The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis - Wikidata - awgldk - TriplyDB

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis

http://www.wikidata.org/entity/Q28754755

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Defects of the Glycinergic Synapse in Zebrafish.Myosin chaperones SMYD proteins: key regulators in skeletal and cardiac muscle development and function Functions of the Hsp90 chaperone system: lifting client proteins to new heights The Myosin Chaperone UNC-45 Is Organized in Tandem Modules to Support Myofilament Formation in C. elegans Size dependent classification of heat shock proteins: a mini-review Early response of heat shock proteins to functional overload of the soleus and plantaris in rats and mice Unc45 activates Hsp90-dependent folding of the myosin motor domain Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain Rbfox-regulated alternative splicing is critical for zebrafish cardiac and skeletal muscle functions Defective glycinergic synaptic transmission in zebrafish motility mutants.Paralysis and delayed Z-disc formation in the Xenopus tropicalis unc45b mutant dicky ticker Whole transcriptome data analysis of zebrafish mutants affecting muscle development Lack of developmental redundancy between Unc45 proteins in zebrafish muscle development Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos Knockdown and overexpression of Unc-45b result in defective myofibril organization in skeletal muscles of zebrafish embryos.Analysis of skeletal muscle defects in larval zebrafish by birefringence and touch-evoke escape response assays UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.Getting folded: chaperone proteins in muscle development, maintenance and disease.Smyd1b_tv1, a key regulator of sarcomere assembly, is localized on the M-line of skeletal muscle fibers.Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome.The UNC-45 myosin chaperone: from worms to flies to vertebrates.Troponin T is essential for sarcomere assembly in zebrafish skeletal muscle.Expression of heat shock protein (Hsp90) paralogues is regulated by amino acids in skeletal muscle of Atlantic salmon.Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization.The Effects of Hsp90α1 Mutations on Myosin Thick Filament Organization The Hsp90 mosaic: a picture emerges Still Heart Encodes a Structural HMT, SMYD1b, with Chaperone-Like Function during Fast Muscle Sarcomere Assembly.Loss of function of myosin chaperones triggers Hsf1-mediated transcriptional response in skeletal muscle cells.Zebrafish models flex their muscles to shed light on muscular dystrophies.Smyd1b is required for skeletal and cardiac muscle function in zebrafish Build it up-Tear it down: protein quality control in the cardiac sarcomere.Zebrafish muscular disease models towards drug discovery.Functional analysis of slow myosin heavy chain 1 and myomesin-3 in sarcomere organization in zebrafish embryonic slow muscles.Chaperones: needed for both the good times and the bad times.Lack of Apobec2-related proteins causes a dystrophic muscle phenotype in zebrafish embryos At the Start of the Sarcomere: A Previously Unrecognized Role for Myosin Chaperones and Associated Proteins during Early Myofibrillogenesis.Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function.Differential requirements for myogenic regulatory factors distinguish medial and lateral somitic, cranial and fin muscle fibre populations The role of hair cells, cilia and ciliary motility in otolith formation in the zebrafish otic vesicle.

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P2860

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis

http://www.wikidata.org/entity/Q28754755

description

2008 nî lūn-bûn

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2008 թուականի Մարտին հրատարակուած գիտական յօդուած

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2008 թվականի մարտին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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type

label

The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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prefLabel

The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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The ATPase-dependent chaperoni ...... etal muscle myofibrillogenesis

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Anna-Pavlina Haramis

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

Cara K Vaughan

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

Chrisostomos Prodromou

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Christelle Etard

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

Laurence H Pearl

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

Martine Behra

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

Nigel Holder

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

Rachel Ashworth

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

Saikat Ray

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

Stephen W Wilson

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

P2860

Titin: a molecular control freak

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.

Striated muscle cytoarchitecture: an intricate web of form and function

Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation

Structure and mechanism of the Hsp90 molecular chaperone machinery

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

Ifm(2)2 is a myosin heavy chain allele that disrupts myofibrillar assembly only in the indirect flight muscle of Drosophila melanogaster

unc-45 gene of Caenorhabditis elegans encodes a muscle-specific tetratricopeptide repeat-containing protein.

Muscle assembly: a titanic achievement?

Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function.

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1147-56

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scholarly article

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426421

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10.1242/DEV.018150

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6

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135

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5596414

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18256191

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molecular chaperones

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2358948

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