Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Greg L. Hersch"'
Publikováno v:
ICHI
Natural language processing (NLP) of clinical trial documents can be useful in new trial design. Here we identify entity types relevant to clinical trial design and propose a framework called CT-BERT for information extraction from clinical trial tex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62e726a91bc3703ccdd32094d7c3b79e
https://doi.org/10.1109/ichi52183.2021.00092
https://doi.org/10.1109/ichi52183.2021.00092
Publikováno v:
IEEE BigData
COVID-19 clinical trial design is a critical task in developing therapeutics for the prevention and treatment of COVID-19. In this study, we apply a deep learning approach to extract eligibility criteria variables from COVID-19 trials to enable quant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0a549578c445252d27530749c8a7d05
http://arxiv.org/abs/2012.10063
http://arxiv.org/abs/2012.10063
Autor:
Elizabeth S.C. Oakes, Igor Levchenko, David A. Wah, Robert T. Sauer, Samia M. Siddiqui, Robert A. Grant, Tania A. Baker, Daniel N. Bolon, Shilpa A. Joshi, Jon A. Kenniston, Julia M. Flynn, Randall E. Burton, Saskia B. Neher, Briana M. Burton, Greg L. Hersch
Publikováno v:
Cell. 119(1):9-18
Machines of protein destruction—including energy-dependent proteases and disassembly chaperones of the AAA+ ATPase family—function in all kingdoms of life to sculpt the cellular proteome, ensuring that unnecessary and dangerous proteins are elimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::839ade293e7f45d8a54ca40c09ec4c81
Publikováno v:
Nature Structural & Molecular Biology. 11:404-411
In the ClpXP compartmental protease, ring hexamers of the AAA(+) ClpX ATPase bind, denature and then translocate protein substrates into the degradation chamber of the double-ring ClpP(14) peptidase. A key question is the extent to which functional c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cc5a077b8791ca9e9a3efa044c7bc5b
https://doi.org/10.1038/nsmb752
https://doi.org/10.1038/nsmb752
Publikováno v:
Molecular Cell. 13:443-449
SspB homodimers deliver ssrA-tagged substrates to ClpXP for degradation. SspB consists of a substrate binding domain and an unstructured tail with a ClpX binding module (XB). Using computational design, we engineered an SspB heterodimer whose subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b48fcfc47a016f76d365b1dbecb6cf6
https://doi.org/10.1016/s1097-2765(04)00027-9
https://doi.org/10.1016/s1097-2765(04)00027-9
The ssrA-degradation tag sequence contains contiguous binding sites for the SspB adaptor and the ClpX component of the ClpXP protease. Although SspB normally enhances ClpXP degradation of ssrA-tagged substrates, it inhibits proteolysis under conditio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3319d96dce76fb28ac8c3fb362372265
https://europepmc.org/articles/PMC514447/
https://europepmc.org/articles/PMC514447/
Publikováno v:
Molecular cell. 13(3)
SspB homodimers deliver ssrA-tagged substrates to ClpXP for degradation. SspB consists of a substrate binding domain and an unstructured tail with a ClpX binding module (XB). Using computational design, we engineered an SspB heterodimer whose subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::180b799d6d8353d55c9c26a89d06af89
https://pubmed.ncbi.nlm.nih.gov/14967151
https://pubmed.ncbi.nlm.nih.gov/14967151
Publikováno v:
Cell. (7):1017-1027
Summary ATP hydrolysis by AAA+ ClpX hexamers powers protein unfolding and translocation during ClpXP degradation. Although ClpX is a homohexamer, positive and negative allosteric interactions partition six potential nucleotide binding sites into thre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbe57ba9d6c38b441eb7f299cb172689