Nanomolar ATP binding to single myosin cross-bridges in rigor: a molecular approach to studying myosin ATP kinetics using single human cardiomyocytes.

ATP analogues ATP-binding kinetics Human heart cardiomyocytes SMLM Single molecule imaging of ATP TIRF microscopy

Journal

Biophysical reviews
ISSN: 1867-2450
Titre abrégé: Biophys Rev
Pays: Germany
ID NLM: 101498573

Informations de publication

Date de publication:
Aug 2020
Historique:
received: 17 06 2020
accepted: 02 07 2020
pubmed: 11 7 2020
medline: 11 7 2020
entrez: 11 7 2020
Statut: ppublish

Résumé

Our knowledge in the field of cardiac muscle and associated cardiomyopathies has been evolving incrementally over the past 60 years and all was possible due to the parallel progress in techniques and methods allowing to take a fresh glimpse at an old problem. Here, we describe an exciting tool used to examine the various states of the human cardiac myosin at the single molecule level. By imaging single Alexa

Identifiants

pubmed: 32648209
doi: 10.1007/s12551-020-00716-2
pii: 10.1007/s12551-020-00716-2
pmc: PMC7429591
doi:

Types de publication

Journal Article Review

Langues

eng

Pagination

1031-1040

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Auteurs

Elvis Pandzic (E)

Biomedical Imaging Facility, Mark Wainwright Analytical Centre, University of New South Wales, Kensington, 2052, Australia. e.pandzic@unsw.edu.au.

Christian A Morkel (CA)

Victor Chang Cardiac Research Institute, Molecular Cardiology Group, Darlinghurst, NSW, 2020, Australia.

Amy Li (A)

Department of Pharmacy & Biomedical Sciences, La Trobe University, Bendigo, 3552, Australia.

Roger Cooke (R)

Department of Biochemistry, University of California, San Francisco, CA, 94158, USA.

Renee M Whan (RM)

Biomedical Imaging Facility, Mark Wainwright Analytical Centre, University of New South Wales, Kensington, 2052, Australia.

Cristobal G Dos Remedios (CG)

Victor Chang Cardiac Research Institute, Molecular Cardiology Group, Darlinghurst, NSW, 2020, Australia.

Classifications MeSH