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Polar residues drive association of polyleucine transmembrane helices

Polar residues drive association of polyleucine transmembrane helices

http://www.wikidata.org/entity/Q34449670

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The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum Quantification of helix-helix binding affinities in micelles and lipid bilayers Predicting helix-helix interactions from residue contacts in membrane proteins How, with whom and when: an overview of CD147-mediated regulatory networks influencing matrix metalloproteinase activity Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation Oligomerization of the {gamma}-aminobutyric acid transporter-1 is driven by an interplay of polar and hydrophobic interactions in transmembrane helix II Structure and inhibition of the SARS coronavirus envelope protein ion channel Role of the conserved glutamine 291 in the rat gamma-aminobutyric acid transporter rGAT-1 β-Subunit of the Ostα-Ostβ organic solute transporter is required not only for heterodimerization and trafficking but also for function Ser/Thr motifs in transmembrane proteins: conservation patterns and effects on local protein structure and dynamics Comparison of helix interactions in membrane and soluble alpha-bundle proteins.Membrane protein folding: beyond the two stage model.Multipass membrane protein structure prediction using Rosetta The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.Polar residues and their positional context dictate the transmembrane domain interactions of influenza A neuraminidases.Comparison of fragments comprising the first two helices of the human Y4 and the yeast Ste2p G-protein-coupled receptors The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site.Rotational orientation of monomers within a designed homo-oligomer transmembrane helical bundle.In vitro selection of membrane-spanning leucine zipper protein-protein interaction motifs using POSSYCCAT.Conformation and environment of channel-forming peptides: a simulation study Synthesis and biophysical characterization of a multidomain peptide from a Saccharomyces cerevisiae G protein-coupled receptor.Evidence for assembly of small multidrug resistance proteins by a "two-faced" transmembrane helix.Packing contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor.Predicting transmembrane helix packing arrangements using residue contacts and a force-directed algorithm Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulum The activating NKG2D receptor assembles in the membrane with two signaling dimers into a hexameric structure.Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ The Calpha ---H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions.Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants Driving forces for transmembrane alpha-helix oligomerization.Structure elucidation of dimeric transmembrane domains of bitopic proteins Model of a putative pore: the pentameric alpha-helical bundle of SARS coronavirus E protein in lipid bilayers.Topology, dimerization, and stability of the single-span membrane protein CadC Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein.The organizing principle in the formation of the T cell receptor-CD3 complex.Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer.

P2860

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P2860

Polar residues drive association of polyleucine transmembrane helices

http://www.wikidata.org/entity/Q34449670

description

2001 nî lūn-bûn

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2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի փետրվարին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

@zh-hant

2001年論文

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2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Polar residues drive association of polyleucine transmembrane helices

@ast

Polar residues drive association of polyleucine transmembrane helices

@en

Polar residues drive association of polyleucine transmembrane helices

@nl

type

label

Polar residues drive association of polyleucine transmembrane helices

@ast

Polar residues drive association of polyleucine transmembrane helices

@en

Polar residues drive association of polyleucine transmembrane helices

@nl

prefLabel

Polar residues drive association of polyleucine transmembrane helices

@ast

Polar residues drive association of polyleucine transmembrane helices

@en

Polar residues drive association of polyleucine transmembrane helices

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Polar residues drive association of polyleucine transmembrane helices

@en

P2093

D M Engelman

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

F X Zhou

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

H J Merianos

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

P2860

Structure of bacteriorhodopsin at 1.55 A resolution

Structural changes linked to proton translocation by subunit c of the ATP synthase

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

Crystal structure of rhodopsin: A G protein-coupled receptor

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices

Transmembrane structure of an inwardly rectifying potassium channel.

TOXCAT: a measure of transmembrane helix association in a biological membrane

Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins.

Modelling G-protein-coupled receptors for drug design.

P304

2250-2255

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scholarly article

P356

10.1073/PNAS.041593698

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5

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P478

98

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Axel T. Brunger

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2001-02-13T00:00:00Z

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transmembrane protein

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30124

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