NMR studies of membrane proteins. - Wikidata - wikimedia - TriplyDB

NMR studies of membrane proteins.

NMR studies of membrane proteins.

http://www.wikidata.org/entity/Q37140814

about

Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1.NMR in drug discovery on membrane proteins.

P2860

Q37781488-0E4DE032-3544-4A8E-A337-EB55CD5CD571 Q38008722-93D4B349-B5B9-4827-97C5-4B09584841C7

P2860

NMR studies of membrane proteins.

http://www.wikidata.org/entity/Q37140814

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on January 2010

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

NMR studies of membrane proteins.

@en

NMR studies of membrane proteins.

@nl

type

label

NMR studies of membrane proteins.

@en

NMR studies of membrane proteins.

@nl

prefLabel

NMR studies of membrane proteins.

@en

NMR studies of membrane proteins.

@nl

P1433

Q37140814-0CF3512C-38FF-42E5-B6D2-08A390F0FFEE

P1476

Q37140814-41878057-BA5E-47CB-B9C1-0A06514C9E34

P2093

Q37140814-2909B8E3-6B2C-4FC7-A178-3C8BB48B3569

Q37140814-37A1F943-B9FA-4955-A32D-8736A34F37D4

P2860

Q37140814-0C16D12C-6DCA-4BC1-8EB1-C1AAE7EEE9A3

Q37140814-191363C5-D653-45EC-A486-AF33E6734BE3

Q37140814-2293C2FE-5D64-468A-BF2A-846423063B58

Q37140814-22F6475C-4909-4953-8357-D026846DA743

Q37140814-28448798-1161-4AA4-9822-CB781AE80053

Q37140814-2BFA25AF-C0C3-4479-96AA-189A1F5B4DBB

Q37140814-407FD740-A155-437E-9A3D-4E384B5370F3

Q37140814-447E055F-2090-42F7-892A-0B58853AF499

Q37140814-491DDC4D-3A5F-4CF2-B834-23DFFBEB5B10

Q37140814-497934ED-0375-447A-AB1A-4C33448B0762

P304

Q37140814-D3BA67D6-EAC5-4485-A4C5-E818AA74395A

P31

Q37140814-5A3A7F2B-5C93-47A1-ABAD-F8FAD50B8095

P356

Q37140814-5A41A606-8C35-4224-B089-D24CE2EE47AF

P407

Q37140814-4479BA2A-9739-4BEA-AD09-F4C56FFBFEF7

P478

Q37140814-54DC2EF9-9AAF-47CD-A368-2CAE84B68FCD

P577

Q37140814-BDAF92C3-D75B-46D8-9687-270BCE3F5D45

P698

Q37140814-6E7E245E-DBAD-4E65-9CEF-FBC549760DF6

P932

Q37140814-AB16565A-0833-42BA-A09C-FEA061BA40E6

P356

978-1-60761-700-6_14

P1433

Methods in Molecular Biology

P1476

NMR studies of membrane proteins.

@en

P2093

Gabriel A Cook

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

Stanley J Opella

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

P2860

Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers

Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy

Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles

Structure of the transmembrane region of the M2 protein H+ channel

Structure of the Rhodobacter sphaeroides light-harvesting 1 beta subunit in detergent micelles

Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints

NMR structure and backbone dynamics of the extended second transmembrane domain of the human neuronal glycine receptor alpha1 subunit

NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles

Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1

NMR structure and dynamics of the second transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit

P304

263-275

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

P31

scholarly article

P356

10.1007/978-1-60761-700-6_14

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

P407

P478

637

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

P577

2010-01-01T00:00:00Z

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

P698

20419440

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

P932

3760502

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