Zobrazeno 1 - 10
of 65
pro vyhledávání: '"Arjun Narayanan"'
Autor:
Arjun Narayanan, Anatoli Meriin, J Owen Andrews, Jan-Hendrik Spille, Michael Y Sherman, Ibrahim I Cisse
Publikováno v:
eLife, Vol 8 (2019)
The formation of misfolded protein aggregates is a hallmark of neurodegenerative diseases. The aggregate formation process exhibits an initial lag phase when precursor clusters spontaneously assemble. However, most experimental assays are blind to th
Externí odkaz:
https://doaj.org/article/9cb2acb9f9ef4b4bb6efad5e37a16563
Publikováno v:
PLoS Computational Biology, Vol 7, Iss 11, p e1002226 (2011)
Actin filament assembly by the actin-related protein (Arp) 2/3 complex is necessary to build many cellular structures, including lamellipodia at the leading edge of motile cells and phagocytic cups, and to move endosomes and intracellular pathogens.
Externí odkaz:
https://doaj.org/article/ecc31272e5964d2f9788ec317c5784cb
Publikováno v:
PLoS Computational Biology, Vol 2, Iss 4, p e32 (2006)
Post-translational phosphorylation is a ubiquitous mechanism for modulating protein activity and protein-protein interactions. In this work, we examine how phosphorylation can modulate the conformation of a protein by changing the energy landscape. W
Externí odkaz:
https://doaj.org/article/232ba3dea8e747e98546ee68d47a5667
Autor:
Cyriac Abby Philips, Philip Augustine, Karthik Ganesan, Shatakshi Ranade, Varun Chopra, Kunal Patil, Sonie Shende, Rizwan Ahamed, Sandeep Kumbar, Sasidharan Rajesh, Tom George, Meera Mohanan, Narain Mohan, Nikhil Phadke, Mridula Rani, Arjun Narayanan, Suchetha M. Jagan
Publikováno v:
Indian Journal of Gastroenterology. 41:37-51
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::880b4443250d1fe3c8bcc0a4a96bb4b8
https://doi.org/10.1007/s12664-021-01157-9
https://doi.org/10.1007/s12664-021-01157-9
Autor:
Allyn T. Londregan, Karlygash Aitmakhanova, James Bennett, Laura J. Byrnes, Daniel P. Canterbury, Xiayun Cheng, Thomas Christott, Jennifer Clemens, Steven B. Coffey, João M. Dias, Matthew S. Dowling, Gillian Farnie, Oleg Fedorov, Kimberly F. Fennell, Vicki Gamble, Carina Gileadi, Charline Giroud, Michael R. Harris, Brett D. Hollingshead, Kilian Huber, Magdalena Korczynska, Kimberly Lapham, Paula M. Loria, Arjun Narayanan, Dafydd R. Owen, Brigitt Raux, Parag V. Sahasrabudhe, Roger B. Ruggeri, Laura Díaz Sáez, Ingrid A. Stock, Benjamin A. Thuma, Andy Tsai, Alison E. Varghese
Publikováno v:
Journal of medicinal chemistry.
A series of small-molecule YEATS4 binders have been discovered as part of an ongoing research effort to generate high-quality probe molecules for emerging and/or challenging epigenetic targets. Analogues such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f200505c5effa14e470509072c0e10b
https://pubmed.ncbi.nlm.nih.gov/36562986
https://pubmed.ncbi.nlm.nih.gov/36562986
Autor:
Lorenzo D’Amore, David F. Hahn, David L. Dotson, Joshua T. Horton, Jamshed Anwar, Ian Craig, Thomas Fox, Alberto Gobbi, Sirish Kaushik Lakkaraju, Xavier Lucas, Katharina Meier, David L. Mobley, Arjun Narayanan, Christina E. M. Schindler, William C. Swope, Pieter J. in ’t Veld, Jeffrey Wagner, Bai Xue, Gary Tresadern
Publikováno v:
J Chem Inf Model
Force fields form the basis for classical molecular simulations and their accuracy is crucial for the quality of, for instance, protein-ligand binding simulations in drug discovery. The huge diversity of small molecule chemistry makes it a challenge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e988b43643d79476b92f3b6827222b57
https://pubmed.ncbi.nlm.nih.gov/36433835
https://pubmed.ncbi.nlm.nih.gov/36433835
Publikováno v:
Methods in Molecular Biology ISBN: 9781071626627
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a47287e914f3ca3bbe7ce2dd8db9c16
https://doi.org/10.1007/978-1-0716-2663-4_21
https://doi.org/10.1007/978-1-0716-2663-4_21
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2563
Biomolecular condensation has emerged as a key organizing principle governing the formation of membraneless cellular assemblies. Revealing the mechanism of formation of biomolecular condensates requires the quantitative examination of their growth ki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e330cfef58d7e16142ee81279194a7f2
https://pubmed.ncbi.nlm.nih.gov/36227486
https://pubmed.ncbi.nlm.nih.gov/36227486
Publikováno v:
Nature. 615:E28-E28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e1ccef17bfc5fff0d8fdc90a95b9d292
https://doi.org/10.1038/s41586-023-05932-w
https://doi.org/10.1038/s41586-023-05932-w
Autor:
Ariamala Gopalsamy, Ann E. Aulabaugh, Amey Barakat, Kevin C. Beaumont, Shawn Cabral, Daniel P. Canterbury, Agustin Casimiro-Garcia, Jeanne S. Chang, Ming Z. Chen, Chulho Choi, Robert L. Dow, Olugbeminiyi O. Fadeyi, Xidong Feng, Scott P. France, Roger M. Howard, Jay M. Janz, Jayasankar Jasti, Reema Jasuja, Lyn H. Jones, Amanda King-Ahmad, Kelly M. Knee, Jeffrey T. Kohrt, Chris Limberakis, Spiros Liras, Carlos A. Martinez, Kim F. McClure, Arjun Narayanan, Jatin Narula, Jonathan J. Novak, Thomas N. O’Connell, Mihir D. Parikh, David W. Piotrowski, Olga Plotnikova, Ralph P. Robinson, Parag V. Sahasrabudhe, Raman Sharma, Benjamin A. Thuma, Dipy Vasa, Liuqing Wei, A. Zane Wenzel, Jane M. Withka, Jun Xiao, Hatice G. Yayla
Publikováno v:
Journal of Medicinal Chemistry. 64:326-342
Sickle cell disease (SCD) is a genetic disorder caused by a single point mutation (β6 Glu → Val) on the β-chain of adult hemoglobin (HbA) that results in sickled hemoglobin (HbS). In the deoxygenated state, polymerization of HbS leads to sickling
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30fb3aa72d831f7f375af97473787b3a
https://doi.org/10.1021/acs.jmedchem.0c01518
https://doi.org/10.1021/acs.jmedchem.0c01518