S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein - Wikidata - wikimedia - TriplyDB

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

http://www.wikidata.org/entity/Q27722821

about

Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence.Computational Structural Biology of -nitrosylation of Cancer Targets

P2860

Q52331604-FA76FB5F-CFC6-4476-833B-05F17D6774AC Q58781601-E250B6A3-7D08-4F2F-9179-6F4717471125

P2860

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

http://www.wikidata.org/entity/Q27722821

description

2016 nî lūn-bûn

@nan

2016 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

name

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@ast

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@en

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@nl

type

label

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@ast

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@en

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@nl

prefLabel

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@ast

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@en

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@nl

P1433

Q27722821-C12340B0-D1A1-4BAA-BFD4-E590B707F6F8

P1476

Q27722821-132F7CCB-6331-4B88-913C-9F45FAF95807

P2093

Q27722821-24C1DF2E-ABD4-44C3-B7B6-8A081806DC8B

Q27722821-467D4607-76F1-4182-B8F0-5DEC01E93D22

Q27722821-B61534A5-A7E1-4881-BD01-628D5D9EEA39

Q27722821-BBB5B780-16BA-4E6D-97BB-260002615A05

Q27722821-C7F89DE8-9C20-4ECC-8CE1-57391691A13E

Q27722821-CFCED176-B2CD-4CDB-8408-7A5A2D9CDD95

Q27722821-EE91A54E-8E88-42B9-AE4A-5829AF184DCC

P2860

Q27722821-0016E76F-109F-4932-BCA8-F4D9DC4EC63C

Q27722821-014767EC-17AC-4173-9F96-969824852ECC

Q27722821-0DA99450-7E4E-4158-ABB2-970E6DCF4228

Q27722821-154A1BE9-C455-4D3A-AB84-79DCAE06F831

Q27722821-28BBF7FB-FA77-4C26-ABF9-648222419AB1

Q27722821-29F53605-2EE1-4D8B-8D8A-4ED4491292A6

Q27722821-3271097B-892E-46C0-945F-937077116ED3

Q27722821-34F5C032-8E6C-4EA2-A280-FB1E4CF5F8A8

Q27722821-3E0F7E05-4B20-4AE6-960D-DB89F4AC7B12

Q27722821-3E1556A8-ACB3-4681-9B5A-F2F7A4109EE0

P304

Q27722821-540C5ECD-8CE2-46ED-B385-FEBEA9EB3274

P31

Q27722821-A2BF00C4-6B13-4195-9CD1-F932B701B4BB

P356

Q27722821-E0E16CAD-A9AE-4283-A736-9255897234FC

P407

Q27722821-4689EC57-F164-4C9A-9F55-55C6F092BC94

P433

Q27722821-AD1D1FE8-7934-4AE6-9DF1-617F4E4D2AD7

P478

Q27722821-C8A0A210-61F7-47DF-9F80-4EFFA395BA32

P50

Q27722821-E2E3F54D-34E5-4943-BD78-C5E6248D036C

P577

Q27722821-0669A069-197E-46C7-9B71-8B88E38972F5

P698

Q27722821-0892176B-1634-4602-8005-2D4EC1A97F12

P932

Q27722821-13B0E993-0834-4441-9E44-F60BA7DD123F

P356

J.JMB.2016.07.010

P1433

Journal of Molecular Biology

P1476

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein

@en

P2093

Christos Tzitzilonis

http://www.w3.org/2001/XMLSchema#string

Innokentiy Maslennikov

http://www.w3.org/2001/XMLSchema#string

Roland Riek

http://www.w3.org/2001/XMLSchema#string

Senyon Choe

http://www.w3.org/2001/XMLSchema#string

Stuart A Lipton

http://www.w3.org/2001/XMLSchema#string

Tomohiro Nakamura

http://www.w3.org/2001/XMLSchema#string

Witek Kwiatkowski

http://www.w3.org/2001/XMLSchema#string

P2860

S-Nitrosylation activates Cdk5 and contributes to synaptic spine loss induced by beta-amyloid peptide

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

A short history of SHELX

Processing of X-ray diffraction data collected in oscillation mode

NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions

Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily

Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin

S-nitrosylation-induced conformational change in blackfin tuna myoglobin

Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli

Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP

P304

3737-3751

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.JMB.2016.07.010

http://www.w3.org/2001/XMLSchema#string

P407

P433

19

http://www.w3.org/2001/XMLSchema#string

P478

428

http://www.w3.org/2001/XMLSchema#string

P50

Cédric Eichmann

P577

2016-09-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27473602

http://www.w3.org/2001/XMLSchema#string

P932

5260856

http://www.w3.org/2001/XMLSchema#string