Reference health
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
48/48 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.
2 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 48 checked references that resolve
resolves10.1083/jcb.91.2.545
Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.
resolves10.1007/s10254-002-0002-9
Signal recognition particle-depencent protein targeting, universal to all kingdoms of life
resolves10.1016/0092-8674(88)90529-6
Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: Analysis of biochemical mutants of SRP
resolves10.1016/0092-8674(89)90129-3
The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
resolves10.1038/340482a0
Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
resolves10.1083/jcb.111.5.1793
The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain.
resolves10.1126/science.287.5456.1232
Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle
resolves10.1002/j.1460-2075.1990.tb07902.x
The methionine‐rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence.
resolves10.1126/science.1072366
Distinct Modes of Signal Recognition Particle Interaction with the Ribosome
resolves10.1038/320081a0
Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact
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.
resolves10.1083/jcb.109.6.2617
Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate.
resolves10.1093/emboj/19.15.4164
Elongation arrest is a physiologically important function of signal recognition particle
resolves10.1083/jcb.100.6.1913
Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane.
resolves10.1002/j.1460-2075.1987.tb02671.x
Evidence for an extended 7SL RNA structure in the signal recognition particle.
resolves10.1016/S0092-8674(01)00541-4
Architecture of the Protein-Conducting Channel Associated with the Translating 80S Ribosome
resolves10.1083/jcb.97.6.1693
Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe.
resolves10.1016/S0092-8674(01)00539-6
Structure of the 80S Ribosome from Saccharomyces cerevisiae—tRNA-Ribosome and Subunit-Subunit Interactions
resolves10.1038/nsb843
Induced structural changes of 7SL RNA during the assembly of human signal recognition particle
resolves10.1021/bi025765t
Systematic Site-Directed Mutagenesis of Human Protein SRP54: Interactions with Signal Recognition Particle RNA and Modes of Signal Peptide Recognition
resolves10.1016/S0969-2126(01)00641-4
The Conformation of Bound GMPPNP Suggests a Mechanism for Gating the Active Site of the SRP GTPase
resolves10.1073/pnas.2436132100
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
resolves10.1073/pnas.85.6.1801
Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined in protein-RNA "footprinting".
resolves10.1126/science.289.5481.905
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
resolves10.1038/35041507
Structure and assembly of the Alu domain of the mammalian signal recognition particle
resolves10.1261/rna.2196403
The signal recognition particle binds to protein L23 at the peptide exit of the <i>Escherichia coli</i> ribosome
resolves10.1083/jcb.200302130
Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the<i>Escherichia coli</i>ribosome
resolves10.1017/S1355838202020095
Crosslinking of 4.5S RNA to the Escherichia coli ribosome in the presence or absence of the protein Ffh
resolves10.1016/S0022-2836(02)01111-7
Structure of the Mammalian Ribosome–Channel Complex at 17Å Resolution
resolves10.1073/pnas.95.23.13425
A general mechanism for regulation of access to the translocon: Competition for a membrane attachment site on ribosomes
resolves10.1093/nar/25.10.1920
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle
resolves10.2174/1389203023380846
Protein Synthesis at Atomic Resolution: Mechanistics of Translation in the Light of Highly Resolved Structures for the Ribosome
resolves10.1093/emboj/19.11.2710
Three‐dimensional cryo‐electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 Å resolution
resolves10.1038/nsb1003
Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
resolves10.1002/j.1460-2075.1988.tb03233.x
Ribosome pausing and stacking during translation of a eukaryotic mRNA.
resolves10.1016/S0092-8674(05)80012-1
SRP samples nascent chains for the presenceof signal sequences by interacting with ribosomes at a discrete step during translation elongation
resolves10.1002/j.1460-2075.1991.tb08008.x
Changes in 7SL RNA conformation during the signal recognition particle cycle.
resolves10.1016/S0076-6879(83)96057-3
[53] Signal recognition particle: A ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties
resolves10.1016/0022-2836(88)90384-1
Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli
resolves10.1107/S0108767390010224
Improved methods for building protein models in electron density maps and the location of errors in these models
The 2 references without a DOI — listed, not checked
no DOI — not checkedSpahn, C. et al. Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J. (in the press)
no DOI — not checkedMartoglio, B., Hauser, S. & Dobberstein, B. in Cell Biology: A Laboratory Handbook (ed. Celis, J. C.) 265–273 (Academic, San Diego, 1997)
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