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Martin R Pool

Showing results (11-20 of 22) with videos related to

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Biochemistry|January 7, 2004
Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognitionLionel Terzi, Martin R Pool, Bernhard Dobberstein, et al.
Plos Biology|June 10, 2011
N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumGabriella M A Forte, Martin R Pool, Colin J Stirling
Wiley Interdisciplinary Reviews. RNA|July 24, 2024
Orchestrated centers for the production of proteins or "translation factories"Robert A Crawford, Matthew Eastham, Martin R Pool, et al.
The Journal of Cell Biology|September 28, 2011
Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the transloconPen-Jen Lin, Candice G Jongsma, Martin R Pool, et al.
Science (New York, N.Y.)|August 24, 2002
Distinct modes of signal recognition particle interaction with the ribosomeMartin R Pool, Joachim Stumm, Tudor A Fulga, et al.
The EMBO Journal|July 2, 2004
Signal recognition particle mediates post-translational targeting in eukaryotesBenjamin M Abell, Martin R Pool, Oliver Schlenker, et al.
Nature Communications|December 5, 2015
Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationBhalchandra Jadhav, Michael McKenna, Nicholas Johnson, et al.
Science (New York, N.Y.)|May 6, 2006
Signal recognition particle receptor exposes the ribosomal translocon binding siteMario Halic, Marco Gartmann, Oliver Schlenker, et al.
Nature|November 7, 2006
Following the signal sequence from ribosomal tunnel exit to signal recognition particleMario Halic, Michael Blau, Thomas Becker, et al.
Nature|February 27, 2004
Structure of the signal recognition particle interacting with the elongation-arrested ribosomeMario Halic, Thomas Becker, Martin R Pool, et al.
Pageof 3

Showing results (11-20 of 22) with videos related to

Sort By:
Pageof 3
Biochemistry|January 7, 2004
Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognitionLionel Terzi, Martin R Pool, Bernhard Dobberstein, et al.
Plos Biology|June 10, 2011
N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumGabriella M A Forte, Martin R Pool, Colin J Stirling
Wiley Interdisciplinary Reviews. RNA|July 24, 2024
Orchestrated centers for the production of proteins or "translation factories"Robert A Crawford, Matthew Eastham, Martin R Pool, et al.
The Journal of Cell Biology|September 28, 2011
Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the transloconPen-Jen Lin, Candice G Jongsma, Martin R Pool, et al.
Science (New York, N.Y.)|August 24, 2002
Distinct modes of signal recognition particle interaction with the ribosomeMartin R Pool, Joachim Stumm, Tudor A Fulga, et al.
The EMBO Journal|July 2, 2004
Signal recognition particle mediates post-translational targeting in eukaryotesBenjamin M Abell, Martin R Pool, Oliver Schlenker, et al.
Nature Communications|December 5, 2015
Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationBhalchandra Jadhav, Michael McKenna, Nicholas Johnson, et al.
Science (New York, N.Y.)|May 6, 2006
Signal recognition particle receptor exposes the ribosomal translocon binding siteMario Halic, Marco Gartmann, Oliver Schlenker, et al.
Nature|November 7, 2006
Following the signal sequence from ribosomal tunnel exit to signal recognition particleMario Halic, Michael Blau, Thomas Becker, et al.
Nature|February 27, 2004
Structure of the signal recognition particle interacting with the elongation-arrested ribosomeMario Halic, Thomas Becker, Martin R Pool, et al.
Pageof 3