Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Karishma Bhasne"'
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e83752 (2013)
Membrane-induced disorder-to-helix transition of α-synuclein, a presynaptic protein, has been implicated in a number of important neuronal functions as well as in the etiology of Parkinson's disease. In order to obtain structural insights of membran
Externí odkaz:
https://doaj.org/article/04602396618c4e959dabdc6444775402
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d1566889491e773229a38fe2c482f7a
https://doi.org/10.1096/fasebj.2022.36.s1.r3782
https://doi.org/10.1096/fasebj.2022.36.s1.r3782
Publikováno v:
Biophysical Journal. 122:152a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2681bacf0f370da58c09601ffd8f7f5d
https://doi.org/10.1016/j.bpj.2022.11.1000
https://doi.org/10.1016/j.bpj.2022.11.1000
Autor:
Anupa Majumdar, Karishma Bhasne, Anubhuti Singh, Samrat Mukhopadhyay, Shruti Arya, Neha Jain, Rishabh Karnawat
Publikováno v:
The journal of physical chemistry. B. 124(5)
α-Synuclein is an intrinsically disordered protein that adopts an α-helical structure upon binding to the negatively charged lipid membrane. Binding-induced conformational change of α-synuclein plays a crucial role in the regulation of synaptic pl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::331283cef39540b1865409b21d513fed
https://pubmed.ncbi.nlm.nih.gov/31917569
https://pubmed.ncbi.nlm.nih.gov/31917569
Publikováno v:
Journal of Molecular Biology. 430:2508-2520
Amyloidogenic intrinsically disordered proteins, α-synuclein and tau are linked to Parkinson's disease and Alzheimer's disease, respectively. A body of evidence suggests that α-synuclein and tau, both present in the presynaptic nerve terminals, co-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c17621441701b766efd97cd425fc8bf
https://doi.org/10.1016/j.jmb.2018.04.020
https://doi.org/10.1016/j.jmb.2018.04.020
Autor:
Constantine Petridis, Karishma Bhasne, Wenli Meng, Eugenia M. Clerico, Lila M. Gierasch, Alexandra Pozhidaeva
Publikováno v:
Biochem J
The Hsp70 family of chaperones works with its co-chaperones, the nucleotide exchange factors and J-domain proteins, to facilitate a multitude of cellular functions. Central players in protein homeostasis, these jacks-of-many-trades are utilized in a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d91541f8f072a741cf9297f61dedb354
https://pubmed.ncbi.nlm.nih.gov/31201219
https://pubmed.ncbi.nlm.nih.gov/31201219
Autor:
Karishma Bhasne, Dominic Narang, Samrat Mukhopadhyay, Vijit Dalal, Neha Jain, Shruti Arya, Mily Bhattacharya
Publikováno v:
Biophysical Journal. 111:768-774
The fundamental backbone dynamics of unfolded proteins arising due to intrinsic ϕ-ψ dihedral angle fluctuations dictate the course of protein folding, binding, assembly, and function. These internal fluctuations are also critical for protein misfol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb508c0a6de90b26ad0f4e02ec9983eb
https://doi.org/10.1016/j.bpj.2016.07.023
https://doi.org/10.1016/j.bpj.2016.07.023
Publikováno v:
Biochemistry. 57(44)
Curli is a biofilm-forming amyloid that is expressed on the surface of Gram-negative enteric bacteria such as Escherichia coli and Salmonella spp. Curli is primarily composed of the major structural subunit, CsgA, and interacts with a wide range of h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d24fc4ea61fed1a38dc2ea873b98e71b
https://pubmed.ncbi.nlm.nih.gov/30338995
https://pubmed.ncbi.nlm.nih.gov/30338995
Autor:
Samrat Mukhopadhyay, Avinash Kumar Singh, Priyanka Dogra, Payel Das, Karishma Bhasne, Anindya Datta, Shruti Arya
Publikováno v:
Biophysical journal. 114(11)
Protein hydration water plays a fundamentally important role in protein folding, binding, assembly, and function. Little is known about the hydration water in intrinsically disordered proteins that challenge the conventional sequence-structure-functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f93ed0ad8acf73efa4f8daf5b8aad1c5
https://pubmed.ncbi.nlm.nih.gov/29874605
https://pubmed.ncbi.nlm.nih.gov/29874605
Autor:
Samrat Mukhopadhyay, Karishma Bhasne
Publikováno v:
PROTEOMICS. 18:1800059
Protein misfolding resulting in the formation of ordered amyloid aggregates is associated with a number of devastating human diseases. Intrinsically disordered proteins (IDPs) do not autonomously fold up into a unique stable conformation and remain a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::736850cf889b844e20a4f91a1fa9b55c
https://doi.org/10.1002/pmic.201800059
https://doi.org/10.1002/pmic.201800059