Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Catherine M Guzzo"'
Autor:
Catherine M Guzzo, Alison Ringel, Eric Cox, Ijeoma Uzoma, Heng Zhu, Seth Blackshaw, Cynthia Wolberger, Michael J Matunis
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e105271 (2014)
SUMO-binding proteins interact with SUMO modified proteins to mediate a wide range of functional consequences. Here, we report the identification of a new SUMO-binding protein, ZNF261. Four human proteins including ZNF261, ZNF198, ZNF262, and ZNF258
Externí odkaz:
https://doaj.org/article/05c4a32aece54783963728f7646945f8
Autor:
Jiang Qian, Michael J. Matunis, Woochang Hwang, Heng Zhu, Seth Blackshaw, Jun Seop Jeong, Ijeoma Uzoma, Eric Cox, Jianfei Hu, Catherine M. Guzzo
Publikováno v:
Molecular & Cellular Proteomics
SUMOylation is a critical regulator of a broad range of cellular processes, and is thought to do so in part by modulation of protein interaction. To comprehensively identify human proteins whose interaction is modulated by SUMOylation, we developed a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::117bed13456033db9669ea232d33dcd5
https://doi.org/10.1074/mcp.m116.063719
https://doi.org/10.1074/mcp.m116.063719
Autor:
C. Rory Goodwin, Jiang Qian, Cedric Moore, Corry Paul, Catherine M. Guzzo, Michael J. Matunis, Shuli Xia, Jian-Ying Zhou, Hee Sool Rho, Seth Blackshaw, Pamela B. Meluh, Eric Cox, Jun Seop Jeong, Olutobi Z Ajala, Jianfei Hu, Heng Zhu, Ijeoma Uzoma, Hui Zhang
Publikováno v:
Molecular & Cellular Proteomics : MCP
Proteomics studies have revealed that SUMOylation is a widely used post-translational modification (PTM) in eukaryotes. However, how SUMO E1/2/3 complexes use different SUMO isoforms and recognize substrates remains largely unknown. Using a human pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3498d0b60cb65c6f091e1308e008f237
https://pubmed.ncbi.nlm.nih.gov/29438996
https://pubmed.ncbi.nlm.nih.gov/29438996
Autor:
Megan E. Fitzgerald, Atanu Maiti, Alexander C. Drohat, Catherine M. Guzzo, Katherine H. Reiter, Christopher T. Coey, Michael J. Matunis
Publikováno v:
Journal of Biological Chemistry. 289:15810-15819
Thymine DNA glycosylase (TDG) initiates the repair of G·T mismatches that arise by deamination of 5-methylcytosine (mC), and it excises 5-formylcytosine and 5-carboxylcytosine, oxidized forms of mC. TDG functions in active DNA demethylation and is e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81c2603caf7608557a4ad443656fc7b1
https://doi.org/10.1074/jbc.m114.572081
https://doi.org/10.1074/jbc.m114.572081
Autor:
Michael J. Matunis, Reuven Wiener, Patrick M. Lombardi, Catherine M. Guzzo, Xiangbin Zhang, Cynthia Wolberger, Anthony T DiBello
Publikováno v:
Nature structural & molecular biology
OTUB1 is a Lys48-specific deubiquitinating enzyme that forms a complex in vivo with E2 ubiquitin (Ub)-conjugating enzymes including UBC13 and UBCH5. OTUB1 binds E2~Ub thioester intermediates and prevents ubiquitin transfer, thereby noncatalytically i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dab7b7a64f19b029ec2a292bc888d1ce
http://europepmc.org/articles/PMC3941643
http://europepmc.org/articles/PMC3941643
Autor:
Leyao Wang, Renfeng Li, Catherine M. Guzzo, Michael J. Matunis, Gangling Liao, S. Diane Hayward, Heng Zhu
Publikováno v:
Journal of Virology. 86:5412-5421
An Epstein-Barr virus (EBV) protein microarray was used to screen for proteins binding noncovalently to the small ubiquitin-like modifier SUMO2. Among the 11 SUMO binding proteins identified was the conserved protein kinase BGLF4. The mutation of pot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a2c5a1a108f140f1797b6e908b04c27
https://doi.org/10.1128/jvi.00314-12
https://doi.org/10.1128/jvi.00314-12
Autor:
David C.H. Yang, Catherine M. Guzzo
Publikováno v:
Biochemical and Biophysical Research Communications. 365:718-723
The functions of evolved mammalian supramolecular assemblies and extensions of enzymes are not well understood. Human lysyl-tRNA synthetase (hKRS) only upon the removal of the amino-terminal extension (hKRSDelta60) bound to EF1alpha and was stimulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::683d150bd48a8776211e91c181886d3b
https://doi.org/10.1016/j.bbrc.2007.11.028
https://doi.org/10.1016/j.bbrc.2007.11.028
Autor:
Jianmei Zhu, Christopher E. Berndsen, Ajit B. Datta, Roger A. Greenberg, Catherine M. Guzzo, Cynthia Wolberger, Michael J. Matunis, Vibhor Gupta
Publikováno v:
The FASEB Journal. 27
The DNA repair function of the breast cancer susceptibility protein BRCA1 depends in part on its interaction with RAP80, which targets BRCA1 to DNA double strand breaks (DSBs) through recognition of K63-linked polyubiquitin chains. The localization o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a9812f0458f87c69b1a0d03fdc8b25a
https://doi.org/10.1096/fasebj.27.1_supplement.782.7
https://doi.org/10.1096/fasebj.27.1_supplement.782.7
Autor:
Michael J. Matunis, Catherine M. Guzzo
Publikováno v:
Cell Cycle
Monomeric and polymeric forms of SUMO and ubiquitin are covalently attached to substrates and recognized by effector proteins containing SUMO-interacting motifs (SIMs) or ubiquitin-interacting motifs (UIMs), thereby triggering a wide range of biologi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeb8c6bbfb7d309a8b5abde4e70bba2c
https://pubmed.ncbi.nlm.nih.gov/23511166
https://pubmed.ncbi.nlm.nih.gov/23511166
Autor:
Michael J, Matunis, Catherine M, Guzzo
Publikováno v:
Pigment cellmelanoma research.
Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) was identified in 1997 as a tumor suppressor gene through mapping of homozygous mutations occurring in multiple sporadic tumor types and in patients with cancer predisposition syndromes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::178c5591cebed031f2551adec8203ef5
https://pubmed.ncbi.nlm.nih.gov/22846175
https://pubmed.ncbi.nlm.nih.gov/22846175