C
C. Mattos
Researcher at University of Maryland, Baltimore
Publications - 4
Citations - 13173
C. Mattos is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Biology & HRAS. The author has an hindex of 1, co-authored 1 publications receiving 12333 citations.
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Journal ArticleDOI
All-atom empirical potential for molecular modeling and dynamics studies of proteins.
Alexander D. MacKerell,D. Bashford,M. Bellott,Roland L. Dunbrack,Jeffrey D. Evanseck,Martin J. Field,Stefan Fischer,Jiali Gao,H. Guo,S. Ha,Diane Joseph-McCarthy,L. Kuchnir,K. Kuczera,F. T. K. Lau,C. Mattos,Stephen W. Michnick,Thien H. Ngo,D. T. Nguyen,B. Prodhom,W. E. Reiher,Benoît Roux,M. Schlenkrich,Jeremy C. Smith,Roland H. Stote,John E. Straub,Masakatsu Watanabe,J. Wiórkiewicz-Kuczera,D. Yin,Martin Karplus +28 more
TL;DR: The results demonstrate that use of ab initio structural and energetic data by themselves are not sufficient to obtain an adequate backbone representation for peptides and proteins in solution and in crystals.
Journal ArticleDOI
Computational studies of the principle of dynamic-change-driven protein interactions.
TL;DR: In this article , an example of how protein-protein interaction (binding of Ras to the Ras binding domain [RBD] of the effector protein Raf) affects a subsequent protein association process by quenching Ras internal motions through dynamic allostery.
Journal ArticleDOI
Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas and NRas.
Alicia Y. Volmar,Hugo Guterres,Hao Zhou,Derion Reid,Spiro Pavlopoulos,Lee Makowski,C. Mattos +6 more
TL;DR: In this article , the authors use accelerated molecular dynamics simulations consistent with solution x-ray scattering experiments to elucidate mechanisms through which isoform-specific residues associated with each Ras isoform affects functionally important regions connected to the active site.
Posted ContentDOI
Allosteric site variants affect GTP hydrolysis on RAS
TL;DR: In this paper , the relationship between intrinsic GTP hydrolysis on HRAS and the position of helix 3 and loop 7 through manipulation of the allosteric site was explored, showing that the two sites are functionally connected.