about
Imaging mitochondrial redox potential and its possible link to tumor metastatic potentialCrystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product ReleaseCrystal Structures of Trypanosoma cruzi UDP-Galactopyranose Mutase Implicate Flexibility of the Histidine Loop in Enzyme ActivationIdentification of a Conserved Histidine as Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.Chloroquine binding reveals flavin redox switch function of quinone reductase 2.Thiol/Disulfide redox switches in the regulation of heme binding to proteins.Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein.H2O2 production rate in Lactobacillus johnsonii is modulated via the interplay of a heterodimeric flavin oxidoreductase with a soluble 28 Kd PAS domain containing protein.Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).Structure, mechanism, and dynamics of UDP-galactopyranose mutase.Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.Structure, function, and mechanism of proline utilization A (PutA).Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A.The signaling protein MucG negatively affects the production and the molecular mass of alginate in Azotobacter vinelandii.
P2860
Q26825824-51668071-37B6-4B62-98C3-E57CD93860B0Q27675129-26256EEE-8C7F-478B-9429-A4E710646308Q27679366-D7D7A874-892A-4FBC-A4A9-DB03D6596342Q30101149-FD848DCE-0264-4713-9228-9C7DB559768BQ34331796-A90A1645-0EAA-4091-A3FE-16ACF59CBA76Q34589250-27796B9C-5268-4167-B7EE-9E8830BCCA4CQ35663174-63D84E4D-157A-462E-8899-F0C19C7B7247Q35847815-35752EDF-03FA-4F46-B17E-6DE0870FC32BQ35926219-2F4B21D6-3E8E-40F6-8823-BCA15C17A43FQ37563541-9B3A15EA-B00F-4760-8EF8-F95CFDABF6BFQ37624622-A4D58118-9439-4489-B929-75508D7C6F82Q37626806-3C110C11-C98C-4871-A657-31FAB891B9AFQ39437714-65DAEA57-4181-4EED-B5AA-31F5EBE0BADEQ47579064-0E49D8F8-DF95-4FCD-A818-3504E6806392Q48263228-5BA3C533-00DB-4ADA-BC7F-41DD66AD8FC7
P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
Flavin redox switching of protein functions
@ast
Flavin redox switching of protein functions
@en
type
label
Flavin redox switching of protein functions
@ast
Flavin redox switching of protein functions
@en
prefLabel
Flavin redox switching of protein functions
@ast
Flavin redox switching of protein functions
@en
P2093
P2860
P356
P1476
Flavin redox switching of protein functions
@en
P2093
Donald F Becker
Michael A Moxley
Weidong Zhu
P2860
P304
P356
10.1089/ARS.2010.3417
P577
2010-10-28T00:00:00Z