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Wyszukujesz frazę ""Whitby, Frank G."" wg kryterium: Autor


Wyświetlanie 1-7 z 7
Tytuł :
A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription.
Autorzy :
Sdano MA; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Fulcher JM; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Palani S; Department of Radiation Oncology, University of Utah School of Medicine, Salt Lake City, United States.; Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, United States.
Chandrasekharan MB; Department of Radiation Oncology, University of Utah School of Medicine, Salt Lake City, United States.; Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, United States.
Parnell TJ; Department of Radiation Oncology, University of Utah School of Medicine, Salt Lake City, United States.; Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, United States.; Department of Oncological Sciences, University of Utah School of Medicine, Salt Lake City, United States.
Whitby FG; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Formosa T; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Hill CP; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
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Źródło :
ELife [Elife] 2017 Aug 16; Vol. 6. Date of Electronic Publication: 2017 Aug 16.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Processing, Post-Translational*
Histone Chaperones/*chemistry
Histone Chaperones/*metabolism
RNA Polymerase II/*chemistry
RNA Polymerase II/*metabolism
Saccharomyces cerevisiae/*enzymology
Saccharomyces cerevisiae/*genetics
Saccharomyces cerevisiae Proteins/*chemistry
Saccharomyces cerevisiae Proteins/*metabolism
Transcriptional Elongation Factors/*chemistry
Transcriptional Elongation Factors/*metabolism
Crystallography, X-Ray ; Models, Molecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Transcription, Genetic
Czasopismo naukowe
Tytuł :
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs.
Autorzy :
Kemble DJ; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
McCullough LL; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Whitby FG; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Formosa T; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA. Electronic address: .
Hill CP; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2015 Oct 15; Vol. 60 (2), pp. 294-306. Date of Electronic Publication: 2015 Oct 08.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
DNA-Binding Proteins/*metabolism
High Mobility Group Proteins/*metabolism
Histones/*metabolism
Nucleosomes/*chemistry
Saccharomyces cerevisiae/*genetics
Saccharomyces cerevisiae Proteins/*metabolism
Transcription Factors/*metabolism
Transcriptional Elongation Factors/*metabolism
Amino Acid Motifs ; Conserved Sequence ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; Gene Expression Regulation, Fungal ; High Mobility Group Proteins/chemistry ; High Mobility Group Proteins/genetics ; Histones/chemistry ; Histones/genetics ; Models, Molecular ; Molecular Sequence Data ; Nucleosomes/metabolism ; Protein Binding ; Protein Multimerization ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Sequence Alignment ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcriptional Elongation Factors/chemistry ; Transcriptional Elongation Factors/genetics
Czasopismo naukowe
Tytuł :
The oligomeric state of the active Vps4 AAA ATPase.
Autorzy :
Monroe N; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA.
Han H; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA.
Gonciarz MD; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA.
Eckert DM; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA.
Karren MA; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA.
Whitby FG; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA.
Sundquist WI; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA. Electronic address: .
Hill CP; Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2014 Feb 06; Vol. 426 (3), pp. 510-25. Date of Electronic Publication: 2013 Oct 23.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Adenosine Triphosphatases/*metabolism
Endosomal Sorting Complexes Required for Transport/*chemistry
Saccharomyces cerevisiae/*enzymology
Saccharomyces cerevisiae Proteins/*chemistry
Adenosine Triphosphatases/chemistry ; Crystallography, X-Ray ; Endosomal Sorting Complexes Required for Transport/metabolism ; Humans ; Models, Molecular ; Protein Conformation ; Protein Multimerization ; Saccharomyces cerevisiae Proteins/metabolism
Czasopismo naukowe
Tytuł :
Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT.
Autorzy :
Kemble DJ; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112-5650, USA.
Whitby FG
Robinson H
McCullough LL
Formosa T
Hill CP
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2013 Apr 12; Vol. 288 (15), pp. 10188-94. Date of Electronic Publication: 2013 Feb 15.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
DNA-Binding Proteins/*chemistry
High Mobility Group Proteins/*chemistry
Molecular Chaperones/*chemistry
Saccharomyces cerevisiae/*chemistry
Saccharomyces cerevisiae Proteins/*chemistry
Transcriptional Elongation Factors/*chemistry
Animals ; Crystallography, X-Ray ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; High Mobility Group Proteins/genetics ; High Mobility Group Proteins/metabolism ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Structural Homology, Protein ; Structure-Activity Relationship ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcriptional Elongation Factors/genetics ; Transcriptional Elongation Factors/metabolism
Czasopismo naukowe
Tytuł :
Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.
Autorzy :
Sadre-Bazzaz K; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Whitby FG
Robinson H
Formosa T
Hill CP
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Źródło :
Molecular cell [Mol Cell] 2010 Mar 12; Vol. 37 (5), pp. 728-35.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Mitochondria/*enzymology
Proteasome Endopeptidase Complex/*chemistry
Saccharomyces cerevisiae/*enzymology
Saccharomyces cerevisiae Proteins/*chemistry
Amino Acid Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Genotype ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Phenotype ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Protein Conformation ; Reactive Oxygen Species/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae.
Autorzy :
Phillips JD; Department of Medicine, University of Utah School of Medicine, Salt Lake City, Utah 84132, USA.
Whitby FG
Warby CA
Labbe P
Yang C
Pflugrath JW
Ferrara JD
Robinson H
Kushner JP
Hill CP
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2004 Sep 10; Vol. 279 (37), pp. 38960-8. Date of Electronic Publication: 2004 Jun 12.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
MeSH Terms :
Coproporphyrinogen Oxidase/*chemistry
Saccharomyces cerevisiae/*enzymology
Saccharomyces cerevisiae Proteins/*chemistry
Amino Acid Sequence ; Binding Sites ; Catalysis ; Coproporphyrinogen Oxidase/metabolism ; Coproporphyrinogens/chemistry ; Crystallography, X-Ray ; DNA, Complementary/metabolism ; Dimerization ; Heme/chemistry ; Humans ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; Protoporphyrins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Homology, Amino Acid
Czasopismo naukowe
    Wyświetlanie 1-7 z 7

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