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Identification and Subcellular Localization of Protein Transport Protein Sec61α and Sec61γ in Nosema Bombycis

https://doi.org/10.2139/ssrn.4097561
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29/29 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.

9 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 29 checked references that resolve
resolves10.1038/nature03670
Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1
resolves10.1242/jcs.03402
Analogs of the Golgi complex in microsporidia: structure and avesicular mechanisms of function
resolves10.1242/jcs.054494
Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum
resolves10.1111/boc.201800030
Sec61 blockade by mycolactone: A central mechanism in Buruli ulcer disease
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.
resolves10.1242/jcs.112.10.1477
The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment
resolves10.1139/bcb-2014-0043
Protein transport into the human ER and related diseases, Sec61-channelopathies
resolves10.1093/infdis/jir324
Contribution of Sec61α to the Life Cycle of Ebola Virus
resolves10.1016/S0966-842X(97)01185-2
Origins of microsporidia
resolves10.1091/mbc.7.5.769
Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations.
resolves10.3389/fphys.2017.00887
An Update on Sec61 Channel Functions, Mechanisms, and Related Diseases
resolves10.1038/sigtrans.2017.2
Let’s talk about Secs: Sec61, Sec62 and Sec63 in signal transduction, oncology and personalized medicine
resolves10.2337/db08-1362
A Point Mutation in Sec61α1 Leads to Diabetes and Hepatosteatosis in Mice
resolves10.7554/eLife.01483
An allosteric Sec61 inhibitor traps nascent transmembrane helices at the lateral gate
resolves10.1242/jcs.198655
Mycolactone reveals the substrate-driven complexity of Sec61-dependent transmembrane protein biogenesis
resolves10.1038/s41419-018-0427-y
Inhibition of Sec61-dependent translocation by mycolactone uncouples the integrated stress response from ER stress, driving cytotoxicity via translational activation of ATF4
resolves10.1146/annurev.cellbio.21.012704.133214
PROTEIN TRANSLOCATION BY THE SEC61/SECY CHANNEL
resolves10.1016/j.chembiol.2016.04.008
Apratoxin Kills Cells by Direct Blockade of the Sec61 Protein Translocation Channel
resolves10.1146/annurev-biophys-050511-102312
Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes
resolves10.1080/19336950.2015.1125737
Sec61: A static framework for membrane-protein insertion
resolves10.1111/1574-6968.12198
Identification of two new polar tube proteins related to polar tube protein 2 in the microsporidian<i>Antonospora locustae</i>
resolves10.1242/jcs.112.23.4185
Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane
resolves10.1016/j.exppara.2004.12.011
Entamoeba histolytica: intracellular distribution of the sec61α subunit of the secretory pathway and down-regulation by antisense peptide nucleic acids
resolves10.1038/emboj.2012.189
BiP‐mediated closing of the Sec61 channel limits Ca2+ leakage from the ER
resolves10.1016/j.jaci.2017.06.042
Plasma cell deficiency in human subjects with heterozygous mutations in Sec61 translocon alpha 1 subunit (SEC61A1)
resolves10.1016/j.jmb.2006.04.028
Characterization of a Divergent Sec61β Gene in Microsporidia
resolves10.1016/B978-0-12-407706-5.00004-6
Microsporidia and ‘The Art of Living Together’
resolves10.1002/9781118395264.ch10
The Microsporidian Polar Tube and Spore Wall
resolves10.1007/s10875-016-0250-0
Components and Mechanisms of Import, Modification, Folding, and Assembly of Immunoglobulins in the Endoplasmic Reticulum
The 9 references without a DOI — listed, not checked
no DOI — not checkedMicrosporidia: Obligate Intracellular Pathogens Within the Fungal Kingdom
no DOI — not checkedDecatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon
no DOI — not checkedMolecular and biochemical responses in the midgut of the silkworm, Bombyx mori, infected with Nosema bombycis
no DOI — not checkedComparative genomics of parasitic silkworm microsporidia reveal an association between genome expansion and host adaptation
no DOI — not checkedCCT? colocalizes with actin and ?-tubulin: Insight into its involvement in the cytoskeleton formation of the intracellular parasite Nosema bombycis
no DOI — not checkedref30
no DOI — not checkedref35
no DOI — not checkedA Complete Sec61 Complex in Nosema bombycis and Its Comparative Genomics Analyses
no DOI — not checkedPrimer sequences and restriction sites for gene amplification Name Primer sequence (5'-3') Target gene length Restriction sites NbSec61?-F
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

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