Publication Date:
1991-03-01
Description:
The challenge presented by myofibril assembly in striated muscle is to understand the molecular mechanisms by which its protein components are arranged at each level of organization. Recent advances in the genetics and cell biology of muscle development have shown that in vivo assembly of the myofilaments requires a complex array of structural and associated proteins and that organization of whole sarcomeres occurs initially at the cell membrane. These studies have been complemented by in vitro analyses of the renaturation, polymerization, and three-dimensional structure of the purified proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Epstein, H F -- Fischman, D A -- AR-32147/AR/NIAMS NIH HHS/ -- GM-33223/GM/NIGMS NIH HHS/ -- HL-42267/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1039-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1998120" target="_blank"〉PubMed〈/a〉
Keywords:
Actins/physiology
;
Amino Acid Sequence
;
Animals
;
Macromolecular Substances
;
Molecular Sequence Data
;
Morphogenesis
;
Muscle Contraction
;
*Muscle Development
;
Muscle Proteins/*physiology
;
Myofibrils/*physiology
;
Myosins/physiology
;
Polymers
;
Sarcolemma/physiology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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