about
Circularly permuted tRNA genes: their expression and implications for their physiological relevance and developmentMechanistic and Structural Studies of Protein-Only RNase P Compared to Ribonucleoproteins Reveal the Two Faces of the Same Enzymatic ActivityMultiple Layers of Stress-Induced Regulation in tRNA BiologyFootprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.tRNA biology in mitochondriaCleavage of Model Substrates by Arabidopsis thaliana PRORP1 Reveals New Insights into Its Substrate RequirementsStructural mechanisms of RNA recognition: sequence-specific and non-specific RNA-binding proteins and the Cas9-RNA-DNA complex.Biophysical analysis of Arabidopsis protein-only RNase P alone and in complex with tRNA provides a refined model of tRNA binding.Ligand-dependent ribozymes.Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P.RNase P RNA from the recently evolved plastid of Paulinella and from algaeDistribution of Ribonucleoprotein and Protein-Only RNase P in Eukarya.Transfer RNA maturation in Chlamydomonas mitochondria, chloroplast and the nucleus by a single RNase P protein.Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.The mitochondrial transcriptome
P2860
Q21131234-DE214015-1CF1-4828-AAB5-72790EA3CBCCQ26746979-84019A88-5A0F-494F-ADAC-7C41049B7434Q26749584-A7F8BCD0-295C-475D-A3BA-0FF6220F7BF6Q27932506-7683E838-F5CA-4BDC-8042-FEF9891BD65BQ28080757-57207270-9A4E-4922-9FFA-14BFBF1B0345Q36095934-B7B1D5C0-5078-45A9-810A-F8D62510065DQ38272498-2DF2F853-7542-4F25-A56B-FD45A005DC95Q38684465-486F6DE9-87A7-4BAE-8030-4203E6ED90C2Q38968316-4A7B8D16-27B4-4806-A47D-B87A23736F1EQ39142994-E4056654-D04F-4491-B18A-5C2E966077A2Q40364054-0D477ECB-9DD7-4644-A535-F89DCA809110Q42583926-7A72B0B4-7309-4A9E-833B-C9AA79248CA9Q44434425-B5524DFD-A731-47B5-95EA-6546825426B3Q50228759-7BFD7470-2FD7-403A-9779-1F7742D8B59EQ52329870-1B6A8CB8-E226-413D-A56B-26D48AFBB566Q57166159-2E945C10-7B22-4469-9DFF-DACE3C6E5F35
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 19 June 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
PPR proteins shed a new light on RNase P biology.
@en
PPR proteins shed a new light on RNase P biology.
@nl
type
label
PPR proteins shed a new light on RNase P biology.
@en
PPR proteins shed a new light on RNase P biology.
@nl
prefLabel
PPR proteins shed a new light on RNase P biology.
@en
PPR proteins shed a new light on RNase P biology.
@nl
P2093
P2860
P921
P356
P1433
P1476
PPR proteins shed a new light on RNase P biology.
@en
P2093
Anthony Gobert
Bernard Gutmann
Claude Sauter
Franziska Pinker
Géraldine Bonnard
Kamel Hammani
Peter A Gegenheimer
Philippe Giegé
P2860
P304
P356
10.4161/RNA.25273
P577
2013-06-19T00:00:00Z