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Courtney Hodges

Researcher at Stanford University

Publications -  15
Citations -  3327

Courtney Hodges is an academic researcher from Stanford University. The author has contributed to research in topics: SWI/SNF & Chromatin remodeling. The author has an hindex of 10, co-authored 12 publications receiving 2795 citations. Previous affiliations of Courtney Hodges include University of California, Berkeley & California Institute of Technology.

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Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes identifies extensive roles in human malignancy

TL;DR: It is demonstrated that mSWI/SNF is the most frequently mutated chromatin-regulatory complex (CRC) in human cancer, exhibiting a broad mutation pattern, similar to that of TP53, and proper functioning of polymorphic BAF complexes may constitute a major mechanism of tumor suppression.
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Following translation by single ribosomes one codon at a time

TL;DR: Pause lengths, and thus the overall rate of translation, depend on the secondary structure of the mRNA; the applied force destabilizes secondary structure and decreases pause durations, but does not affect translocation times.
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Dynamics and Memory of Heterochromatin in Living Cells

TL;DR: A chromatin in vivo assay (CiA) system employing chemically induced proximity to initiate and terminate chromatin modifications in living cells and quantitative modeling of reaction kinetics revealed that dynamic competition between histone marking and turnover, determines the boundaries and stability of H3K9me3 domains.
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Nucleosomal fluctuations govern the transcription dynamics of RNA polymerase II.

TL;DR: An optical tweezers assay to follow individual Pol II complexes as they transcribe nucleosomal DNA is developed and obtained direct evidence that transcription through a nucleosome involves transfer of the core histones behind the transcribing polymerase via a transient DNA loop.
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ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates

TL;DR: Direct observations of mechanical, force-induced protein unfolding by the ClpX unfoldase from E. coli, alone, and in complex with the ClPP peptidase are reported.