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Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum

https://doi.org/10.1261/rna.721108
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42/42 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 42 checked references that resolve
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Genome-Scale Identification of Membrane-Associated Human mRNAs
resolves10.1038/75603
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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle.
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The signal recognition particle in S. cerevisiae
resolves10.1083/jcb.109.6.3223
Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth.
resolves10.1091/mbc.E04-05-0398
mRNA Localization and ER-based Protein Sorting Mechanisms Dictate the Use of Transitional Endoplasmic Reticulum-Golgi Units Involved in Gurken Transport in <i>Drosophila</i> Oocytes
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resolves10.1083/jcb.65.3.513
Direct association of messenger RNA with microsomal membranes in human diploid fibroblasts.
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resolves10.1261/rna.2318906
mRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation
resolves10.1261/rna.5610403
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resolves10.1038/270630a0
Direct association of Balbiani ring 75S RNA with membranes of the endoplasmic reticulum
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resolves10.1016/j.ymeth.2006.06.003
Isolation and fractionation of rat liver nuclear envelopes and nuclear pore complexes
resolves10.1038/297647a0
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resolves10.1016/0022-2836(74)90522-1
Membrane-bound polyribosomes in HeLa cells: Association of polyadenylic acid with membranes
resolves10.1083/jcb.90.2.495
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resolves10.1091/mbc.12.3.577
Multifaceted Physiological Response Allows Yeast to Adapt to the Loss of the Signal Recognition Particle-dependent Protein-targeting Pathway
resolves10.1139/o05-147
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resolves10.1091/mbc.3.8.895
Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.
resolves10.1146/annurev.cellbio.17.1.569
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resolves10.1016/0092-8674(85)90200-4
Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency
resolves10.1091/mbc.E04-03-0184
Differential Regulation of the TRAIL Death Receptors DR4 and DR5 by the Signal Recognition Particle
resolves10.1038/nrm1643
Moving messages: the intracellular localization of mRNAs
resolves10.1091/mbc.E05-07-0685
Stable Ribosome Binding to the Endoplasmic Reticulum Enables Compartment-specific Regulation of mRNA Translation
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Analysis of mRNA Partitioning Between the Cytosol and Endoplasmic Reticulum Compartments of Mammalian Cells
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Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein.
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Signal Sequence Recognition and Protein Targeting to the Endoplasmic Reticulum Membrane
resolves10.1042/bj3070679
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resolves10.1093/nar/gkg595
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The 2 references without a DOI — listed, not checked
no DOI — not checkedAlberts, B. Johnson, A. Lewis, J. Raff, M. Roberts, K. Walter, P. (2002) Molecular Biology of the Cell (Garland Science, New York).
no DOI — not checkedEarly events in the biosynthesis of secretory and membrane proteins: The signal hypothesis
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