3FD43Q33888270-6C5A5FF6-DBB8-4BB9-A17D-A86C8CB23FFFQ33921124-8BC6A581-5A04-41DB-8A83-DC92C74ACA86Q34141080-04B5C3A2-7E85-4EFA-939E-F23E71C0A530Q34390813-0CC9E67A-68DB-4A55-9E7A-A678DF344F38Q35004861-B2B4088A-AF10-4DED-85C0-F026332D607DQ35592656-A991652C-15C3-4334-928B-4F98CCBE1A71Q35925764-97CFE151-90B9-4665-BA48-9A0999636AABQ36583222-EB3CFDE2-EC14-4C97-BBBF-721CDC08E2DCQ37406805-AE82C551-3C84-45AB-B5C4-A25219FDF2FA
P2860
Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain
description
2011 nî lūn-bûn
@nan
2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Dynamically-driven inactivatio ...... A mutation on the extra domain
@ast
Dynamically-driven inactivatio ...... A mutation on the extra domain
@en
Dynamically-driven inactivatio ...... A mutation on the extra domain
@nl
type
label
Dynamically-driven inactivatio ...... A mutation on the extra domain
@ast
Dynamically-driven inactivatio ...... A mutation on the extra domain
@en
Dynamically-driven inactivatio ...... A mutation on the extra domain
@nl
prefLabel
Dynamically-driven inactivatio ...... A mutation on the extra domain
@ast
Dynamically-driven inactivatio ...... A mutation on the extra domain
@en
Dynamically-driven inactivatio ...... A mutation on the extra domain
@nl
P2093
P2860
P1476
Dynamically-driven inactivatio ...... A mutation on the extra domain
@en
P2093
J Sivaraman
Liangzhong Lim
Lushan Wang
Shixiong Lua
Yuguang Mu
P2860
P304
P356
10.1371/JOURNAL.PCBI.1001084
P407
P577
2011-02-01T00:00:00Z