C
Carrie A. Hughes
Researcher at University of California, San Diego
Publications - 5
Citations - 324
Carrie A. Hughes is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Protein subunit & Binding site. The author has an hindex of 5, co-authored 5 publications receiving 319 citations.
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Journal ArticleDOI
Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
TL;DR: The epitope of a monoclonal antibody raised against human thrombin has been determined by hydrogen/deuterium exchange coupled to MALDI mass spectrometry and turned out to be the more structured of two surface regions in which higher sequence variation between the three species is seen.
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Amide H/2H Exchange Reveals Communication Between the cAMP and Catalytic Subunit-binding Sites in the RIα Subunit of Protein Kinase A
TL;DR: The results suggest that the mutually exclusive binding of either cAMP or C-subunit is controlled by binding at one site transmitting long distance changes to the other site.
Journal ArticleDOI
Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB.
Carrie A. Hughes,Jeffrey G. Mandell,Ganesh S. Anand,Ganesh S. Anand,Ann M. Stock,Ann M. Stock,Ann M. Stock,Elizabeth A. Komives +7 more
TL;DR: Comparison with results from the isolated catalytic domain-containing C-terminal fragment of CheB showed that the increased solvent accessibility was less than would have occurred upon detachment of the regulatory domain.
Journal ArticleDOI
Solvent Exposed Non-contacting Amino Acids Play a Critical Role in NF-κB/IκBα Complex Formation
Tom Huxford,Dennis Mishler,Christopher B. Phelps,De-Bin Huang,Lei Lei Sengchanthalangsy,Ryan Reeves,Carrie A. Hughes,Elizabeth A. Komives,Gourisankar Ghosh +8 more
TL;DR: X-ray crystallographic and solvent accessibility experiments suggest that these solvent-exposed amino acid residues contribute to NF-κB/IκBα complex formation by modulating the NF-σκB p65 subunit NLS polypeptide.
ComponentDOI
NF-kappaB p65 subunit dimerization domain homodimer N202R mutation
T. Huxford,D. Mishler,Christopher B. Phelps,De-Bin Huang,Lei Lei Sengchanthalangsy,Ryan Reeves,Carrie A. Hughes,Elizabeth A. Komives,G. Ghosh +8 more
TL;DR: X-ray crystallographic and solvent accessibility experiments suggest that these solvent-exposed amino acid residues contribute to NF-kappaB/IkappaBalpha complex formation by modulating the NF- kappaB p65 subunit NLS polypeptide.