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Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin

Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7352323

Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin

About this item

Full title

Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin

Publisher

Switzerland: MDPI AG

Journal title

International journal of molecular sciences, 2020-06, Vol.21 (12), p.4285

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

In striated muscle the extent of the overlap between actin and myosin filaments contributes to the development of force. In slow twitch muscle fibers actin filaments are longer than in fast twitch fibers, but the mechanism which determines this difference is not well understood. We hypothesized that tropomyosin isoforms Tpm1.1 and Tpm3.12, the acti...

Alternative Titles

Full title

Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7352323

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7352323

Other Identifiers

ISSN

1422-0067,1661-6596

E-ISSN

1422-0067

DOI

10.3390/ijms21124285

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