Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Emanuel M. Schreiber"'
Publikováno v:
Journal of Proteome Research. 13:3693-3705
Basement membranes (BMs) are extracellular matrix sheets comprising the laminins, type-IV collagens, nidogens, and the heparan sulfate proteoglycans, perlecan, collagen XVIII, and agrin. In intact BMs, BM proteins are physiologically insoluble and pa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65fa0cfe71e1f30c70c1ce0f06f4c1bb
https://doi.org/10.1021/pr5002065
https://doi.org/10.1021/pr5002065
Autor:
Emanuel M. Schreiber, Joseph Candiello, Willi Halfter, Justin Kurtz, Manimalha Balasubramani, Goundappa K. Balasubramani
Publikováno v:
Matrix Biology. 29:471-483
Basement membranes (BMs) are physiologically insoluble extracellular matrix sheets present in all multicellular organisms. They play an important role in providing mechanical strength to tissues and regulating cell behavior. Proteomic analysis of BM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a021953968605a85c129845c6fc62bab
https://doi.org/10.1016/j.matbio.2010.04.002
https://doi.org/10.1016/j.matbio.2010.04.002
Proteolysis of Rad17 by Cdh1/APC regulates checkpoint termination and recovery from genotoxic stress
Autor:
Emanuel M. Schreiber, Chi Hoon Park, Takeo Fujita, Weijun Liu, Manimalha Balasubramani, Xiao-Fan Wang, Jing Wu, Hyun Kim, Liyong Zhang, Yong Wan
Publikováno v:
The EMBO Journal. 29:1726-1737
Recent studies have shown a critical function for the ubiquitin-proteasome system (UPS) in regulating the signalling network for DNA damage responses and DNA repair. To search for new UPS targets in the DNA damage signalling pathway, we have carried
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0085274da9ad44f9dfe68da09263e9c
https://doi.org/10.1038/emboj.2010.55
https://doi.org/10.1038/emboj.2010.55
Publikováno v:
Journal of Natural Products. 72:1748-1754
The polyketide natural product (+)-discodermolide is a potent microtubule stabilizer that has generated considerable interest in its synthetic, medicinal, and biological chemistry. It progressed to early clinical oncology trials, where it showed some
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5c2c71589ac389e13d86d3da260535e
https://doi.org/10.1021/np900245k
https://doi.org/10.1021/np900245k
Autor:
Yunyun Su, Billy W. Day, Shinji Ishikawa, Alessandra Stella, Kazuhisa Shitoh, Chunjiang Fu, Bo Liu, Emanuel M. Schreiber, Masayuki Kojima
Publikováno v:
Molecular Cell. 32:652-661
Ubiquitin-dependent proteolysis is an important mechanism that suppresses the beta-catenin transcription factor in cells without Wnt stimulation. A critical step in this regulatory pathway is to create a SCF(beta-TrCP) E3 ubiquitin ligase binding sit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9f50778bb3a063c9b99060a4d3ee0f5
https://doi.org/10.1016/j.molcel.2008.10.023
https://doi.org/10.1016/j.molcel.2008.10.023
Publikováno v:
Chemical Research in Toxicology. 19:937-943
Etoposide is a widely used antineoplastic agent that has provided great success in the treatment of childhood leukemias and other malignancies. Unfortunately, its use is associated with the increased risk of development of secondary acute myelogenous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e54e76b503a11d6ce3f03f876b952e6
https://doi.org/10.1021/tx0600595
https://doi.org/10.1021/tx0600595
Autor:
John S. Lazo, John J. Skoko, Caleb Foster, Beomjun Joo, Pallavi Bansal, Marni Brisson, Billy W. Day, Emanuel M. Schreiber, Peter Wipf, Theresa Nguyen
Publikováno v:
Molecular Pharmacology. 68:1810-1820
Intracellular reduction and oxidation pathways regulate protein functionality through both reversible and irreversible mechanisms. The Cdc25 phosphatases, which control cell cycle progression, are potential subjects of oxidative regulation. Many of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22f4531c05a7d6655ad2db5c0960426e
https://doi.org/10.1124/mol.105.016360
https://doi.org/10.1124/mol.105.016360
Autor:
Al-Walid Mohsen, Emanuel M. Schreiber, M. Michael Barmada, Wei-wei Wang, Billy W. Day, Manimalha Balasubramani, Guy Uechi, Jerry Vockley
Publikováno v:
Molecular genetics and metabolism. 112(1)
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is an autosomal recessive inborn error of metabolism that leads to the impaired mitochondrial fatty acid β-oxidation of short chain fatty acids. It is heterogeneous in clinical presentation includ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a87c8d9ae4d1fdc69ea2519072c1b9dc
https://pubmed.ncbi.nlm.nih.gov/24685553
https://pubmed.ncbi.nlm.nih.gov/24685553
Autor:
Jerry Vockley, Manimalha Balasubramani, Radha Uppala, Matthew D. Hirschey, Bradford W. Gibson, Megan E. Beck, Yuxun Zhang, Al-Walid Mohsen, Matthew J. Rardin, Sivakama S. Bharathi, Guy Uechi, Eric Verdin, Emanuel M. Schreiber, Eric S. Goetzman
Publikováno v:
The Journal of biological chemistry. 288(47)
Long-chain acyl-CoA dehydrogenase (LCAD) is a key mitochondrial fatty acid oxidation enzyme. We previously demonstrated increased LCAD lysine acetylation in SIRT3 knockout mice concomitant with reduced LCAD activity and reduced fatty acid oxidation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28f7d742e9311c49536c5146f0593fca
https://pubmed.ncbi.nlm.nih.gov/24121500
https://pubmed.ncbi.nlm.nih.gov/24121500
Autor:
Manimalha Balasubramani, Joseph Candiello, Emanuel M. Schreiber, Peng Zhang, Willi Halfter, Haiyu Hu
Publikováno v:
Cell Adhesion & Migration
Basement membranes (BMs) evolved together with the first metazoan species approximately 500 million years ago. Main functions of BMs are stabilizing epithelial cell layers and connecting different types of tissues to functional, multicellular organis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ff7f58c48d12cf7e009f3a0835ce75d
https://pubmed.ncbi.nlm.nih.gov/23154404
https://pubmed.ncbi.nlm.nih.gov/23154404