about
A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomesAsparaginase treatment side-effects may be due to genes with homopolymeric Asn codons (Review-Hypothesis)Structural Flexibility of the Macrophage Dengue Virus Receptor CLEC5ACrystal structure of Lyme disease antigen outer surface protein A complexed with an FabCalcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeastCardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils.Trinucleotide repeats: a structural perspectiveIntrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity.How are close residues of protein structures distributed in primary sequence?Polyglutamine pathogenesis.Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases.Amyloid structure: conformational diversity and consequences.Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.A skeletal muscle ryanodine receptor interaction domain in triadinPolyglutamine fibrillogenesis: the pathway unfoldsA compact beta model of huntingtin toxicity.Dynamics of potentiation and activation: GAGA factor and its role in heat shock gene regulation.Side-chain interactions determine amyloid formation by model polyglutamine peptides in molecular dynamics simulations.Building specificity with nonspecific RNA-binding proteins.A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors.Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregatesBreaking symmetry in protein dimers: designs and functions.Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains.Aggregation formation in the polyglutamine diseases: protection at a cost?Comparative analysis of amino acid repeats in rodents and humans.Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect.Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin.Trinucleotide repeats and long homopeptides in genes and proteins associated with nervous system disease and development.Mechanisms of amyloid fibril formation--focus on domain-swapping.Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins.SHOC2 subcellular shuttling requires the KEKE motif-rich region and N-terminal leucine-rich repeat domain and impacts on ERK signalling.Discovery of Therapeutic Approaches for Polyglutamine Diseases: A Summary of Recent Efforts.A proline-rich region with a highly periodic sequence in Streptococcal beta protein adopts the polyproline II structure and is exposed on the bacterial surface.Human beta-synuclein rendered fibrillogenic by designed mutations.Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations.Solution structure of the heterotrimeric complex between the interaction domains of RFX5 and RFXAP from the RFX gene regulatory complex.A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues.Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease.
P2860
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P2860
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Polar zippers: their role in human disease.
@ast
Polar zippers: their role in human disease.
@en
type
label
Polar zippers: their role in human disease.
@ast
Polar zippers: their role in human disease.
@en
prefLabel
Polar zippers: their role in human disease.
@ast
Polar zippers: their role in human disease.
@en
P2860
P356
P1433
P1476
Polar zippers: their role in human disease.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560031002
P577
1994-10-01T00:00:00Z