Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. - Wikidata - wikimedia - TriplyDB

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

http://www.wikidata.org/entity/Q34063410

about

Dynamics of the rhomboid-like protein RHBDD2 expression in mouse retina and involvement of its human ortholog in retinitis pigmentosa Evolutionarily conserved intercalated disc protein Tmem65 regulates cardiac conduction and connexin 43 function The survival motor neuron protein forms soluble glycine zipper oligomers TMPad: an integrated structural database for helix-packing folds in transmembrane proteins Membrane protein prediction methods Bioinformatics approaches for functional annotation of membrane proteins Transmembrane Domains of Hepatitis C Virus Envelope Glycoproteins: Residues Involved in E1E2 Heterodimerization and Involvement of These Domains in Virus Entry Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1 Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases Computational design of a protein crystal Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca²⁺.Solid state NMR: The essential technology for helical membrane protein structural characterization.The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.Regulation of KCNQ/Kv7 family voltage-gated K+ channels by lipids.Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.Structure and dynamic properties of membrane proteins using NMR.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion Consensus motif for integrin transmembrane helix association Metals and cholesterol: two sides of the same coin in Alzheimer's disease pathology.Characterization of the water defect at the HIV-1 gp41 membrane spanning domain in bilayers with and without cholesterol using molecular simulations.Driving forces for transmembrane alpha-helix oligomerization.Structure elucidation of dimeric transmembrane domains of bitopic proteins Specificity for homooligomer versus heterooligomer formation in integrin transmembrane helices A Gly-zipper motif mediates homodimerization of the transmembrane domain of the mitochondrial kinase ADCK3.Interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infection Role of BNIP3 and NIX in cell death, autophagy, and mitophagy Structure of the lethal phage pinhole.Helix-packing motifs in membrane proteins.Interferon-stimulated gene ISG12b2 is localized to the inner mitochondrial membrane and mediates virus-induced cell death.Mechanisms of integral membrane protein insertion and folding A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo.C19orf12 mutation leads to a pallido-pyramidal syndrome.Transmembrane domain determinants of CD4 Downregulation by HIV-1 Vpu.Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly.Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.The directed cooperative assembly of proteorhodopsin into 2D and 3D polarized arrays.Suppressor mutations in the Glutamine Dumper1 protein dissociate disturbance in amino acid transport from other characteristics of the Gdu1D phenotype.Oligomeric Properties of Survival Motor Neuron·Gemin2 Complexes

P2860

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P2860

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

http://www.wikidata.org/entity/Q34063410

description

2005 nî lūn-bûn

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2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@ast

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@en

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@nl

type

label

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@ast

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@en

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@nl

prefLabel

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@ast

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@en

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@nl

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PNAS.0501234102

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

P1476

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.

@en

P2093

Amit Oberai

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

Duan Yang

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

Jacob J Schmidt

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James U Bowie

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

Sanguk Kim

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

Tae-Joon Jeon

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

The Protein Data Bank

Side-chain contributions to membrane protein structure and stability

Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin

A transmembrane helix dimer: structure and implications

The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel

Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum

Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel

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40

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102

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16179394

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transmembrane protein

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1242278

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