Reference health
Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
31/31 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
1 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 31 checked references that resolve
resolves10.1126/science.278.5346.2123
Alignment of Conduits for the Nascent Polypeptide Chain in the Ribosome-Sec61 Complex
resolves10.1016/0022-2836(74)90408-2
Ribosomal-membrane interaction: In vitro binding of ribosomes to microsomal membranes
resolves10.1016/0378-1119(93)90046-6
The efficiency and versatility of catalytic RNA: implications for an RNA world
resolves10.1016/0092-8674(94)90424-3
Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
resolves10.1038/349806a0
Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
resolves10.1074/jbc.270.34.20106
SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase
resolves10.1002/j.1460-2075.1996.tb00492.x
A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.
resolves10.1016/0092-8674(93)90483-7
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
resolves10.1016/0092-8674(92)90517-G
A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
resolves10.1093/nar/21.13.3055
A compilation of large subunit (23S and 23S-like) ribosomal RNA structures: 1993
resolves10.1016/S0092-8674(00)81391-4
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
resolves10.1038/367654a0
Evolutionary conservation of components of the protein translocation complex
resolves10.1016/0092-8674(95)90313-5
A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
resolves10.1083/jcb.126.4.925
Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex.
resolves10.1083/jcb.141.4.887
The β Subunit of the Sec61 Complex Facilitates Cotranslational Protein Transport and Interacts with the Signal Peptidase during Translocation
resolves10.1002/j.1460-2075.1994.tb06713.x
Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.
resolves10.1091/mbc.9.1.103
Binding of Signal Recognition Particle Gives Ribosome/Nascent Chain Complexes a Competitive Advantage in Endoplasmic Reticulum Membrane Interaction
resolves10.1126/science.1604315
Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures
resolves10.1016/0092-8674(95)90077-2
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
resolves10.1016/0092-8674(83)90352-5
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation
resolves10.1002/j.1460-2075.1991.tb07699.x
One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.
resolves10.1006/jmbi.1996.0119
Comprehensive Comparison of Structural Characteristics in Eukaryotic Cytoplasmic Large Subunit (23 S-like) Ribosomal RNA
resolves10.1074/jbc.272.4.2053
FtsY, the Prokaryotic Signal Recognition Particle Receptor Homologue, Is Essential for Biogenesis of Membrane Proteins
resolves10.1073/pnas.75.2.814
Nascent peptide as sole attachment of polysomes to membranes in bacteria.
resolves10.1016/S0092-8674(00)81839-5
The E. coli Signal Recognition Particle Is Required for the Insertion of a Subset of Inner Membrane Proteins
resolves10.1038/269118a0
Three-dimensional model of membrane-bound ribosomes obtained by electron microscopy
resolves10.1083/jcb.91.2.557
Translocation 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.
The 1 reference without a DOI — listed, not checked
no DOI — not checkedBrimacombe R (1995) The structure of ribosomal RNA: a three‐dimensional jigsaw puzzle. Eur J Biochem, 230, 365–383.
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