Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange - Wikidata - wikimedia - TriplyDB

Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange

Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange

http://www.wikidata.org/entity/Q33373955

about

Mechanisms of amyloid formation revealed by solution NMR Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Automation of peak-tracking analysis of stepwise perturbed NMR spectra.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Binding dynamics and energetic insight into the molecular forces driving nucleotide binding by guanylate kinase.Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation.

P2860

Q26797492-F9E2EEEA-9EC7-463F-B977-B21ADF37E5F9 Q37877295-1DF0CAFA-1259-4DD6-8086-86F72CDD359C Q38954411-8735A814-F341-4C46-A4EA-88026F44AEC3 Q39494899-448EDB3C-2E49-4D21-9325-D8ABD9C395EB Q39777395-D07EB758-9455-446C-A5FA-281DE763B1D4 Q43127628-FE81430A-681A-4289-BF4F-AFC1304BA29C Q43233916-20DAB46E-449C-4111-A09C-A489B130BA15 Q54735249-0F50F8CA-7512-4CEC-B1CA-26FE5E271818

P2860

Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange

http://www.wikidata.org/entity/Q33373955

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին 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

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@ast

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@en

type

label

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@ast

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@en

prefLabel

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@ast

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@en

P1433

Q33373955-593FCA19-6DC0-41BE-A80C-68050B912EB2

P1476

Q33373955-FB2655CA-61A1-4C5D-B6EF-A6D75639E7DA

P2093

Q33373955-14A3015F-0420-472A-836B-76BEEB045D85

Q33373955-36F389DF-F952-4E8E-8C2A-1D6553819216

Q33373955-377C640C-F4A9-4C45-8555-45C2A5249A12

Q33373955-5A661160-11E7-403A-B1D8-52654E4EBC3A

Q33373955-9E13B5E5-C54C-4934-BFEC-13E4E9CBEB05

P2860

Q33373955-093AB8FF-4689-4B37-B355-371B1B26ED45

Q33373955-1B085CFB-E939-4C86-A72C-01731FA3B5C0

Q33373955-1DCE0A98-5265-4857-9407-72DBE363386B

Q33373955-2D49EBC4-7EF5-445C-9809-3B84F1C2AC9B

Q33373955-35288391-7874-4990-8E22-B0E4A296F22C

Q33373955-389E7C2F-03E4-440A-8C60-FAD53FC1A581

Q33373955-3C976678-3A61-48DB-9F55-C8D85085AA29

Q33373955-4390D983-0340-4B25-B8D8-6922834F9D26

Q33373955-46570296-E641-49EA-B7B2-1486CE04C953

Q33373955-5182600F-8596-41B0-AB08-176DA47775F8

P304

Q33373955-EA08B3BF-5D0A-4C24-B323-019226889C53

P31

Q33373955-7A7A4BC0-948D-403F-AB89-DE46216F1F34

P356

Q33373955-92A65B77-CBDD-4F28-AFAD-B81336C1B2A9

P407

Q33373955-5BF0B509-A2F9-47D8-9DA5-492719A348AF

P433

Q33373955-EED405F2-4C29-46C6-82E6-D219D0D19392

P478

Q33373955-5644D5BE-1DEC-44FD-A130-887D3BC17002

P50

Q33373955-01361CDE-AEB4-4D5C-AD2E-7965FCD4CA65

Q33373955-2FC02158-1C15-40E9-89D4-6DAFFE0F2A7F

Q33373955-7A4FD78B-55B3-4784-B1F9-7BA5EF468F3E

P577

Q33373955-1777A7A0-2B2A-4305-9D2E-9B832FF203BB

P5875

Q33373955-1285CEBA-2A23-491D-A46C-8D0DD51173CB

P698

Q33373955-D59EA4F7-DDB6-4803-BE96-D49A3DE302B1

P932

Q33373955-4F999A0E-73E1-4F41-A19A-37F3087E89EC

P356

BIOPHYSJ.108.142448

P1433

Biophysical Journal

P1476

Equilibrium unfolding thermody ...... ough native-state H/D exchange

@en

P2093

Enrico Rennella

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

Gennaro Esposito

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

Monica Stoppini

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

Paolo Viglino

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

Sofia Giorgetti

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

P2860

Structure of the human class I histocompatibility antigen, HLA-A2

The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic properties

High-resolution crystal structure of beta2-microglobulin formed at pH 7.0

The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties

MOLMOL: a program for display and analysis of macromolecular structures

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Primary structure effects on peptide group hydrogen exchange

Comparisons of pressure and temperature activation parameters for amide hydrogen exchange in T4 lysozyme.

Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin.

P304

169-179

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

P31

scholarly article

P356

10.1529/BIOPHYSJ.108.142448

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

P407

P433

1

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

P478

96

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

P50

Alessandra Corazza

Federico Fogolari

P577

2009-01-01T00:00:00Z

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

P5875

23300417

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

P698

18835891

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

P932

2710044

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