Zobrazeno 1 - 10
of 536
pro vyhledávání: '"Lewis E, Kay"'
Autor:
Satra Nim, Darren M. O’Hara, Carles Corbi-Verge, Albert Perez-Riba, Kazuko Fujisawa, Minesh Kapadia, Hien Chau, Federica Albanese, Grishma Pawar, Mitchell L. De Snoo, Sophie G. Ngana, Jisun Kim, Omar M. A. El-Agnaf, Enrico Rennella, Lewis E. Kay, Suneil K. Kalia, Lorraine V. Kalia, Philip M. Kim
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)
Abstract Accumulation of α-synuclein into toxic oligomers or fibrils is implicated in dopaminergic neurodegeneration in Parkinson’s disease. Here we performed a high-throughput, proteome-wide peptide screen to identify protein-protein interaction
Externí odkaz:
https://doaj.org/article/5d9353322078445d81d882610543e049
Autor:
Yuki Toyama, Lewis E. Kay
Publikováno v:
Journal of Magnetic Resonance Open, Vol 12, Iss , Pp 100065- (2022)
NMR studies exploit spin relaxation in a multitude of different ways, providing information on molecular structure and dynamics. Calculating the relaxation rates of NMR active nuclei in multi-spin systems is often a prerequisite for the proper analys
Externí odkaz:
https://doaj.org/article/92770d57c4714877a7be5f77ec60d3c6
Autor:
Arun Parupudi, Sumit K. Chaturvedi, Regina Adão, Robert W. Harkness, Sonia Dragulin-Otto, Lewis E. Kay, Reza Esfandiary, Huaying Zhao, Peter Schuck
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Abstract Weak macromolecular interactions assume a dominant role in the behavior of highly concentrated solutions, and are at the center of a variety of fields ranging from colloidal chemistry to cell biology, neurodegenerative diseases, and manufact
Externí odkaz:
https://doaj.org/article/e909457b3b7a460aaae039df639e78fb
Publikováno v:
eLife, Vol 9 (2020)
The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins. ClpXP is an important target for drug development ag
Externí odkaz:
https://doaj.org/article/822beeb8932145e48d5d5f0bd6a2ecf3
Autor:
Anatoly Malevanets, P. Andrew Chong, D. Flemming Hansen, Paul Rizk, Yulong Sun, Hong Lin, Ranjith Muhandiram, Avi Chakrabartty, Lewis E. Kay, Julie D. Forman-Kay, Shoshana J. Wodak
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Abstract Misofolding of mammalian prion proteins (PrP) is believed to be the cause of a group of rare and fatal neurodegenerative diseases. Despite intense scrutiny however, the mechanism of the misfolding reaction remains unclear. We perform nuclear
Externí odkaz:
https://doaj.org/article/2cc9aa29f07a4e49a4b2965ad45484b5
Publikováno v:
Journal of Biomolecular NMR. 76:137-152
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f312e48d590773714ce2116883dc411d
https://doi.org/10.1007/s10858-022-00401-4
https://doi.org/10.1007/s10858-022-00401-4
Autor:
Tae Hun Kim, Michael L. Nosella, Nicolas Bolik-Coulon, Robert W. Harkness, Shuya Kate Huang, Lewis E. Kay
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Epigenetic modifications of chromatin play a critical role in regulating the fidelity of the genetic code and in controlling the translation of genetic information into the protein components of the cell. One key posttranslational modification is ace
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b762aa1c4dc9822749594faa42076058
https://doi.org/10.1073/pnas.2301063120
https://doi.org/10.1073/pnas.2301063120
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(36)
Electrostatic interactions and charge balance are important for the formation of biomolecular condensates involving proteins and nucleic acids. However, a detailed, atomistic picture of the charge distribution around proteins during the phase-separat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fc7d3f0fd2563785ffd33de2c6590d3
https://pubmed.ncbi.nlm.nih.gov/36040869
https://pubmed.ncbi.nlm.nih.gov/36040869
Autor:
Danny D. Sahtoe, Ewa A. Andrzejewska, Hannah L. Han, Enrico Rennella, Matthias M. Schneider, Georg Meisl, Maggie Ahlrichs, Justin Decarreau, Hannah Nguyen, Alex Kang, Paul Levine, Mila Lamb, Xinting Li, Asim K. Bera, Lewis E. Kay, Tuomas P.J. Knowles, David Baker
Segments of proteins with β-strand propensity can self associate to form amyloid fibrils associated with many diseases. These regions often adopt alternative structures in their folded states, or are intrinsically disordered in solution, making it d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e438a9b349f9863535f67448f91f321
https://doi.org/10.1101/2023.01.13.523785
https://doi.org/10.1101/2023.01.13.523785
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 5, p e1006180 (2018)
Ligand binding sites in proteins are often localized to deeply buried cavities, inaccessible to bulk solvent. Yet, in many cases binding of cognate ligands occurs rapidly. An intriguing system is presented by the L99A cavity mutant of T4 Lysozyme (T4
Externí odkaz:
https://doaj.org/article/b08ace012c2e449082b5ed98a6dfea53