Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Peter, Gegenheimer"'
Autor:
Venkat, Gopalan, Timothy, Nilsen, Ann M, Altman, Benjamin C, Stark, Sheldon I, Feinstein, Ray, Koski, Cristina, Mickiewicz, Ben, Stark, Peter, Gegenheimer, Leif A, Kirsebom, John George, Arnez, Anthony C, Forster, Sergei A, Kazakov, Yan, Yuan, Fenyong, Liu, Nayef, Jarrous, Li, Yang, Ge, Jiang, Taijiao, Jiang, Joel L, Rosenbaum, George, Miller, Daniel, DiMaio, John R, Carlson, William H, McClain, Michael B, Mathews, Raymond, Kaempfer, Murray P, Deutscher, Ling-Ling, Chen, Yong, Li, Enduo, Wang, Olga, Patutina, Marina, Zenkova, Valentin, Vlassov, Julius B, Lucks
Publikováno v:
RNA (New York, N.Y.). 28(11)
Autor:
Julius B. Lucks, Olga Patutina, Yong Li, Ling-Ling Chen, Murray P. Deutscher, Raymond Kaempfer, Michael B. Mathews, William H. McClain, John R. Carlson, Daniel DiMaio, George Miller, Joel L. Rosenbaum, Li Yang, Nayef Jarrous, Fenyong Liu, Yan Yuan, Sergei A. Kazakov, Anthony C. Forster, John George Arnez, Leif A. Kirsebom, Peter Gegenheimer, Ray Koski, Sheldon I. Feinstein, Benjamin C. Stark, Ann M. Altman, Venkat Gopalan, Timothy Nilsen, Cristina Mickiewicz, Ben Stark, Ge Jiang, Taijiao Jiang, Enduo Wang, Marina Zenkova, Valentin Vlassov
Publikováno v:
RNA. 28:1393-1429
Autor:
Géraldine Bonnard, Franziska Pinker, Bernard Gutmann, Philippe Giegé, Peter Gegenheimer, Claude Sauter, Kamel Hammani, Anthony Gobert
Publikováno v:
RNA Biology
A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset of PPR proteins called PRORP possesses RNase P activity in several eukaryotes, both in nuclei and or
Publikováno v:
RNA. 6:545-553
The transfer RNA 59 maturation enzyme RNase P has been characterized in Bacteria, Archaea, and Eukarya. The purified enzyme from all three kingdoms is a ribonucleoprotein containing an essential RNA subunit; indeed, the RNA subunit of bacterial RNase
Publikováno v:
RNA. 6:554-562
Ribonuclease P is the enzyme responsible for removing the 5'-leader segment of precursor transfer RNAs in all organisms. All eukaryotic nuclear RNase Ps are ribonucleoproteins in which multiple protein components and a single RNA species are required
Publikováno v:
Journal of Biological Chemistry. 274:13824-13829
It has been suggested that the last seven to nine amino acid residues at the C terminus of the gamma subunit of the ATP synthase act as a spindle for rotation of the gamma subunit with respect to the alpha beta subunits during catalysis (Abrahams, J.
Autor:
Peter Gegenheimer
Publikováno v:
Molecular Biology Reports. 22:147-150
Chloroplasts of land plants have an active transfer RNA processing system, consisting of an RNase P-like 5' endonuclease, a 3' endonuclease, and a tRNA:CCA nucleotidyltransferase. The specificity of these enzymes resembles more that of their eukaryot
Autor:
Peter Gegenheimer
Publikováno v:
RNA. 6:1695-1697
Altman and colleagues (this issue) call attention to the inability of current standardized enzyme nomenclature to distinguish between enzymatic activities that reside in nonhomologous macromolecules+ This issue is highlighted by the fact that the pre
Autor:
Fei Gao, Cindy L. Berrie, Mark L. Richter, Hardeep S. Samra, Feng He, Etter Hoang, Zugen Chen, Peter Gegenheimer
Publikováno v:
The Journal of biological chemistry. 281(41)
The gamma subunit of the F1 portion of the chloroplast ATP synthase contains a critically placed dithiol that provides a redox switch converting the enzyme from a latent to an active ATPase. The switch prevents depletion of intracellular ATP pools in
Publikováno v:
Photosynthesis: Mechanisms and Effects ISBN: 9780792355472
The ATP synthase enzymes of the inner membranes of mitochondria, chloroplasts and of the bacterial cytoplasmic membrane, couple the energy of a transmembrane electrochemical proton gradient to the synthesis of ATP from ADP and inorganic phosphate. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::69628fbd580a7fd1c8a56cb72d0a6224
https://doi.org/10.1007/978-94-011-3953-3_390
https://doi.org/10.1007/978-94-011-3953-3_390