Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Shilpa Yadahalli"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Many single-domain proteins are not only stable and water-soluble, but they also populate few to no intermediates during folding. This reduces interactions between partially folded proteins, misfolding, and aggregation, and makes the proteins tractab
Externí odkaz:
https://doaj.org/article/ea2dc114c13440969612b7f7878c4126
Autor:
Stephen J. Fox, Shilpa Yadahalli, Lauren M. Reid, Jianguo Li, Nirali Desai, Chandra S. Verma, Jonathan W. Essex, Pietro G. A. Aronica
Publikováno v:
Journal of Chemical Information and Modeling. 61:3172-3196
The evolution of antibiotic-resistant bacteria is an ongoing and troubling development that has increased the number of diseases and infections that risk going untreated. There is an urgent need to develop alternative strategies and treatments to add
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57f69817fdcbbbbf7ddbffe85eee4bb0
https://doi.org/10.1021/acs.jcim.1c00175
https://doi.org/10.1021/acs.jcim.1c00175
Autor:
Shilpa Yadahalli, Chandra S. Verma
Targeting intracellular pathways with peptide drugs is becoming increasingly desirable but often limited in application due to their poor cell permeability. Understanding cellular permeability of peptides remains a major challenge with very little st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed0f9fda095b7ddc75e842f8e9d1bfac
https://doi.org/10.1101/2020.10.15.341149
https://doi.org/10.1101/2020.10.15.341149
Autor:
Anasuya Chattopadhyay, Yaw Sing Tan, Chandra S. Verma, Laura S. Itzhaki, José L. Neira, Christopher M. Johnson, Pamela J. E. Rowling, Shilpa Yadahalli
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Scientific Reports
instname
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Scientific Reports
15 pags., 6 figs., 3 tabs. -- Open Access funded by Creative Commons Atribution Licence 4.0
p53 is frequently mutated in human cancers. Its levels are tightly regulated by the E3 ubiquitin ligase MDM2. The complex between MDM2 and p53 is largely
p53 is frequently mutated in human cancers. Its levels are tightly regulated by the E3 ubiquitin ligase MDM2. The complex between MDM2 and p53 is largely
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::554c4313adde727b3859cbfc73763580
https://doi.org/10.1038/s41598-018-36589-5
https://doi.org/10.1038/s41598-018-36589-5
Autor:
Srinivasaraghavan Kannan, Arumay Pal, Matthew Nguyen, Yaw Sing Tan, Stephen J. Fox, Jianguo Li, Zahra Ouaray, Shilpa Yadahalli
Publikováno v:
Current Pharmaceutical Design. 22:3585-3600
Discovery of new therapeutics is a very challenging, expensive and time-consuming process. With the number of approved drugs declining steadily, combined with increasing costs, a rational approach is needed to facilitate, expedite and streamline the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d14f86655349683ce8b13f789808e80d
https://doi.org/10.2174/1381612822666160425120507
https://doi.org/10.2174/1381612822666160425120507
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Scientific Reports
Scientific Reports
The conformational landscapes of p53 peptide variants and phage derived peptide (12/1) variants, all known to bind to MDM2, are studied using hamiltonian replica exchange molecular dynamics simulations. Complementing earlier observations, the current
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce08fb5e626e36d1dc1c1923be34fc82
https://doi.org/10.1038/s41598-017-15930-4
https://doi.org/10.1038/s41598-017-15930-4
Autor:
Shilpa Yadahalli, Shachi Gosavi
Publikováno v:
Physical chemistry chemical physics : PCCP. 19(13)
Comparative studies of proteins from a family have been used to understand the factors that determine the folding routes of proteins. It has been conjectured that the folding mechanism of ribonuclease-H (RNase-H) proteins is determined by the topolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3367c15cd83b395d359fd43a39cd000
https://pubmed.ncbi.nlm.nih.gov/28317959
https://pubmed.ncbi.nlm.nih.gov/28317959
Publikováno v:
Israel Journal of Chemistry. 54:1230-1240
Natural proteins have evolved amino acid sequences that provide a native-structural bias to folding. Structure-based models (SBMs) of proteins ignore all non-native interactions and encode this bias by including only interactions present in the nativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b29e0bd978ceaae81378bd1ff634086c
https://doi.org/10.1002/ijch.201400035
https://doi.org/10.1002/ijch.201400035
Autor:
Shachi Gosavi, Shilpa Yadahalli
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 82:364-374
The topology of the designed protein Top7 is not found in natural proteins. Top7 shows signatures of non-cooperative folding in both experimental studies and computer simulations. In particular, molecular dynamics of coarse-grained structure-based mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a53e59ff9c0b6ce7773895731013775e
https://doi.org/10.1002/prot.24393
https://doi.org/10.1002/prot.24393
Autor:
Shilpa Yadahalli, Shachi Gosavi
Publikováno v:
Journal of molecular biology. 428(2 Pt)
Functional residues can modulate the folding mechanisms of proteins. In some proteins, mutations to such residues can radically change the primary folding route. Is it possible then to learn more about the functional regions of a protein by investiga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1f1d114b78933921956f71a2cee7cc8
https://pubmed.ncbi.nlm.nih.gov/26724535
https://pubmed.ncbi.nlm.nih.gov/26724535