Nonuniform Rates of Turnover of Myofibrillar Proteins in Rat Diaphragm

Overview

Journal J Cell Biol

Specialty Cell Biology

Date 1973 Feb 1

PMID 4682905

Citations 9

Authors

R B Low

A L GOLDBERG

Affiliations

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Citing Articles

Isolation of human skeletal muscle myosin heavy chain and actin for measurement of fractional synthesis rates.

Hasten D, Morris G, Ramanadham S, Yarasheski K Am J Physiol. 1998; 275(6):E1092-9.

PMID: 9843753 PMC: 4139966. DOI: 10.1152/ajpendo.1998.275.6.E1092.

The reorganization of subcellular structure in muscle undergoing fast-to-slow type transformation. A stereological study.

Eisenberg B, Salmons S Cell Tissue Res. 1981; 220(3):449-71.

PMID: 7296641 DOI: 10.1007/BF00216750.

Myofibrillar protein turnover. Synthesis of protein-bound 3-methylhistidine, actin, myosin heavy chain and aldolase in rat skeletal muscle in the fed and starved states.

Bates P, Grimble G, Sparrow M, Millward D Biochem J. 1983; 214(2):593-605.

PMID: 6615482 PMC: 1152286. DOI: 10.1042/bj2140593.

Evidence for the lack of feedback regulation of gene activity and for the absence of subunit exchange between lactate dehydrogenase tetramers in vivo.

Nadal-Ginard B Proc Natl Acad Sci U S A. 1976; 73(10):3618-22.

PMID: 1086475 PMC: 431169. DOI: 10.1073/pnas.73.10.3618.

Protein turnover in the smooth muscle cell of the aortic tunica media as visualized by radioautography.

Terquem A, Dadoune J Cell Tissue Res. 1977; 183(1):91-104.

PMID: 922831 DOI: 10.1007/BF00219994.

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