Synthesis of a cyclic tripeptide modelling the ?active? conformation of oxytocin

1977 ◽  
Vol 13 (3) ◽  
pp. 373-374
Author(s):  
E. I. Grigor'ev ◽  
E. A. Krol' ◽  
O. A. Kaurov
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pp. 1053-1061 ◽  
Author(s):  
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Damian Bartuzi ◽  
Dariusz Matosiuk

ChemMedChem ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. 1207-1216 ◽  
Author(s):  
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Giorgio Costa ◽  
Giorgio Cozza ◽  
Flavio Meggio ◽  
Leonardo Scapozza ◽  
...  

2002 ◽  
Vol 277 (20) ◽  
pp. 17970-17977 ◽  
Author(s):  
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Dierk Scheide ◽  
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Luitgard Nagel-Steger ◽  
Thorsten Friedrich

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Renata Grzela ◽  
Julien Nusbaum ◽  
Sonia Fieulaine ◽  
Francesco Lavecchia ◽  
Willy V. Bienvenut ◽  
...  

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Tao Li ◽  
Hee Jong Kim ◽  
Jose J. Gorbea Colón ◽  
Mitchell I. Parker ◽  
...  

During transcription initiation, the general transcription factor TFIIH marks RNA polymerase II by phosphorylating Ser5 of the carboxyl-terminal domain (CTD) of Rpb1, which is followed by extensive modifications coupled to transcription elongation, mRNA processing, and histone dynamics. We have determined a 3.5-Å resolution cryo–electron microscopy (cryo-EM) structure of the TFIIH kinase module (TFIIK in yeast), which is composed of Kin28, Ccl1, and Tfb3, yeast homologs of CDK7, cyclin H, and MAT1, respectively. The carboxyl-terminal region of Tfb3 was lying at the edge of catalytic cleft of Kin28, where a conserved Tfb3 helix served to stabilize the activation loop in its active conformation. By combining the structure of TFIIK with the previous cryo-EM structure of the preinitiation complex, we extend the previously proposed model of the CTD path to the active site of TFIIK.


1980 ◽  
Vol 68 (2) ◽  
pp. 139-146 ◽  
Author(s):  
B.Kenneth Koe ◽  
Susan W. Koch ◽  
Beryl W. Dominy

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