Zobrazeno 1 - 10
of 107
pro vyhledávání: '"Richard E. Gillilan"'
Autor:
Tyler J. Florio, Ravi K. Lokareddy, Daniel P. Yeggoni, Rajeshwer S. Sankhala, Connor A. Ott, Richard E. Gillilan, Gino Cingolani
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Nuclear translocation of the p50/p65 heterodimer is essential for NF-κB signaling. Here, the authors identify a bipartite Nuclear Localization Signal in the NF-κB p50/p65 heterodimer that is recognized with high affinity by importin α3.
Externí odkaz:
https://doaj.org/article/d004aa35a7694540be4e536ac4fcacbd
Autor:
Kairit Zovo, Hegne Pupart, Arie Van Wieren, Richard E. Gillilan, Qingqiu Huang, Sudipta Majumdar, Tiit Lukk
Publikováno v:
ACS Omega, Vol 7, Iss 7, Pp 6184-6194 (2022)
Externí odkaz:
https://doaj.org/article/0bd22120f1fe4579ad4b989fcb60c771
Autor:
Rajeshwer S. Sankhala, Ravi K. Lokareddy, Salma Begum, Ruth A. Pumroy, Richard E. Gillilan, Gino Cingolani
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
Importin α3 facilitates the nuclear transport of the Ran guanine nucleotide exchange factor RCC1. Here the authors reveal the molecular basis for the selectivity of RCC1 for importin α3 vs the generic importin α1 and discuss the evolution of impor
Externí odkaz:
https://doaj.org/article/84f5d97d72034197ba5d8d902d0d44a1
Publikováno v:
Structural Dynamics, Vol 2, Iss 5, Pp 054701-054701-8 (2015)
Several X-ray crystal structures of the E. coli core clamp loader containing the five core (δ′, δ, and three truncated γ) subunits have been determined, but they lack the ψ and χ subunits. We report the first solution structure of the complete
Externí odkaz:
https://doaj.org/article/1d9f480a1d994b519de0f62a00e4943f
Autor:
Magda Møller, Søren S. Nielsen, Sekar Ramachandran, Li Yunxing, Giancarlo Tria, Werner Streicher, Maxim V. Petoukhov, Richard A. Cerione, Richard E. Gillilan, Bente Vestergaard
Publikováno v:
PLoS ONE, Vol 8, Iss 12 (2013)
Externí odkaz:
https://doaj.org/article/c4a43ad7dc5f47859e577cc3b44531af
Publikováno v:
The journal of physical chemistry. B. 126(50)
Given the central role of conformational dynamics in protein function, it is essential to characterize the time scales and structures associated with these transitions. High pressure (HP) perturbation favors transitions to excited states because they
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2add601c4895cd14b43ede7edb85c8aa
https://pubmed.ncbi.nlm.nih.gov/36455152
https://pubmed.ncbi.nlm.nih.gov/36455152
Autor:
Ching-Lin Hsieh, Christopher P Ptak, Andrew Tseng, Igor Massahiro de Souza Suguiura, Sean P McDonough, Tepyuda Sritrakul, Ting Li, Yi-Pin Lin, Richard E Gillilan, Robert E Oswald, Yung-Fu Chang
Publikováno v:
eLife, Vol 6 (2017)
Pathogens rely on proteins embedded on their surface to perform tasks essential for host infection. These obligatory structures exposed to the host immune system provide important targets for rational vaccine design. Here, we use a systematically des
Externí odkaz:
https://doaj.org/article/a50dc2ca412046858cd4e180b079cee2
Publikováno v:
Biomacromolecules
Environment-triggered protein conformational changes have garnered wide interest in both fundamental research, for deciphering in vivo acclimatory responses, and practical applications, for designing stimuli-responsive probes. Here, we propose a prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::051410b4d7b17b5c97a81f92e57fc054
https://doi.org/10.1021/acs.biomac.1c01095
https://doi.org/10.1021/acs.biomac.1c01095
Autor:
Richard E, Gillilan
Publikováno v:
Methods in enzymology. 677
The biological relevance of hydrostatic pressure is becoming much more widely understood and appreciated as discoveries of new niches for extreme life continue to emerge. The unusual chemistry and physiological adaptations of organisms under extreme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4d5dfbdee9351d338f29c333e89252ce
https://pubmed.ncbi.nlm.nih.gov/36410954
https://pubmed.ncbi.nlm.nih.gov/36410954
Publikováno v:
Protein science : a publication of the Protein Society. 31(12)
As continuing discoveries highlight the surprising abundance and resilience of deep ocean and subsurface microbial life, the effects of extreme hydrostatic pressure on biological structure and function have attracted renewed interest. Biological smal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81d4e10cea625ea95fa17abba44584b1
https://pubmed.ncbi.nlm.nih.gov/36320105
https://pubmed.ncbi.nlm.nih.gov/36320105