Zobrazeno 1 - 10
of 22
pro vyhledávání: '"William J. Chirico"'
Publikováno v:
The Cell Surface, Vol 6, Iss , Pp 100045- (2020)
Proteins are secreted from eukaryotic cells by several mechanisms besides the well-characterized classical secretory system. Proteins destined to enter the classical secretory system contain a signal peptide for translocation into the endoplasmic ret
Externí odkaz:
https://doaj.org/article/89ab18eabe9a4832b1d9c8dc3aed6b9c
Publikováno v:
Microorganisms, Vol 9, Iss 12, p 2584 (2021)
Yeast PARK9 (YPK9) shares homology with human ATP13A2, which encodes a polyamine transporter implicated in juvenile forms of Parkinson’s disease. We used YPK9 to gain insight into how ATP13A2 affects cell growth and sensitivity to oxidative stress.
Externí odkaz:
https://doaj.org/article/b5f25ade72c84d5ab5bc3d7a327aef01
Publikováno v:
Pigment Cell & Melanoma Research. 27:1014-1031
The pigmentation of mammalian skin and hair develops through the interaction of two basic cell types — pigment donors and recipients. The pigment donors are melanocytes, which produce and distribute melanin through specialized structures. The pigme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f2fc7b6e26095f6a7a6bf98ae3c4344
https://doi.org/10.1111/pcmr.12301
https://doi.org/10.1111/pcmr.12301
Autor:
Maulik R. Patel, Jason C. Young, Tony Taldone, Tanaji T. Talele, William J. Chirico, Hediye Erdjument-Bromage, Gabriela Chiosis, Hardik J. Patel, Y C Patel, Pengrong Yan, Imad Baaklini, Alexander Gozman, Chenghua Yang, Ronnie Maharaj, Pallav D. Patel, Yanlong Kang, Anna Rodina, Michael J.H. Wong
Publikováno v:
Chemistry & Biology. 20(12):1469-1480
SummaryHsp70s are important cancer chaperones that act upstream of Hsp90 and exhibit independent anti-apoptotic activities. To develop chemical tools for the study of human Hsp70, we developed a homology model that unveils a previously unknown allost
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf5b586f8bf876187efa5d171dbce5c4
Publikováno v:
Journal of Immunoassay and Immunochemistry. 29:220-233
Phosphoglycerate kinase (PGK1) is a key enzyme in glycolysis that can also be released from certain cells. In the extracellular milieu, PGK1 reportedly acts as a disulphide reductase to activate plasmin, resulting in the production of angiostatin, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::091d56ae201262efd3c954ecef00b685
https://doi.org/10.1080/15321810802119588
https://doi.org/10.1080/15321810802119588
Publikováno v:
Journal of Biological Chemistry. 279:40153-40160
Members of high (22-, 22.5-, 24-, and 34-kDa) and low (18-kDa) molecular mass forms of fibroblast growth factor-2 (FGF-2) regulate cell proliferation, differentiation, and migration. FGF-2s have been previously shown to accumulate in the nucleus and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f406c89d4aa79323e9af7017bf62133e
https://doi.org/10.1074/jbc.m400123200
https://doi.org/10.1074/jbc.m400123200
Publikováno v:
Protein Expression and Purification. 27:267-271
Basic fibroblast growth factor (bFGF) is a potent mitogen of many cell types and plays an important role in angiogenesis. To help identify proteins that bind to bFGF and mediate its intracellular transport and signaling, we overexpressed and purified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21b9e28314f036110a5021dbfcb4a00b
https://doi.org/10.1016/s1046-5928(02)00601-0
https://doi.org/10.1016/s1046-5928(02)00601-0
Autor:
Aynih Hermawan, William J. Chirico
Publikováno v:
Archives of Biochemistry and Biophysics. 369:157-162
Hsp70 molecular chaperones facilitate protein folding and translocation by binding to hydrophobic regions of nascent or unfolded proteins, thereby preventing their aggregation. N-Ethylmaleimide (NEM) inhibits the ATPase and protein translocation-stim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef23cbd864606280d0eef2a011c67e74
https://doi.org/10.1006/abbi.1999.1354
https://doi.org/10.1006/abbi.1999.1354
Publikováno v:
Biochemistry. 37:13862-13870
Hsp70 molecular chaperones are highly conserved ATPases that guide the folding and assembly of proteins in many cellular pathways. They use the energy of ATP binding and hydrolysis to regulate their interactions with hydrophobic regions of unfolded p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9a585a6307d4a86598749f0e8a2bc7a
https://doi.org/10.1021/bi980597j
https://doi.org/10.1021/bi980597j
Publikováno v:
Journal of Biological Chemistry. 271:29937-29944
Hsp70 molecular chaperones are ATPases that bind to hydrophobic regions of proteins and guide their folding, assembly, and translocation across membranes. The ability of purified Hsp70s to uncoat clathrin-coated vesicles or to stimulate the post-tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3908fe7eaf9315581e4e457b031f2a76
https://doi.org/10.1074/jbc.271.47.29937
https://doi.org/10.1074/jbc.271.47.29937