T
Teresita Silva
Researcher at University of Medicine and Dentistry of New Jersey
Publications - 10
Citations - 426
Teresita Silva is an academic researcher from University of Medicine and Dentistry of New Jersey. The author has contributed to research in topics: Triple helix & Protein structure. The author has an hindex of 10, co-authored 10 publications receiving 382 citations. Previous affiliations of Teresita Silva include Rutgers University & Center for Advanced Biotechnology and Medicine.
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Journal ArticleDOI
Mechanism of Stabilization of a Bacterial Collagen Triple Helix in the Absence of Hydroxyproline
Angela Mohs,Teresita Silva,Takeshi Yoshida,Ravish Amin,Slawomir Lukomski,Masayori Inouye,Barbara Brodsky +6 more
TL;DR: The high enthalpic contribution to the stability of the Scl2 collagenous domain supports the presence of a hydration network in the absence of Hyp, and the degree of electrostatic stabilization observed for SCl2 was similar to the contribution Hyp makes to the Stability of mammalian collagens.
Journal ArticleDOI
Self-association of streptococcus pyogenes collagen-like constructs into higher order structures.
Ayumi Yoshizumi,Zhuoxin Yu,Teresita Silva,Geetha Thiagarajan,John A. M. Ramshaw,Masayori Inouye,Barbara Brodsky +6 more
TL;DR: Although this S. pyogenes collagen‐like protein is a cell surface protein with no indication of participation in higher order structure, the triple‐helix domain has the potential of forming fibrillar structures even in the absence of hydroxyproline, which suggests bacterial collagen proteins may be useful for biomaterials and tissue engineering applications.
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Self-Assembly of Left- and Right-Handed Molecular Screws
Fei Xu,I. John Khan,Kenneth N. McGuinness,Avanish S. Parmar,Teresita Silva,N. Sanjeeva Murthy,Vikas Nanda +6 more
TL;DR: A geometric ridges-in-grooves model of interacting helices indicates that heterochiral associations should generally be favored in this class of structures, and tested this principle using a collagen peptide triple-helix.
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Computational design of a collagen A:B:C-type heterotrimer.
TL;DR: The power of automated computational design is highlighted, providing model systems to probe the biophysics of collagen assembly and developing general methods for the design of fibrous proteins.
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Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders.
TL;DR: Peptide studies raise the possibility that mutant collagen could fold in a C to N direction in a zipper-like manner up to the mutation site and that completion of the triple helix N-terminal to the mutations would involve an alternative mechanism.