Work

1H, 13C, and 15N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216–420) of a binary toxin from Clostridium difficile

Year: 2016

Type: article

Source: Biomolecular NMR Assignments

DOI: 10.1007/s12104-016-9669-8

Authors: Braden M. Roth, Raquel Godoy-Ruiz, Kristen M. Varney, Richard R. Rustandi, David J. Weber

Institutions: University of Maryland, Baltimore, Merck & Co., Inc., Rahway, NJ, USA (United States)

Language: English

Topic: Clostridium difficile and Clostridium perfringens research

Subfield: Infectious Diseases

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Science Foundation, National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Center for Research Resources

Awards: 600 MHz NMR Spectrometer Console, 600 MHZ NMR SPECTROMETER, 950 MHz NMR Spectrometer with Cryogenic Probe, Cryoprobe for a 600 Mhz NMR spectrometer, G65548561, 800 MHZ NMR SPECTROMETER, Interdisciplinary Training Program in Muscle Biology

OpenAlex ID: W2278322168

FWCI: 0.498

Cites: 10

Cited by: 5

Related to: 10