Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Mahender B. Dewal"'
Autor:
Vincent L. Butty, Edward P. Browne, Emmanuel E Nekongo, Mahender B. Dewal, Matthew D. Shoulders, Anna I. Ponomarenko
Publikováno v:
PMC
ACS Infect Dis
ACS Infect Dis
Copyright © 2020 American Chemical Society. Host protein folding stress responses can play important roles in RNA virus replication and evolution. Prior work suggested a complicated interplay between the cytosolic proteostasis stress response, contr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c4cd115aa58a73346b5400f2ff3e4cc
https://doi.org/10.1021/acsinfecdis.0c00166
https://doi.org/10.1021/acsinfecdis.0c00166
Autor:
Joseph C. Genereux, Aristotelis Antonopoulos, Lara K. Mahal, Kenny Chen, Anne Dell, Brian Kasper, Charles A. Whittaker, Mahender B. Dewal, Pyae P. Hein, Stuart M. Haslam, Madeline Y. Wong, Matthew D. Shoulders, Rebecca J. Taylor
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 115, iss 43
Classically, the unfolded protein response (UPR) safeguards secretory pathway proteostasis. The most ancient arm of the UPR, the IRE1-activated spliced X-box binding protein 1 (XBP1s)-mediated response, has roles in secretory pathway maturation beyon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdaa7c6816bd5c3ca826d2914f1b8a16
https://doi.org/10.1073/pnas.1805425115
https://doi.org/10.1073/pnas.1805425115
Autor:
Nancy B. Lu, Mahender B. Dewal, Emmanuel E Nekongo, Christopher L. Moore, Stuart S. Levine, Sebasthian Santiago, Matthew D. Shoulders
Publikováno v:
ACS Chemical Biology. 11:200-210
Proteostasis in the cytosol is governed by the heat shock response. The master regulator of the heat shock response, heat shock factor 1 (HSF1), and key chaperones whose levels are HSF1-regulated have emerged as high-profile targets for therapeutic a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeab2ddbf80ee0339df4e4028218b32c
https://doi.org/10.1021/acschembio.5b00740
https://doi.org/10.1021/acschembio.5b00740
Autor:
Mahender B. Dewal, Steven M. Firestine
Publikováno v:
Current Medicinal Chemistry. 18:2420-2428
Protein-protein interactions play a major role in almost all biological pathways and thus, these interactions have a profound impact on the pathogenesis of diseases. The ability to modulate protein-protein interactions with small molecules is an impo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::840cde3efc5149cfcae1b29044b848fe
https://doi.org/10.2174/092986711795843227
https://doi.org/10.2174/092986711795843227
Autor:
Mahender B. Dewal, Monissa C. Paderes, David Sobransingh, Mark D. Smith, Linda S. Shimizu, Jeanette A. Krause, Perry J. Pellechia, Sandipan Dawn, Arief Wibowo
Publikováno v:
Journal of the American Chemical Society. 133:7025-7032
There is much interest in designing molecular sized containers that influence and facilitate chemical reactions within their nanocavities. On top of the advantages of improved yield and selectivity, the studies of reactions in confinement also give i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52a79bf5d1489e763387ff5b2de06527
https://doi.org/10.1021/ja110779h
https://doi.org/10.1021/ja110779h
Examination of the Structural Features That Favor the Columnar Self-Assembly of Bis-urea Macrocycles
Publikováno v:
The Journal of Organic Chemistry. 74:102-110
Second-generation self-assembling bis-urea macrocycles were designed that form columnar structures in the solid state. The new macrocycles were constructed from more flexible building blocks yielding greater solubility and a more efficient synthesis.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87d4287ce8c201c4ad66aaef58dc1eea
https://doi.org/10.1021/jo801717w
https://doi.org/10.1021/jo801717w
Autor:
Matthew D. Shoulders, Rebecca J. Taylor, Anne Dell, Andrew S. DiChiara, Mahender B. Dewal, Chyleigh J. Harmon, Stuart M. Haslam, Aristotelis Antonopoulos
Publikováno v:
PMC
The molecular architecture of the mature N-glycome is dynamic, with consequences for both normal and pathologic processes. Elucidating cellular mechanisms that modulate the N-linked glycome is, therefore, crucial. The unfolded protein response (UPR)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9df9aceefe9be2144a94d8be2cfee6a1
https://pubmed.ncbi.nlm.nih.gov/26496683
https://pubmed.ncbi.nlm.nih.gov/26496683
Autor:
Michael W. Lufaso, Andrew D. Hughes, Linda S. Shimizu, Stevan A Samuel, Perry J. Pellechia, Mahender B. Dewal
Publikováno v:
Chemistry of Materials. 18:4855-4864
We report herein the characterization and binding properties of a microporous crystalline host formed by the self assembly of a bis-urea macrocycle 1. Bis-urea macrocycle 1 has been designed to crystallize into stacked hollow columns. The self-assemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f82bd76485353d69c2be7a3028e6e24
https://doi.org/10.1021/cm0614057
https://doi.org/10.1021/cm0614057
Autor:
Steven M. Firestine, Mahender B. Dewal
N(5)-CAIR synthetase, an essential enzyme in microorganisms, converts 5-aminoimidazole ribonucleotide (AIR) and bicarbonate to N(5)-CAIR with the aid of ATP. Previous X-ray crystallographic analyses of Aspergillus clavatus N(5)-CAIR synthetase postul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c04c5ab0552eb9786bd0b355921f495d
https://europepmc.org/articles/PMC3820426/
https://europepmc.org/articles/PMC3820426/
Publikováno v:
Organicbiomolecular chemistry. 9(18)
The enormous success of antibiotics is seriously threatened by the development of resistance to most of the drugs available on the market. Thus, novel antibiotics are needed that are less prone to bacterial resistance and are directed toward novel bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e0e420b4c70c0c272f9611df589e5b2
https://pubmed.ncbi.nlm.nih.gov/21792399
https://pubmed.ncbi.nlm.nih.gov/21792399