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Roger L. Williams

Researcher at Laboratory of Molecular Biology

Publications -  188
Citations -  25758

Roger L. Williams is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Protein subunit & ESCRT. The author has an hindex of 75, co-authored 188 publications receiving 22360 citations. Previous affiliations of Roger L. Williams include Stoke Mandeville Hospital & University of California, Riverside.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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A Pharmacological Map of the PI3-K Family Defines a Role for p110α in Insulin Signaling

Zachary A. Knight, +13 more
- 19 May 2006 - 
TL;DR: It is found that p110alpha is the primary insulin-responsive PI3-K in cultured cells, whereas p110beta is dispensable but sets a phenotypic threshold for p110 alpha activity, which illustrates systematic target validation using a matrix of inhibitors that span a protein family.
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Structural Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, LY294002, Quercetin, Myricetin, and Staurosporine

Edward H. Walker, +6 more
- 01 Oct 2000 - 
TL;DR: Interestingly, LY294002 and the lead compound on which it was designed, quercetin, as well as the closely related flavonoid myricetin bind PI3K in remarkably different orientations that are related to each other by 180 degrees rotations.
Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA

Alfredo Jacobo-Molina, +9 more
- 01 Jul 1993 - 
TL;DR: The structure of the HIV-1 RT/DNA/Fab complex should aid the understanding of general mechanisms of nucleic acid polymerization and AIDS therapies may be enhanced by a fuller understanding of drug inhibition and resistance emerging from these studies.