Work

Temperature-sensitive sarcomeric protein post-translational modifications revealed by top-down proteomics

Year: 2018

Type: article

Source: Journal of Molecular and Cellular Cardiology

DOI: 10.1016/j.yjmcc.2018.07.247

Authors: Wenxuan Cai, Zachary L. Hite, Beini Lyu, Zhijie Wu, Ziqing Lin, Zachery R. Gregorich, Andrew E. Messer, Sean J. McIlwain, Steve B. Marston, Takushi Kohmoto, Ying Ge

Institutions: University of Wisconsin–Madison, Imperial College London, University of Wisconsin Carbone Cancer Center, University of Wisconsin System

Language: English

Topic: Advanced Proteomics Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

SDG: Good health and well-being

Open Access status: green

Funders: American Heart Association, British Heart Foundation, National Institutes of Health, National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences

Awards: G1660817726, MASH Explorer, a Comprehensive Software Environment for Top-Down Proteomics, G4058825104, A Systems Biology Approach to Understand Hypertrophic Cardiomyopathy, Enabling Top-Down Proteomics through Material Chemistry and Nanotechnology, Deciphering Myofilament Modifications in Ischemic Cardiomyopathy, G650911148, G7266456259, Top-Down Proteomics of Myofilaments in Heart Failure, G836431152, RENEWAL: Molecular mechanisms by which mutations in myofibrillar proteins cause primary cardiomyopathies, Ultra High Resolution Mass Spectrometer for Biomedical Research, G9000018737

OpenAlex ID: W2883963853

FWCI: 0.649

Cites: 75

Cited by: 19

Related to: 10