M
Martin R. Pool
Researcher at University of Manchester
Publications - 30
Citations - 2335
Martin R. Pool is an academic researcher from University of Manchester. The author has contributed to research in topics: Signal recognition particle & Endoplasmic reticulum. The author has an hindex of 19, co-authored 29 publications receiving 2182 citations. Previous affiliations of Martin R. Pool include Albert Einstein College of Medicine & Heidelberg University.
Papers
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Journal ArticleDOI
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
Mario Halic,Thomas Becker,Martin R. Pool,Christian M. T. Spahn,Robert A. Grassucci,Robert A. Grassucci,Joachim Frank,Joachim Frank,Roland Beckmann +8 more
TL;DR: The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.
Journal ArticleDOI
Following the signal sequence from ribosomal tunnel exit to signal recognition particle.
Mario Halic,Michael Blau,Thomas Becker,Thorsten Mielke,Martin R. Pool,Klemens Wild,Irmgard Sinning,Roland Beckmann +7 more
TL;DR: An ensemble of structures at subnanometre resolution is presented, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome–SRP complexes, and providing the structural basis for improving the understanding of the early steps of co-translational protein sorting.
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Distinct Modes of Signal Recognition Particle Interaction with the Ribosome
TL;DR: Using protein cross-linking, this work detected distinct modes in the binding of SRP to the ribosome that may allow the translocon to dock with the Ribosome, leading to insertion of the signal peptide into the translocation channel.
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Co-translational targeting and translocation of proteins to the endoplasmic reticulum.
TL;DR: The current understanding of this translocation pathway is reviewed and how molecular details obtained in the related bacterial system have provided insight into the mechanism of targeting and translocation are reviewed.
Journal ArticleDOI
N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
TL;DR: A systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the secretory pathway found an equal and opposite bias against such modification for secretory proteins.