Eric B Gibbs
Overview
Explore the profile of Eric B Gibbs including associated specialties, affiliations and a list of published articles.
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Articles
8
Citations
250
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0
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Recent Articles
1.
Gibbs E, Kriwacki R
Proc Natl Acad Sci U S A
. 2018 Nov;
115(47):11868-11870.
PMID: 30389709
No abstract available.
2.
Mitrea D, Chandra B, Ferrolino M, Gibbs E, Tolbert M, White M, et al.
J Mol Biol
. 2018 Jul;
430(23):4773-4805.
PMID: 30017918
Membrane-less organelles are cellular structures which arise through the phenomenon of phase separation. This process enables compartmentalization of specific sets of macromolecules (e.g., proteins, nucleic acids), thereby regulating cellular processes...
3.
Gibbs E, Laremore T, Usher G, Portz B, Cook E, Showalter S
Biophys J
. 2017 Oct;
113(9):1909-1911.
PMID: 28992937
The positive transcription elongation factor b (P-TEFb) promotes transcription elongation through phosphorylation of the RNA polymerase II C-terminal domain. This process is not well understood, partly due to difficulties in...
4.
Gibbs E, Cook E, Showalter S
Arch Biochem Biophys
. 2017 May;
628:57-70.
PMID: 28502465
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins, and their clear functional advantages for signaling and gene regulation have created an imperative for high-resolution structural and mechanistic...
5.
Gibbs E, Lu F, Portz B, Fisher M, Medellin B, Laremore T, et al.
Nat Commun
. 2017 May;
8:15233.
PMID: 28497798
The carboxy-terminal domain (CTD) of the RNA polymerase II (Pol II) large subunit cycles through phosphorylation states that correlate with progression through the transcription cycle and regulate nascent mRNA processing....
6.
Portz B, Lu F, Gibbs E, Mayfield J, Mehaffey M, Zhang Y, et al.
Nat Commun
. 2017 May;
8:15231.
PMID: 28497792
RNA polymerase II contains a repetitive, intrinsically disordered, C-terminal domain (CTD) composed of heptads of the consensus sequence YSPTSPS. The CTD is heavily phosphorylated and serves as a scaffold, interacting...
7.
Gibbs E, Showalter S
J Phys Chem B
. 2016 Aug;
120(34):8960-9.
PMID: 27551949
Intrinsically disordered protein regions (IDRs) partially or completely lack a cooperatively folded structure under native conditions, preventing their equilibrium state from being adequately described by a single structural model. As...
8.
Gibbs E, Showalter S
Biochemistry
. 2015 Jan;
54(6):1314-26.
PMID: 25631161
Intrinsically disordered proteins (IDPs) are broadly defined as protein regions that do not cooperatively fold into a spatially or temporally stable structure. Recent research strongly supports the hypothesis that a...