C
Cami K. Bruns
Researcher at Scripps Research Institute
Publications - 6
Citations - 722
Cami K. Bruns is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Protein folding & Superoxide dismutase. The author has an hindex of 6, co-authored 6 publications receiving 690 citations. Previous affiliations of Cami K. Bruns include Stanford University.
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Journal ArticleDOI
Nickel superoxide dismutase structure and mechanism.
David P. Barondeau,Carey J. Kassmann,Cami K. Bruns,Cami K. Bruns,John A. Tainer,Elizabeth D. Getzoff +5 more
TL;DR: The 1.30 A resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site that provides almost all interactions critical for metal binding and catalysis, and thus will likely be diagnostic of NiSODs.
Journal ArticleDOI
ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization
Michael DiDonato,Lisa Craig,Mary E. Huff,Maria M. Thayer,Rosa M.F. Cardoso,Carey J. Kassmann,Terence P. Lo,Terence P. Lo,Cami K. Bruns,Cami K. Bruns,Evan T. Powers,Jeffery W. Kelly,Elizabeth D. Getzoff,John A. Tainer +13 more
TL;DR: Characterizations of beta-barrel (H43R) and dimer interface (A4V) FALS mutants reveal reduced stability and drastically increased aggregation propensity, and electron and atomic force microscopy indicate that these defects promote the formation of filamentous aggregates.
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Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase.
Rosa M.F. Cardoso,Maria M. Thayer,Michael DiDonato,Terence P. Lo,Cami K. Bruns,Cami K. Bruns,Elizabeth D. Getzoff,John A. Tainer +7 more
TL;DR: It is argued that architectural destabilization of the HSOD protein may underlie the toxic function of the many HSOD FALS mutations.
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Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants.
Cami K. Bruns,Ron R. Kopito +1 more
TL;DR: It is reported that, despite being a small, single‐domain protein, human SOD1 folds post‐translationally to a hyperstable native‐like conformation without a requirement for ATP‐dependent molecular chaperones, and this model is suggested to provide an important source of proto‐toxic protein.
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Structural, Functional, and Immunogenic Insights on Cu,Zn Superoxide Dismutase Pathogenic Virulence Factors from Neisseria meningitidis and Brucella abortus
Ashley J. Pratt,Ashley J. Pratt,Michael DiDonato,David S. Shin,David S. Shin,Diane E. Cabelli,Cami K. Bruns,Carol A. Belzer,Andrew Gorringe,Paul R. Langford,Louisa B. Tabatabai,J. Simon Kroll,John A. Tainer,John A. Tainer,Elizabeth D. Getzoff +14 more
TL;DR: The identified functional contributions, motifs, and targets distinguishing bacterial and eukaryotic SOD assemblies presented here provide a foundation for efforts to develop SOD-specific inhibitors of or vaccines against these harmful pathogens.