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BRAF protein, human

Known as: v-raf murine sarcoma viral oncogene homolog B1, human, B-RAF Serine/Threonine Protein Kinase, RAFB1 Protein 
Serine/threonine-protein kinase B-raf (766 aa, ~84 kDa) is encoded by the human BRAF gene. This protein plays a role in protein phosphorylation… 
National Institutes of Health

Related topics

Related topics

27 relations
Angiogenic ProcessApoptosisBRAF geneBRAF(V600E) Kinase Inhibitor RO5212054

Broader (1)

Proto-Oncogene Proteins B-raf

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2008
Review
2008
Calpain 3, the “gatekeeper” of proper sarcomere assembly, turnover and maintenance
Highly Cited
2004
Highly Cited
2004
Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro.
The giant protein titin serves a primary role as a scaffold for sarcomere assembly; however, proteins that mediate this… 
Highly Cited
2004
Highly Cited
2004
Possible Regulation of the Conventional Calpain System by Skeletal Muscle-specific Calpain, p94/Calpain 3*
p94 (also called calpain 3) is the skeletal muscle-specific calpain and is considered to be a “modulator protease” in various… 
Highly Cited
2001
Highly Cited
2001
Active Ras induces heterodimerization of cRaf and BRaf.
Growth factor-induced signalling leads to activation of members of the Ras family and subsequent stimulation of different Raf… 
Highly Cited
1999
Highly Cited
1999
Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine longissimus muscle.
Tenderization of skeletal muscle in meat animals has been closely linked to the postmortem activity of the calpain proteolytic… 
Review
1997
Review
1997
Structure and physiological function of calpains.
For a long time now, two ubiquitously expressed mammalian calpain isoenzymes have been used to explore the structure and function… 
Highly Cited
1997
Highly Cited
1997
Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs.
Using the yeast two-hybrid system, we have recently reported that skeletal muscle-specific calpain, p94, binds specifically to… 
Highly Cited
1995
Highly Cited
1995
Muscle-specific Calpain, p94, Responsible for Limb Girdle Muscular Dystrophy Type 2A, Associates with Connectin through IS2, a p94-specific Sequence (*)
p94, a muscle-specific member of calpain family, is unique in that it undergoes rapid and exhaustive autolysis with a half-life… 
Highly Cited
1993
Highly Cited
1993
Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle.
Highly Cited
1989
Highly Cited
1989
Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle.
Two types of calcium-dependent protease with distinct calcium requirements (termed muCANP and mCANP) are known in mammalian… 
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