Empty Site Forms of the SRP54 and SRα GTPases Mediate Targeting of Ribosome–Nascent Chain Complexes to the Endoplasmic Reticulum
- 1 May 1997
- Vol. 89 (5) , 703-713
- https://doi.org/10.1016/s0092-8674(00)80253-6
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targetingNature, 1996
- The Srp54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe.Molecular and Cellular Biology, 1994
- GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor.The Journal of cell biology, 1993
- Requirement of GTP Hydrolysis for Dissociation of the Signal Recognition Particle from Its ReceptorScience, 1991
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990
- Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particleNature, 1989
- The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptideCell, 1989
- Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor.The Journal of cell biology, 1989
- Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.The Journal of cell biology, 1986