Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Erik C. Hansen"'
Autor:
Aneliya Antonova, Barbara Hummel, Ashkan Khavaran, Desiree M. Redhaber, Fernando Aprile-Garcia, Prashant Rawat, Kathrin Gundel, Megan Schneck, Erik C. Hansen, Jan Mitschke, Gerhard Mittler, Cornelius Miething, Ritwick Sawarkar
Publikováno v:
Cell Reports, Vol 29, Iss 6, Pp 1645-1659.e9 (2019)
Summary: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de
Externí odkaz:
https://doaj.org/article/b0e8519e759d44d6bd040867ed687809
Autor:
Erik C Hansen, Monica Ransom, Jay R Hesselberth, Nina N Hosmane, Adam A Capoferri, Katherine M Bruner, Ross A Pollack, Hao Zhang, Michael Bradley Drummond, Janet M Siliciano, Robert Siliciano, James T Stivers
Publikováno v:
eLife, Vol 5 (2016)
We report that a major subpopulation of monocyte-derived macrophages (MDMs) contains high levels of dUTP, which is incorporated into HIV-1 DNA during reverse transcription (U/A pairs), resulting in pre-integration restriction and post-integration mut
Externí odkaz:
https://doaj.org/article/db3a368d8fbf4bbfb556874b4bc89f4b
The evolutionary capacitor HSP90 buffers the regulatory effects of mammalian endogenous retroviruses
Autor:
Erik C Hansen, Barbara Hummel, Fernando Aprile-Garcia, Rebecca Hussong, Ritwick Sawarkar, Aneliya Yoveva
Publikováno v:
Nature Structural and Molecular Biology
Understanding how genotypes are linked to phenotypes is important in biomedical and evolutionary studies. The chaperone heat-shock protein 90 (HSP90) buffers genetic variation by stabilizing proteins with variant sequences, thereby uncoupling phenoty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb23051c6de8a510fccdd8285834a5e1
https://doi.org/10.1038/nsmb.3368
https://doi.org/10.1038/nsmb.3368
Autor:
Desiree M. Redhaber, Ritwick Sawarkar, Fernando Aprile-Garcia, Prashant Rawat, Jan Mitschke, Megan Schneck, Kathrin Gundel, Gerhard Mittler, Ashkan Khavaran, Barbara Hummel, Erik C Hansen, Cornelius Miething, Aneliya Antonova
Publikováno v:
Cell Reports
Cell Reports, Vol 29, Iss 6, Pp 1645-1659.e9 (2019)
Cell Reports, Vol 29, Iss 6, Pp 1645-1659.e9 (2019)
Summary: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0d1116d5c60acc6e4600fc077d84831
https://pubmed.ncbi.nlm.nih.gov/31693902
https://pubmed.ncbi.nlm.nih.gov/31693902
Autor:
Ritwick Sawarkar, Mark S. Hipp, Jenny Presto, F. Ulrich Hartl, Lisa Vincenz-Donnelly, Hauke Holthusen, Jan Johansson, Erik C Hansen, Roman Körner
Publikováno v:
The EMBO Journal
Protein aggregation is associated with neurodegeneration and various other pathologies. How specific cellular environments modulate the aggregation of disease proteins is not well understood. Here, we investigated how the endoplasmic reticulum (ER) q
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65bc70bf5b8f3522a23674fa50df7eb5
https://hdl.handle.net/21.11116/0000-0000-AF13-621.11116/0000-0000-AF15-4
https://hdl.handle.net/21.11116/0000-0000-AF13-621.11116/0000-0000-AF15-4
Autor:
Namandjé N. Bumpus, Kyle J. Seamon, Anastasia P. Kadina, James T. Stivers, Erik C Hansen, Boris A. Kashemirov, Charles E. McKenna
Publikováno v:
Journal of the American Chemical Society
SAMHD1 is a GTP-activated nonspecific dNTP triphosphohydrolase that depletes dNTP pools in resting CD4+ T cells and macrophages and effectively restricts infection by HIV-1. We have designed a nonsubstrate dUTP analogue with a methylene bridge connec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d97b6330ddd51f8bf702b6333805e713
https://doi.org/10.1021/ja5035717
https://doi.org/10.1021/ja5035717
Autor:
Jay R. Hesselberth, Janet M. Siliciano, Robert F. Siliciano, Hao Zhang, James T. Stivers, Katherine M. Bruner, Monica Ransom, Adam A. Capoferri, Erik C Hansen, M.B. Drummond, Ross A. Pollack, Nina N. Hosmane
Publikováno v:
eLife, Vol 5 (2016)
eLife
eLife
We report that a major subpopulation of monocyte-derived macrophages (MDMs) contains high levels of dUTP, which is incorporated into HIV-1 DNA during reverse transcription (U/A pairs), resulting in pre-integration restriction and post-integration mut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67ea88b52727ac6ba47b3da79cf8a025
https://doi.org/10.7554/elife.18447
https://doi.org/10.7554/elife.18447
Autor:
Robert F. Siliciano, James T. Stivers, Janet M. Siliciano, Jay R. Hesselberth, Nina N. Hosmane, Adam A. Capoferri, Ross A. Pollack, Erik C Hansen, Monica Ransom, Hao Zhang, M.B. Drummond, Katherine M. Bruner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d34ab008342496b06edc5f86a12cad8
https://doi.org/10.7554/elife.18447.030
https://doi.org/10.7554/elife.18447.030
Autor:
Alex B. Burgin, Magnus H. Haraldsson, Brian Pease, Hidong Kim, Douglas R. Davies, Lance Stewart, David E. Zembower, Rama K. Mishra, Alex S. Kiselyov, Jasbir Singh, Jeff Christensen, Mark E. Gurney, Olafur T. Magnusson, Bjorn Mamat, Erik C Hansen
Publikováno v:
Journal of Medicinal Chemistry
We describe a novel fragment library termed fragments of life (FOL) for structure-based drug discovery. The FOL library includes natural small molecules of life, derivatives thereof, and biaryl protein architecture mimetics. The choice of fragments f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f07d1eacdd95f68e81c0612e91bb2494
https://doi.org/10.1021/jm900259h
https://doi.org/10.1021/jm900259h
Publikováno v:
Proceedings of the National Academy of Sciences. 111
The HIV-1 restriction factor sterile α-motif/histidine-aspartate domain-containing protein 1 (SAMHD1) is a tetrameric protein that catalyzes the hydrolysis of all dNTPs to the deoxynucleoside and tripolyphosphate, which effectively depletes the dNTP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6df3fee8a6edc9a778e4cb97a6485570
https://doi.org/10.1073/pnas.1401706111
https://doi.org/10.1073/pnas.1401706111