Zobrazeno 1 - 10
of 87
pro vyhledávání: '"Athi N Naganathan"'
Autor:
Achinta Sannigrahi, Sourav Chowdhury, Bidisha Das, Amrita Banerjee, Animesh Halder, Amaresh Kumar, Mohammed Saleem, Athi N Naganathan, Sanat Karmakar, Krishnananda Chattopadhyay
Publikováno v:
eLife, Vol 10 (2021)
Aggregation of Cu–Zn superoxide dismutase (SOD1) is implicated in the motor neuron disease, amyotrophic lateral sclerosis (ALS). Although more than 140 disease mutations of SOD1 are available, their stability or aggregation behaviors in membrane en
Externí odkaz:
https://doaj.org/article/db76a746c753473ca3210586e80a4cca
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 12, p e1003403 (2013)
The stability of the repeat protein IκBα, a transcriptional inhibitor in mammalian cells, is critical in the functioning of the NF-κB signaling module implicated in an array of cellular processes, including cell growth, disease, immunity and apopt
Externí odkaz:
https://doaj.org/article/4ca32e533e98449c8fa976f728445569
Publikováno v:
ACS Bio & Med Chem Au, Vol 4, Iss 1, Pp 53-67 (2023)
Externí odkaz:
https://doaj.org/article/0b2769ca53e947f1b693e60b5932b871
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
GPCRs are integral membrane proteins that serve as attractive drug targets. Here, authors delineate the conformational landscapes of 45 GPCRs using a statistical model, highlighting their malleable native ensembles and providing functional insights.
Externí odkaz:
https://doaj.org/article/35eabd4c900d4cd1a6e691ceec3bf423
Publikováno v:
Molecules, Vol 27, Iss 24, p 8762 (2022)
The mutations G170R and I244T are the most common disease cause in primary hyperoxaluria type I (PH1). These mutations cause the misfolding of the AGT protein in the minor allele AGT-LM that contains the P11L polymorphism, which may affect the foldin
Externí odkaz:
https://doaj.org/article/70acc055b13a40a58a70307115ca250f
Publikováno v:
Current Research in Structural Biology, Vol 1, Iss , Pp 6-12 (2019)
Statistical mechanical models that afford an intermediate resolution between macroscopic chemical models and all-atom simulations have been successful in capturing folding behaviors of many small single-domain proteins. However, the applicability of
Externí odkaz:
https://doaj.org/article/0109be945e6e4033b3b8e828ec758aa3
Autor:
Rahul Dani, Westley Pawloski, Dhruv Kumar Chaurasiya, Nonavinakere Seetharam Srilatha, Sonal Agarwal, David Fushman, Athi N. Naganathan
Paralogous proteins confer enhanced fitness to organismsviacomplex sequence-conformation codes that shape functional divergence, specialization, or promiscuity. Here, we resolve the underlying mechanism of promiscuous bindingversuspartial sub-functio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b06ba3c1ad7cc60578199e9fa4b5e44
https://doi.org/10.1101/2023.05.12.540612
https://doi.org/10.1101/2023.05.12.540612
Autor:
Divya Rajendran, Shrutarshi Mitra, Hiroyuki Oikawa, Kulkarni Madhurima, Ashok Sekhar, Satoshi Takahashi, Athi N. Naganathan
Publikováno v:
J Phys Chem Lett
We investigate the conformational properties of the intrinsically disordered DNA-binding domain of CytR in the presence of the polymeric crowder PEG. Integrating CD, NMR and single-molecule FRET measurements, we demonstrate that disordered CytR popul
Autor:
Juan Luis Pacheco-García, Dmitry S. Loginov, Athi N. Naganathan, Pavla Vankova, Mario Cano-Muñoz, Petr Man, Angel L. Pey
Phosphoglycerate kinase has been a model for the stability, folding cooperativity and catalysis of a two-domain protein. The human isoform 1 (hPGK1) is associated with cancer development and rare genetic diseases that affect several of its features.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::885223ee7bd98a2a21a5e22646fb39b6
https://doi.org/10.21203/rs.3.rs-1945879/v1
https://doi.org/10.21203/rs.3.rs-1945879/v1
Autor:
Juan Luis Pacheco-García, Dmitry S. Loginov, Athi N. Naganathan, Pavla Vankova, Mario Cano-Muñoz, Petr Man, Angel L. Pey
Publikováno v:
Scientific reports. 12(1)
Phosphoglycerate kinase has been a model for the stability, folding cooperativity and catalysis of a two-domain protein. The human isoform 1 (hPGK1) is associated with cancer development and rare genetic diseases that affect several of its features.