J
John E. Straub
Researcher at Boston University
Publications - 222
Citations - 23553
John E. Straub is an academic researcher from Boston University. The author has contributed to research in topics: Vibrational energy relaxation & Fibril. The author has an hindex of 56, co-authored 215 publications receiving 21519 citations. Previous affiliations of John E. Straub include California State University & University of Maryland, College Park.
Papers
More filters
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
Classical and modern methods in reaction rate theory
TL;DR: In this article, the determination des constantes de vitesses dans les gaz and les liquides is discussed. And the methodes theoriques and techniques numeriques for des systemes isoles ou dans des solvants are presented.
Journal ArticleDOI
Monomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock–lock mechanism
TL;DR: The dock–lock mechanism should be a generic mechanism for growth of oligomers of amyloidogenic peptides, and surprisingly, the mobile structured oligomers undergo large conformational changes in order to accommodate the added monomer.
Journal ArticleDOI
Role of water in protein aggregation and amyloid polymorphism.
TL;DR: Evidence is offered that a two-step model, similar to that postulated for protein crystallization, must also hold for higher order amyloid structure formation starting from N*.
Journal ArticleDOI
Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis
Phuong H. Nguyen,Ayyalusamy Ramamoorthy,Bikash R. Sahoo,Jie Zheng,Peter Faller,John E. Straub,Laura Dominguez,Joan-Emma Shea,Nikolay V. Dokholyan,Alfonso De Simone,Alfonso De Simone,Buyong Ma,Buyong Ma,Ruth Nussinov,Saeed Najafi,Son Tung Ngo,Antoine Loquet,Mara Chiricotto,Pritam Ganguly,James McCarty,Mai Suan Li,Carol K. Hall,Yiming Wang,Yifat Miller,Simone Melchionna,Birgit Habenstein,Stepan Timr,Jiaxing Chen,Brianna Hnath,Birgit Strodel,Rakez Kayed,Sylvain Lesné,Guanghong Wei,Fabio Sterpone,Andrew J. Doig,Philippe Derreumaux,Philippe Derreumaux +36 more
TL;DR: In this paper, the authors review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease, Parkinson's disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research.