Zobrazeno 1 - 10
of 140
pro vyhledávání: '"Paul B. Sigler"'
Autor:
Yakov Korkhin, Ulug M Unligil, Otis Littlefield, Pamlea J Nelson, David I Stuart, Paul B Sigler, Stephen D Bell, Nicola G. A Abrescia
Publikováno v:
PLoS Biology, Vol 8, Iss 8 (2010)
Externí odkaz:
https://doaj.org/article/3a02b24003a84c5495a8d7f07769f657
Autor:
Yakov Korkhin, Ulug M Unligil, Otis Littlefield, Pamlea J Nelson, David I Stuart, Paul B Sigler, Stephen D Bell, Nicola G A Abrescia
Publikováno v:
PLoS Biology, Vol 7, Iss 5, p e1000102 (2009)
The archaeal RNA polymerase (RNAP) shares structural similarities with eukaryotic RNAP II but requires a reduced subset of general transcription factors for promoter-dependent initiation. To deepen our knowledge of cellular transcription, we have det
Externí odkaz:
https://doaj.org/article/8606eed1a0604377bdd45343053e2e4a
Autor:
Paul B. Sigler, Francis T.F. Tsai, Wah Chiu, Sukyeong Lee, Masasuke Yoshida, Yo-hei Watanabe, Mathew E. Sowa
Publikováno v:
Cell. 115(2):229-240
Molecular chaperones assist protein folding by facilitating their "forward" folding and preventing aggregation. However, once aggregates have formed, these chaperones cannot facilitate protein disaggregation. Bacterial ClpB and its eukaryotic homolog
Publikováno v:
Nature. 422:534-539
Transcription factor IIIB (TFIIIB), consisting of the TATA-binding protein (TBP), TFIIB-related factor (Brf1) and Bdp1, is a central component in basal and regulated transcription by RNA polymerase III. TFIIIB recruits its polymerase to the promoter
Publikováno v:
Journal of Biological Chemistry. 277:24694-24700
We have determined the x-ray crystal structure of the transcription factor NF-κB p50·p65 heterodimer complexed to κB DNA from the cytokine interferon β enhancer (IFNβ-κB). To better understand how the binding modes of NF-κB on its two best stu
Publikováno v:
Structure. 9:869-880
Background: Arrestins are responsible for the desensitization of many sequence-divergent G protein-coupled receptors. They compete with G proteins for binding to activated phosphorylated receptors, initiate receptor internalization, and activate addi
Publikováno v:
Journal of Molecular Biology. 302:303-313
GroEL-assisted protein folding is regulated by a cycle of large coordinated domain movements in the 14-subunit double-ring assembly. The transition path between the closed (unliganded) and the open (liganded) states, calculated with a targeted molecu
Autor:
Michael L. Moritz, David S. Geller, Richard P. Lifton, Francis T.F. Tsai, Paul B. Sigler, Adrian Spitzer, Gretchen Meinke, Nikki Pinkerton, Michael Fradley, Anita Farhi
Publikováno v:
Science. 289:119-123
Hypertension and pregnancy-related hypertension are major public health problems of largely unknown causes. We describe a mutation in the mineralocorticoid receptor (MR), S810L, that causes early-onset hypertension that is markedly exacerbated in pre
Autor:
Francis T.F. Tsai, Paul B. Sigler
Publikováno v:
The EMBO Journal. 19:25-36
Transcription initiation requires the assembly of a preinitiation complex (PIC), which is nucleated through binding of the TATA-box binding protein (TBP) to the promoter. Biochemical studies have shown, however, that TBP recognizes the TATA-box in bo
Autor:
Adele L. Boskey, Michael L. Shuler, Noel D. Jones, Gary S. Stein, Bi-Cheng Wang, William M. Miller, John Kuriyan, Paul B. Sigler
Publikováno v:
Journal of Cellular Biochemistry. 79:662-671
The recent National Research Council report, Future Biotechnology Research on the International Space Station, evaluates NASA's plans for research in cell science and protein crystal growth to be conducted on the International Space Station. This rep