about
Signal recognition particle mediates post-translational targeting in eukaryotesStructure and Switch Cycle of SRβ as Ancestral Eukaryotic GTPase Associated with Secretory MembranesFollowing the signal sequence from ribosomal tunnel exit to signal recognition particleN-terminal acetylation inhibits protein targeting to the endoplasmic reticulumSignal recognition particle receptor exposes the ribosomal translocon binding site.Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review).Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationCo-translational targeting and translocation of proteins to the endoplasmic reticulum.Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation.Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum.Protein targeting and translocation; a comparative survey.Structure of the signal recognition particle interacting with the elongation-arrested ribosome.Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC.A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase.Cell biology: Sort of unexpected.The perplexing PEXEL protein secretory pathway
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description
onderzoeker
@nl
researcher
@en
հետազոտող
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name
Martin R Pool
@ast
Martin R Pool
@en
Martin R Pool
@es
Martin R Pool
@nl
type
label
Martin R Pool
@ast
Martin R Pool
@en
Martin R Pool
@es
Martin R Pool
@nl
prefLabel
Martin R Pool
@ast
Martin R Pool
@en
Martin R Pool
@es
Martin R Pool
@nl
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