Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Joyce E. Heckman"'
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:241-244
Poly(A) polymerase (PAP) synthesizes the polyadenine tail at the 3'-end of messenger RNA. A disulfide cross-linking strategy was implemented to obtain a complex between bovine PAP (bPAP) and a 15-mer oligo(A). All seven endogenous cysteines were muta
Publikováno v:
Biochemistry. 44:4148-4156
The hammerhead ribozyme has been intensively studied for approximately 15 years, but its cleavage mechanism is not yet understood. Crystal structures reveal a Y-shaped molecule in which the cleavage site is not ideally aligned for an S N2 reaction an
Autor:
John M. Burke, Dominic Lambert, Robert Pinard, Philip A. Chan, Joyce E. Heckman, François Major, Ken J. Hampel
Publikováno v:
The EMBO Journal. 20:6434-6442
The catalytic determinants for the cleavage and ligation reactions mediated by the hairpin ribozyme are integral to the polyribonucleotide chain. We describe experiments that place G8, a critical guanosine, at the active site, and point to an essenti
Publikováno v:
Journal of Molecular Biology. 287:239-251
The hairpin ribozyme-substrate complex contains two independently folding domains that interact with one another to form a catalytic complex. However, little is known about the key structural elements involved in these tertiary interactions. Here, we
Publikováno v:
Journal of Biological Chemistry. 273:23524-23533
Combinatorial libraries of hairpin ribozymes representing all possible cleavage specificities (>10(5)) were used to evaluate all ribozyme cleavage sites within a large (4.2-kilobase) and highly structured viral mRNA, the 26 S subgenomic RNA of Sindbi
Autor:
C.William Gundlach, Dominic Lambert, Ken J. Hampel, Gary D. Glick, Robert Pinard, Nils G. Walter, José A. Esteban, Joyce E. Heckman, François Major, John M. Burke
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
The two domains of the hairpin ribozyme-substrate complex, usually depicted as straight structural elements, must interact with one another in order to form an active conformation. Little is known about the internal geometry of the individual domains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b21a6619d89d926a9c295e748b1b2e4
http://hdl.handle.net/10261/39887
http://hdl.handle.net/10261/39887
The hairpin ribozyme acts as a reversible, site-specific endoribonuclease that ligates much more rapidly than it cleaves cognate substrate. While the reaction pathway for ligation is the reversal of cleavage, little is known about the atomic and elec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ab1a5fa188e4527a8ecf33dab594a67
https://europepmc.org/articles/PMC2151026/
https://europepmc.org/articles/PMC2151026/
Publikováno v:
Biochemistry. 45(23)
Native hammerhead ribozymes contain RNA domains that enable high catalytic activity under physiological conditions, where minimal hammerheads show little activity. However, little is known about potential differences in native versus minimal ribozyme
Autor:
Samuel E. Butcher, Aloke Raj Banerjee, John M. Burke, Nils G. Walter, José A. Esteban, Joyce E. Heckman, J. Bond, Alfredo Berzal-Herranz, Bruno Sargueil
Publikováno v:
ACS Symposium Series ISBN: 9780841235410
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
A wide range of experimental methods have been used to explore the structure and function of the hairpin ribozyme. In vitro selection methods has provided comprehensive information on RNA secondary structure and the identity of essential bases within
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59148a0da1f6ef929b5ebccd823e09f0
http://hdl.handle.net/10261/40053
http://hdl.handle.net/10261/40053