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March 1, 1993The Journal of Cell BiologyOpen Access

GTPase domain of the 54-kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding.

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Authors

DZDieter ZopfBayer (Germany)HBHarris D. BernsteinNational Institute of Diabetes and Digestive and Kidney Diseases
Peter Walter
Peter WalterQB3

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Zopf et al. (1993) studied this question.

synapsesocial.com/papers/6a76ca0d137c7dcc81bd6872https://doi.org/10.1083/jcb.120.5.1113
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The signal sequence interacts with the methionine-rich domain of the 54-kD protein of signal recognition particle.1991 · 97 citations
  2. 2Requirement of GTP Hydrolysis for Dissociation of the Signal Recognition Particle from Its Receptor1991 · 223 citations
  3. 3Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.1981 · 820 citations
  4. 4Mechanism of Protein Translocation Across the Endoplasmic Reticulum Membrane1986 · 515 citations
  5. 5Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA.1990 · 87 citations