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Acetylation of Histones and Transcription-Related Factors

Microbiology and Molecular Biology Reviews, 2000-06, Vol.64 (2), p.435-459

2000

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Ubiquitin-specific Protease-7 Inhibition Impairs Tip60-dependent Foxp3+ T-regulatory Cell Function and Promotes Antitumor Immunity

EBioMedicine, 2016-11, Vol.13 (C), p.99-112

2016

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Characterization of ubiquitin and ubiquitin‐like‐protein isopeptidase activities

Protein science, 2008-06, Vol.17 (6), p.1035-1043

2008

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USP7-Specific Inhibitors Target and Modify the Enzyme's Active Site via Distinct Chemical Mechanisms

Cell chemical biology, 2017-12, Vol.24 (12), p.1501-1512.e5

2017

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Targeting the Ubiquitin E3 Ligase MuRF1 to Inhibit Muscle Atrophy

Cell biochemistry and biophysics, 2011-06, Vol.60 (1-2), p.113-118

2011

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SALSA, a Variant of Yeast SAGA, Contains Truncated Spt7, Which Correlates with Activated Transcription

Proceedings of the National Academy of Sciences - PNAS, 2002-09, Vol.99 (18), p.11622-11627

2002

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TAM receptors attenuate murine NK‐cell responses via E3 ubiquitin ligase Cbl‐b

European journal of immunology, 2020-01, Vol.50 (1), p.48-55

2020

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Histone Modifications: Now Summoning Sumoylation

Proceedings of the National Academy of Sciences - PNAS, 2003-11, Vol.100 (23), p.13118-13120

2003

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Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator

Proceedings of the National Academy of Sciences - PNAS, 1999-08, Vol.96 (16), p.8931-8936

1999

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The SANT Domain of Ada2 Is Required for Normal Acetylation of Histones by the Yeast SAGA Complex

The Journal of biological chemistry, 2002-03, Vol.277 (10), p.8178-8186

2002

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Combined deep learning and molecular docking simulations approach identifies potentially effective FDA approved drugs for repurposing against SARS-CoV-2

Computers in biology and medicine, 2022-02, Vol.141, p.105049-105049, Article 105049

2022

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The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes

Trends in cell biology, 1998-05, Vol.8 (5), p.193-197

1998

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Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications

Genes & development, 2006-04, Vol.20 (8), p.966-976

2006

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Expression and purification of SARS coronavirus proteins using SUMO-fusions

Protein expression and purification, 2005-07, Vol.42 (1), p.100-110

2005

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Gcn5p-dependent acetylation induces degradation of the meiotic transcriptional repressor Ume6p

Molecular biology of the cell, 2012-05, Vol.23 (9), p.1609-1617

2012

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Comprehensive Ubiquitin E2 Profiling of Ten Ubiquitin E3 Ligases

Cell biochemistry and biophysics, 2013-09, Vol.67 (1), p.161-167

2013

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Functional Organization of the Yeast SAGA Complex: Distinct Components Involved in Structural Integrity, Nucleosome Acetylation, and TATA-Binding Protein Interaction

Molecular and Cellular Biology, 1999-01, Vol.19 (1), p.86-98

1999

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The ADA Complex Is a Distinct Histone Acetyltransferase Complex in Saccharomyces cerevisiae

Molecular and Cellular Biology, 1999-10, Vol.19 (10), p.6621-6631

1999

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Inhibition of TATA-Binding Protein Function by SAGA Subunits Spt3 and Spt8 at Gcn4-Activated Promoters

Molecular and Cellular Biology, 2000-01, Vol.20 (2), p.634-647

2000

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Small ubiquitin-like modifying protein isopeptidase assay based on poliovirus RNA polymerase activity

Analytical biochemistry, 2006-03, Vol.350 (2), p.214-221

2006

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Novel Approach for Characterizing Ubiquitin E3 Ligase Function

Journal of biomolecular screening, 2010-12, Vol.15 (10), p.1220-1228

2010

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Sumoylation of the Yeast Gcn5 Protein

Biochemistry (Easton), 2006-01, Vol.45 (3), p.1035-1042

2006

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Acetylation of Histones and Transcription-Related Factors

Potent and selective covalent inhibition of the papain-like protease from SARS-CoV-2

Ubiquitin-specific Protease-7 Inhibition Impairs Tip60-dependent Foxp3+ T-regulatory Cell Function and Promotes Antitumor Immunity

Characterization of ubiquitin and ubiquitin‐like‐protein isopeptidase activities

USP7-Specific Inhibitors Target and Modify the Enzyme's Active Site via Distinct Chemical Mechanisms

Targeting the Ubiquitin E3 Ligase MuRF1 to Inhibit Muscle Atrophy

SALSA, a Variant of Yeast SAGA, Contains Truncated Spt7, Which Correlates with Activated Transcription

TAM receptors attenuate murine NK‐cell responses via E3 ubiquitin ligase Cbl‐b

Histone Modifications: Now Summoning Sumoylation

Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator

The SANT Domain of Ada2 Is Required for Normal Acetylation of Histones by the Yeast SAGA Complex

Combined deep learning and molecular docking simulations approach identifies potentially effective FDA approved drugs for repurposing against SARS-CoV-2

The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes

Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications

Expression and purification of SARS coronavirus proteins using SUMO-fusions

Gcn5p-dependent acetylation induces degradation of the meiotic transcriptional repressor Ume6p

Comprehensive Ubiquitin E2 Profiling of Ten Ubiquitin E3 Ligases

Functional Organization of the Yeast SAGA Complex: Distinct Components Involved in Structural Integrity, Nucleosome Acetylation, and TATA-Binding Protein Interaction

The ADA Complex Is a Distinct Histone Acetyltransferase Complex in Saccharomyces cerevisiae

Inhibition of TATA-Binding Protein Function by SAGA Subunits Spt3 and Spt8 at Gcn4-Activated Promoters

Process for Assembly and Transformation into Saccharomyces cerevisiae of a Synthetic Yeast Artificial Chromosome Containing a Multigene Cassette to Express Enzymes That Enhance Xylose Utilization Designed for an Automated Platform

Small ubiquitin-like modifying protein isopeptidase assay based on poliovirus RNA polymerase activity

Novel Approach for Characterizing Ubiquitin E3 Ligase Function

Sumoylation of the Yeast Gcn5 Protein

Engineered Saccharomyces cerevisiae strain for improved xylose utilization with a three-plasmid SUMO yeast expression system

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