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MyoD and myogenin protein expression in skeletal muscles of senile rats [PDF]

open access: yesCell and Tissue Research, 2003
We analyzed the level of protein expression of two myogenic regulatory factors (MRFs), MyoD and myogenin, in senile skeletal muscles and determined the cellular source of their production in young adult (4 months old), old (24, 26, and 28 months old), and senile (32 months old) male rats. Immunoblotting demonstrated levels of myogenin approximately 3.2,
Eduard I Dedkov   +2 more
exaly   +4 more sources
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MyoD-family inhibitor proteins act as auxiliary subunits of Piezo channels

Science, 2023
Piezo channels are critical cellular sensors of mechanical forces. Despite their large size, ubiquitous expression, and irreplaceable roles in an ever-growing list of physiological processes, few Piezo channel–binding proteins have emerged. In this work, we found that MyoD (myoblast determination)–family inhibitor proteins (MDFIC and MDFI) are PIEZO1/2
Zijing Zhou   +15 more
openaire   +4 more sources

MyoD protein expression in Xenopus embryos closely follows a mesoderm induction-dependent amplification of MyoD transcription and is synchronous across the future somite axis

Mechanisms of Development, 1992
The MyoD-related genes code for key regulators of skeletal muscle commitment and differentiation. In this study, expression of MyoD protein has been examined during Xenopus development. Protein is first detected in presumptive mesoderm at early gastrulation, directly following a dramatic increase in MyoD transcription that occurs in response to ...
Richard P Harvey
exaly   +3 more sources

Nuclear import of the myogenic factor MyoD requires cAMP-dependent protein kinase activity but not the direct phosphorylation of MyoD

Journal of Cell Science, 1994
ABSTRACT MyoD is a nuclear phosphoprotein that belongs to the family of myogenic regulatory factors and acts in the tran-scriptional activation of muscle-specific genes. We have investigated the role of cAMP-dependent protein kinase (A-kinase) in modulating the nuclear locale of MyoD.
M, Vandromme   +5 more
openaire   +2 more sources

Transduction of MyoD protein into myoblasts induces myogenic differentiation without addition of protein transduction domain

Biochemical and Biophysical Research Communications, 2009
Protein transduction is a new technology with the potential for controlling cellular functions. Addition of tissue-specific transcription factors into cells could induce a specific differentiation pathway. In this paper, MyoD protein, a muscle-specific transcription factor, was introduced into the mouse myoblast cell line C2C12 to induce myogenic ...
Masayasu Mie
exaly   +3 more sources

Activation of Xenopus MyoD Transcription by Members of the MEF2 Protein Family

Developmental Biology, 1994
Members of the MEF2 family of DNA binding proteins interact with a set of AT-rich sequences commonly found in the promoters and enhancers of muscle-specific genes. We have shown that a MEF2 binding site precisely overlaps the TFIID binding site (TATA box) in the Xenopus MyoDa (XMyoDa) promoter and appears to play an important role in muscle-specific ...
M W, Wong   +4 more
openaire   +2 more sources

Melatonin‐induced autophagy is associated with degradation of MyoD protein in C2C12 myoblast cells

Journal of Pineal Research, 2012
Abstract:  MyoD is a muscle‐specific transcriptional factor that acts as a master switch for skeletal muscle differentiation. This protein regulates myoblast proliferation and myogenic differentiation and is also a short‐lived regulatory protein that is degraded by the ubiquitin system. However, the lysosomal pathway of MyoD protein degradation remains
Chi Hyun Kim, Yeong-Min Yoo
exaly   +3 more sources

Differential binding modes of the bromodomains of CREB-binding protein (CBP) and p300 with acetylated MyoD [PDF]

open access: yesBiochemical and Biophysical Research Communications, 2008
The recruitment of the bromodomains of CREB-binding protein (CBP) and p300 by the acetylated myogenic transcription factor MyoD was previously shown to be critical for the enhanced MyoD transcriptional activity following acetylation at its Lys99 and Lys102 positions.
Lanlan Wei, Zhenghe Wang
exaly   +3 more sources

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