Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Arthur V. Hauenstein"'
Autor:
Arthur V. Hauenstein, Seong Ho Hong, David Rooklin, Archana Gautam, Ethel Cesarman, Michael G. Wuo, Jouliana Sadek, Yingkai Zhang, Hao Wu, Paramjit S. Arora
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications
Nature Communications
Protein-protein interactions featuring intricate binding epitopes remain challenging targets for synthetic inhibitors. Interactions of NEMO, a scaffolding protein central to NF-κB signaling, exemplify this challenge. Various regulators are known to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6650e4f189316ffca5a4499439ab6ed
https://doaj.org/article/c91a73658de949548aa1a6962b0fe8cd
https://doaj.org/article/c91a73658de949548aa1a6962b0fe8cd
Autor:
Qi Qiao, Humayun Sharif, Liudmila Andreeva, Li Wang, Wei Li Wang, Arthur V. Hauenstein, Venkat Giri Magupalli, Youdong Mao, Gabriel Núñez, Hao Wu, Zhaolong Wu
Publikováno v:
Nature. 570:338-343
The NLRP3 inflammasome can be activated by stimuli that include nigericin, uric acid crystals, amyloid-β fibrils and extracellular ATP. The mitotic kinase NEK7 licenses the assembly and activation of the NLRP3 inflammasome in interphase. Here we rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63d72d6df00137e31ca811614232b4db
https://doi.org/10.1038/s41586-019-1295-z
https://doi.org/10.1038/s41586-019-1295-z
Autor:
Humayun, Sharif, Li, Wang, Wei Li, Wang, Venkat Giri, Magupalli, Liudmila, Andreeva, Qi, Qiao, Arthur V, Hauenstein, Zhaolong, Wu, Gabriel, Núñez, Youdong, Mao, Hao, Wu
Publikováno v:
Nature
The NLRP3 inflammasome can be activated by stimuli that include nigericin, uric acid crystals, amyloid-β fibrils and extracellular ATP. The mitotic kinase NEK7 licenses the assembly and activation of the NLRP3 inflammasome in interphase. Here we rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::4c44d3a91560efb08de7c1a81e5c78a6
http://europepmc.org/articles/PMC6774351
http://europepmc.org/articles/PMC6774351
Autor:
Smarajit Polley, De-Bin Huang, Arthur V Hauenstein, Amanda J Fusco, Xiangyang Zhong, Don Vu, Bärbel Schröfelbauer, Youngchang Kim, Alexander Hoffmann, Inder M Verma, Gourisankar Ghosh, Tom Huxford
Publikováno v:
PLoS Biology, Vol 11, Iss 6, p e1001581 (2013)
Activation of the IκB kinase (IKK) is central to NF-κB signaling. However, the precise activation mechanism by which catalytic IKK subunits gain the ability to induce NF-κB transcriptional activity is not well understood. Here we report a 4 Å x-r
Externí odkaz:
https://doaj.org/article/43e7e959d3ba4586a7f0c6da67fd6cc8
Autor:
Katherine A. Fitzgerald, Humayun Sharif, Yuzi Tian, Tomas Kirchhausen, Hasan B. Alam, Jun Jacob Hu, Pontus Orning, Venkat Giri Magupalli, Arthur V. Hauenstein, Jonathan C. Kagan, Roberto Negro, Zoltan Maliga, Florian I. Schmidt, Charles L. Evavold, Qiufang Deng, Yongqing Li, Wesley Skillern, Giuseppe Di Caprio, Hao Wu
Publikováno v:
Science
The MTOC is “speck”-tacular Inflammasome complexes are formed in response to pathogen-associated molecules. They initiate both the maturation of inflammatory cytokines and pyroptosis, a type of programmed cell death. One notable feature for infla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f38e7bb9f472840a2b6f720ef45fdab
https://europepmc.org/articles/PMC7814939/
https://europepmc.org/articles/PMC7814939/
Autor:
Arthur V. Hauenstein, Li Wang
Publikováno v:
Molecular Aspects of Medicine. 76:100889
NLRP3 is the best characterized cytosolic nod-like pattern recognition receptor which can detect microbial motifs, endogenous danger and stress signals. Activation of NLRP3 leads to the formation of a cytosolic multiprotein signaling complex called t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3f5a988e2a746ef824a91b91a7da9bb
https://doi.org/10.1016/j.mam.2020.100889
https://doi.org/10.1016/j.mam.2020.100889
Autor:
Anthony C. Liang, Pengda Liu, Wenyi Wei, Wenjian Gan, Arthur V. Hauenstein, Ming Xu, Tian-Min Fu, Bradley B. Brasher, Carsten Schwerdtfeger, Siyuan Su
Publikováno v:
Science Signaling. 11
Polyubiquitylation is canonically viewed as a posttranslational modification that governs protein stability or protein-protein interactions, in which distinct polyubiquitin linkages ultimately determine the fate of modified protein(s). We explored wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5858ef14ad1316ff6b32b2e06f291a79
https://doi.org/10.1126/scisignal.aar8133
https://doi.org/10.1126/scisignal.aar8133
Autor:
Banumathi Sankaran, Sanford I. Bernstein, Valerie Engelke, Tom Huxford, Chi F. Lee, Jonathan K. Fleming, Arthur V. Hauenstein, William C. Gasper
Publikováno v:
Structure. 19(3):397-408
UCS proteins, such as UNC-45, influence muscle contraction and other myosin-dependent motile processes. We report the first x-ray crystal structure of a UCS domain-containing protein, the UNC-45 myosin chaperone from Drosophila melanogaster (DmUNC-45
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e0dc755bcda04d2cb4454920c62807e
Autor:
W. Eric Rogers, De-Bin Huang, Tom Huxford, Jacob D. Shaul, Gourisankar Ghosh, Arthur V. Hauenstein
Publikováno v:
Biochemistry, vol 53, iss 12
Biochemistry
Biochemistry
Catalytic subunits of the IκB kinase (IKK), IKK1/IKKα, and IKK2/IKKβ function in vivo as dimers in association with the necessary scaffolding subunit NEMO/IKKγ. Recent X-ray crystal structures of IKK2 suggested that dimerization might be mediated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::849b6dc32beebcb55f29fd0010b46938
https://escholarship.org/uc/item/9273917j
https://escholarship.org/uc/item/9273917j
Autor:
Arthur V. Hauenstein, Banumathi Sankaran, Sanford I. Bernstein, William C. Gasper, Tom Huxford, Chi F. Lee
Publikováno v:
Biophysical Journal. (3):34a
UNC-45 is a chaperone that may aid in folding myosin's motor domain. Mutations in UNC-45 cause muscle defects and dysfunction, due to the importance of myosin in muscle structure and contraction. UNC-45 is composed of an N-terminal tetra-tricopeptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2a0db7cc4b95d813eb529efa4637439