Protein misassembly: macromolecular crowding and molecular chaperones.
about
Mechanisms of CFTR Folding at the Endoplasmic ReticulumExtracellular HSPs: The Complicated Roles of Extracellular HSPs in ImmunityQuality control and fate determination of Hsp90 client proteinsThe p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin statusProtein complexes are under evolutionary selection to assemble via ordered pathwaysFilming protein fibrillogenesis in real time.Human Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations.Prognostic implication of HSPA (HSP70) in breast cancer patients treated with neoadjuvant anthracycline-based chemotherapy.Deletion of the mitochondrial chaperone TRAP-1 uncovers global reprogramming of metabolic networks.Molecular chaperone dysfunction in neurodegenerative diseases and effects of curcumin.Genetic constraints on protein evolutionCoevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furinHumoral response against small heat shock proteins in Parkinson's disease.Pharmacological chaperones for misfolded gonadotropin-releasing hormone receptorsHeat shock proteins and cancer vaccines: developments in the past decade and chaperoning in the decade to comeA Chemical Biology Study of Human Pluripotent Stem Cells Unveils HSPA8 as a Key Regulator of PluripotencyMolecular chaperones in mammary cancer growth and breast tumor therapyRelative Cosolute Size Influences the Kinetics of Protein-Protein Interactions.Protein folding in confined and crowded environments.Antibodies against small heat-shock proteins in Alzheimer's disease as a part of natural human immune repertoire or activation of humoral response?Heat Shock Proteins Promote Cancer: It's a Protection RacketSpecificity in the actions of the UBR1 ubiquitin ligase in the degradation of nuclear receptors.The shock of aging: molecular chaperones and the heat shock response in longevity and aging--a mini-review.Tat-HSP22 inhibits oxidative stress-induced hippocampal neuronal cell death by regulation of the mitochondrial pathwayHSP90 manages the ends.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Postconditioning hormesis and the homeopathic Similia principle: molecular aspects.The molecular anatomy of human Hsp60 and its similarity with that of bacterial orthologs and acetylcholine receptor reveal a potential pathogenetic role of anti-chaperonin immunity in myasthenia gravis.The role of heat shock proteins in antigen cross presentation.Cellular and molecular chaperone fusion vaccines: targeting resistant cancer cell populations.Molecular cochaperones: tumor growth and cancer treatment.Role of water in protein folding, oligomerization, amyloidosis and miniprotein.Harnessing Hierarchical Nano- and Micro-Fabrication Technologies for Musculoskeletal Tissue Engineering.Purification, preparation, and use of chaperone-peptide complexes for tumor immunotherapy.Molecular Chaperone Accumulation in Cancer and Decrease in Alzheimer's Disease: The Potential Roles of HSF1.HSF1, a versatile factor in tumorogenesis.Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1Editorial: HSPs-Ambiguous Mediators of ImmunityHeat shock proteins, autoimmunity, and cancer treatment
P2860
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P2860
Protein misassembly: macromolecular crowding and molecular chaperones.
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
name
Protein misassembly: macromolecular crowding and molecular chaperones.
@ast
Protein misassembly: macromolecular crowding and molecular chaperones.
@en
Protein misassembly: macromolecular crowding and molecular chaperones.
@nl
type
label
Protein misassembly: macromolecular crowding and molecular chaperones.
@ast
Protein misassembly: macromolecular crowding and molecular chaperones.
@en
Protein misassembly: macromolecular crowding and molecular chaperones.
@nl
prefLabel
Protein misassembly: macromolecular crowding and molecular chaperones.
@ast
Protein misassembly: macromolecular crowding and molecular chaperones.
@en
Protein misassembly: macromolecular crowding and molecular chaperones.
@nl
P1476
Protein misassembly: macromolecular crowding and molecular chaperones.
@en
P2093
R John Ellis
P356
10.1007/978-0-387-39975-1_1
P407
P577
2007-01-01T00:00:00Z