Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jesús E. Serrano-Negrón"'
Autor:
Dustin T. King, Jesús E. Serrano-Negrón, Yanping Zhu, Christopher L. Moore, Matthew D. Shoulders, Leonard J. Foster, David J. Vocadlo
Publikováno v:
J Am Chem Soc
Post-translational modifications alter the biophysical properties of proteins and thereby influence cellular physiology. One emerging manner by which such modifications regulate protein function is through their ability to perturb protein stability.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c9fb7539735bb76df15f45d676af59e
https://doi.org/10.1021/jacs.1c10621
https://doi.org/10.1021/jacs.1c10621
Autor:
Edwin E. Escobar, Erin H. Seeley, Jesús E. Serrano-Negrón, David J. Vocadlo, Jennifer S. Brodbelt
Publikováno v:
Cancers
Volume 15
Issue 4
Pages: 1224
Volume 15
Issue 4
Pages: 1224
Post-translational O-glycosylation of proteins via the addition of N-acetylglucosamine (O-GlcNAc) is a regulator of many aspects of cellular physiology. Processes driven by perturbed dynamics of O-GlcNAcylation modification have been implicated in ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3408037a0f0a96a88aa1698152394ca7
https://doi.org/10.3390/cancers15041224
https://doi.org/10.3390/cancers15041224
Autor:
Dustin T. King, Matthew G. Alteen, Edwin E. Escobar, Jennifer S. Brodbelt, Jesús E. Serrano-Negrón, David J. Vocadlo
Publikováno v:
J Am Chem Soc
Despite its central importance as a regulator of cellular physiology, identification and precise mapping of O-linked N-acetylglucosamine (O-GlcNAc) post-translational modification (PTM) sites in proteins by mass spectrometry (MS) remains a considerab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce5dbe6f17f00c484e94df186061c07a
http://summit.sfu.ca/item/20486
http://summit.sfu.ca/item/20486
Autor:
Jesús E Serrano-Negrón, Krishna Baksi, Andrea P Rivera-Ruiz, Aditi Banerjee, Zhenbo Zhang, Neysharie Sánchez-Torres, Eva C Romero-Nutz, Dipak K. Banerjee
Publikováno v:
Glycobiology. 29(7)
GRP78 (an Mr 78 kDa calcium dependent glucose binding protein) is located in ER lumen. It functions as ER chaperone and translocates proteins for glycosylation at the asparagine residue present in the sequon Asn-X-Ser/Thr. Paraffin sections from N-gl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c6ee4f8bd915210d5540c5d2350098d
https://pubmed.ncbi.nlm.nih.gov/29206917
https://pubmed.ncbi.nlm.nih.gov/29206917
Publikováno v:
Advances in experimental medicine and biology. 1112
Dolichol phosphate mannose synthase (DPMS) is an inverting GT-A-folded enzyme and classified as GT2 by CAZy. DPMS sequence carries a metal-binding DXD motif, a PKA motif, and a variable number of hydrophobic domains. Human and bovine DPMS possess a s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::04e8fc8495592f76be6e67cb0498a4e1
https://pubmed.ncbi.nlm.nih.gov/30637701
https://pubmed.ncbi.nlm.nih.gov/30637701
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9789811330643
Dolichol phosphate mannose synthase (DPMS) is an inverting GT-A-folded enzyme and classified as GT2 by CAZy. DPMS sequence carries a metal-binding DXD motif, a PKA motif, and a variable number of hydrophobic domains. Human and bovine DPMS possess a s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::967ef0d83d8377522f3f7d6eb2804d2c
https://doi.org/10.1007/978-981-13-3065-0_16
https://doi.org/10.1007/978-981-13-3065-0_16
Publikováno v:
Glycoconjugate journal. 34(4)
N-glycans provide structural and functional stability to asparagine-linked (N-linked) glycoproteins, and add flexibility. Glycan biosynthesis is elaborative, multi-compartmental and involves many glycosyltransferases. Failure to assemble N-glycans le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a54f8381d8f517e0332dac7e487e9c29
https://pubmed.ncbi.nlm.nih.gov/28616799
https://pubmed.ncbi.nlm.nih.gov/28616799