Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Srabasti Acharya"'
Autor:
William F. DeGrado, Stanley B. Prusiner, Julia Becker, Mark J. S. Kelly, Manasi P. Bhate, Srabasti Acharya, Mimi Nick, Gerald Stubbs, Kathleen Robinson, Haifan Wu, Carlo Condello, Feng Gai, Jan Stöhr, Jeffrey M. Rodgers, Yibing Wu, Thomas Lemmin, Noah R. Johnson
Publikováno v:
Nature Chemistry. 9:874-881
The self-propagation of misfolded conformations of tau underlies neurodegenerative diseases, including Alzheimer’s disease. There is considerable interest in discovering the minimal sequence and active conformational nucleus that defines this self-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40adadc35328763a61601ae52bb7ac8f
https://doi.org/10.1038/nchem.2754
https://doi.org/10.1038/nchem.2754
Publikováno v:
ChemPhysChem. 17:3470-3479
The rate of reconfiguration-or intramolecular diffusion-of monomeric Alzheimer (Aβ) peptides is measured and, under conditions that aggregation is more likely, peptide diffusion slows down significantly, which allows bimolecular associations to be i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e68b8cd9a1aa1f87e265f464c1b93f96
https://doi.org/10.1002/cphc.201600706
https://doi.org/10.1002/cphc.201600706
Publikováno v:
The Journal of Physical Chemistry B. 119:15443-15450
It is still poorly understood why α-synuclein, the intrinsically disordered protein involved in Parkinson’s and other neurodegenerative diseases, is so prone to aggregation. Recent work has shown a correlation between the aggregation rate and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f3aaaaab56f6b605bb6424a30b7bf47
https://doi.org/10.1021/acs.jpcb.5b10136
https://doi.org/10.1021/acs.jpcb.5b10136
Autor:
Lisa J. Lapidus, Frank-Gerrit Klärner, Joseph A. Loo, Aida Attar, Brian M. Safaie, Piriya Wongkongkathep, Thomas Schrader, Srabasti Acharya, Magdalena I. Ivanova, Gal Bitan
Publikováno v:
Acharya, S; Safaie, BM; Wongkongkathep, P; Ivanova, MI; Attar, A; Klärner, FG; et al.(2014). Molecular basis for preventing α-synuclein aggregation by a molecular tweezer. Journal of Biological Chemistry, 289(15), 10727-10737. doi: 10.1074/jbc.M113.524520. UCLA: Retrieved from: http://www.escholarship.org/uc/item/11m276mr
The Journal of biological chemistry, vol 289, iss 15
The Journal of biological chemistry, vol 289, iss 15
Recent work on α-synuclein has shown that aggregation is controlled kinetically by the rate of reconfiguration of the unstructured chain, such that the faster the reconfiguration, the slower the aggregation. In this work we investigate this relation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23f871b6614d09f78bdaf907a3726410
http://www.escholarship.org/uc/item/11m276mr
http://www.escholarship.org/uc/item/11m276mr
Autor:
Ling Wu, Stephen J. DeCamp, Vijay S. Pande, Lisa J. Lapidus, Michael King, Christian R. Schwantes, Diwakar Shukla, Srabasti Acharya
Publikováno v:
Biophysical journal. 107(4)
The B1 domain of protein G has been a classic model system of folding for decades, the subject of numerous experimental and computational studies. Most of the experimental work has focused on whether the protein folds via an intermediate, but the evi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01114af26f70c7cd2bbf12003a0c4715
https://pubmed.ncbi.nlm.nih.gov/25140430
https://pubmed.ncbi.nlm.nih.gov/25140430
Autor:
Lisa J. Lapidus, Srabasti Acharya
Publikováno v:
Biophysical Journal. (2):65a-66a
Protein aggregation is a complex, multistep process, but the first step is likely the formation of a dimer through non-specific interactions of two disordered monomers. In this work we measure the rate of reconfiguration, or intramolecular diffusion,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3357ac9be63317ca57b74e3b2e930508