about
Scratching the surface: actin' and other roles for the C-terminal Eps15 homology domain protein, EHD2Lack of correlation between outcomes of membrane repair assay and correction of dystrophic changes in experimental therapeutic strategy in dysferlinopathyPOPDC1(S201F) causes muscular dystrophy and arrhythmia by affecting protein traffickingEffects of delayed NSAID administration after experimental eccentric contraction injury – A cellular and proteomics studyDysferlin regulates cell membrane repair by facilitating injury-triggered acid sphingomyelinase secretion.Sarcolemmal repair is a slow process and includes EHD2.Expression levels of sarcolemmal membrane repair proteins following prolonged exercise training in miceDysferlin-deficient immortalized human myoblasts and myotubes as a useful tool to study dysferlinopathy.GRAF1 deficiency blunts sarcolemmal injury repair and exacerbates cardiac and skeletal muscle pathology in dystrophin-deficient mice.GRAF1 promotes ferlin-dependent myoblast fusionAnnexin A1 Deficiency does not Affect Myofiber Repair but Delays Regeneration of Injured Muscles.Calcium signaling in membrane repair.Phosphatidylserine directly and positively regulates fusion of myoblasts into myotubes.EHD1 mediates vesicle trafficking required for normal muscle growth and transverse tubule development.Muscle cell communication in development and repair.A novel dysferlin mutant pseudoexon bypassed with antisense oligonucleotides.Disrupted prenatal RNA processing and myogenesis in congenital myotonic dystrophy.Myoferlin regulates epithelial cancer cell plasticity and migration through autocrine TGF-β1 signaling.Sequencing of Supernumerary Chromosomes of Red Fox and Raccoon Dog Confirms a Non-Random Gene Acquisition by B Chromosomes
P2860
Q26827254-3C23911D-4078-4E86-968E-31ABC91755B7Q27301945-2B1F45EB-7ABF-4F77-8FC4-FC592C352512Q27332394-52215773-7729-4F86-B617-0B977E1EC5E9Q29248906-A95674E3-43C5-4839-A1AA-0C19C2A3F668Q30582564-BC848AD1-94C2-423D-B94F-B23B13E742E8Q31063871-E2B6413C-8647-447E-B606-07EF4DA0F74FQ33878140-A42F302D-13C6-4803-9189-545DA13D764BQ34172739-E5C1123A-47A6-44A8-942D-C92BE00CAF68Q35753474-8513B3B7-021B-4565-BA0B-0366B48489ACQ35949289-E0A87C55-1BC8-426D-8139-C3DCB6F5B900Q36369804-BC69430C-C2FD-4F2C-BCBB-6B82BB0054F0Q38620889-7BDC27DD-691A-4CF8-B295-F274FAEB035AQ38738830-DDDD5A92-8A86-4C30-940D-755D72FB2D18Q38768174-E57E056B-5670-45F6-BE48-A1C09B5DB494Q39248771-E235A7C9-751D-46C6-826F-7D5447956528Q41877911-F3289855-805F-455A-A97D-B30782E1AB6AQ47154610-1B8A0109-841B-47D1-B3D6-E24039D3C895Q52714350-55267EE2-13E4-47F4-8AB5-EB6D7B39F6F7Q58789479-A0BD4943-E9B2-49A8-8075-23671ED49807
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Ferlin proteins in myoblast fusion and muscle growth.
@en
Ferlin proteins in myoblast fusion and muscle growth.
@nl
type
label
Ferlin proteins in myoblast fusion and muscle growth.
@en
Ferlin proteins in myoblast fusion and muscle growth.
@nl
prefLabel
Ferlin proteins in myoblast fusion and muscle growth.
@en
Ferlin proteins in myoblast fusion and muscle growth.
@nl
P2860
P1476
Ferlin proteins in myoblast fusion and muscle growth
@en
P2093
Avery D Posey
Elizabeth M McNally
P2860
P304
P356
10.1016/B978-0-12-385940-2.00008-5
P577
2011-01-01T00:00:00Z