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Research report: Human EMC4 (UniProt Q5J8M3; gene EMC4; synonyms TMEM85, PIG17) — functional annotation

0) Target verification (mandatory)

The literature and database evidence retrieved here consistently match the UniProt-provided identity: human EMC4 = “ER membrane protein complex subunit 4”, encoded by EMC4 (Ensembl ENSG00000128463), and functioning as a subunit of the ER membrane protein complex (EMC). This aligns with UniProt Q5J8M3 (ER membrane protein complex subunit 4; TMEM85/ PIG17) and with Open Targets target metadata. (OpenTargets Search: -EMC4)

1) Key concepts and current understanding

1.1 What is EMC and what does it do?

The endoplasmic reticulum membrane protein complex (EMC) is an ER-localized, multi-subunit membrane protein biogenesis factor that acts as a co- and post-translational insertase for certain transmembrane helices (TMDs). Structural and biochemical evidence supports a model in which EMC provides a hydrophilic vestibule within the bilayer to reduce the energetic barrier for insertion of challenging TMDs (e.g., weakly hydrophobic tail-anchors), while also supporting later steps of folding/assembly for complex multipass clients. (pleiner2020structuralbasisfor pages 7-11, pleiner2020structuralbasisfor pages 1-3, odonnell2020thearchitectureof pages 1-2)

A central mechanistic concept is that EMC contains intramembrane cavities/surfaces that engage substrate TMDs and provide an “energy-independent” insertion route without nucleotide-binding domains. (odonnell2020thearchitectureof pages 1-2, odonnell2020thearchitectureof pages 2-4)

1.2 What is EMC4 specifically?

EMC4 is a membrane-embedded EMC subunit that (i) contributes to the architecture enclosing the insertase vestibule and (ii) participates in EMC’s client-facing surfaces.

A major update from 2023 is that improved cryo-EM maps unambiguously assign three transmembrane domains (TMDs) in human EMC4; EMC4, together with the single TMDs of EMC7 and EMC10, helps enclose the insertase vestibule. (pleiner2023aselectivityfilter pages 4-6)

Mechanistically, EMC4 is not merely a passive scaffold: EMC4 is found at the client-interaction environment (vestibule side) and can be crosslinked to substrates, consistent with a direct role in substrate handling. (pleiner2023aselectivityfilter pages 2-4, pleiner2023aselectivityfilter pages 19-23)

2) Structure, localization, and mechanistic role of EMC4

2.1 Subcellular localization

EMC (including EMC4) is localized to the endoplasmic reticulum membrane. This is directly supported by multiple human EMC structural studies performed on purified/reconstituted complexes and by functional assays in cells where EMC supports ER membrane insertion events. (pleiner2020structuralbasisfor pages 7-11, pleiner2020structuralbasisfor pages 1-3, odonnell2020thearchitectureof pages 1-2)

2.2 EMC architecture and where EMC4 sits

High-resolution cryo-EM defines the EMC as a tripartite assembly with cytosolic, membrane, and lumenal domains. In one foundational structure, the human EMC map was reported at ~3.4 Å overall resolution, with a prominent intramembrane hydrophilic vestibule formed by the conserved insertase core (EMC3/EMC6). (pleiner2020structuralbasisfor pages 1-3)

EMC4 is positioned adjacent to this insertase core and contributes to the vestibule enclosure:
* Pleiner et al. (J Cell Biol, 2023-05) show that the hydrophilic vestibule is partially enclosed by dynamic TMDs from EMC4/7/10, and that three EMC4 TMDs can be assigned in an improved reconstruction. (pleiner2023aselectivityfilter pages 4-6)
* Li et al. (Aging, 2024-03) likewise describe EMC4 as an ordered three-TMH bundle adjacent to EMC3/EMC6 that forms part of the sidewall of the hydrophilic vestibule, reinforcing EMC4’s direct role in shaping the substrate-binding/insertion environment. (li2024structuralinsightsinto pages 1-3)

2.3 Insertase mechanism and the EMC4 contribution

The EMC insertase is centered on the EMC3/EMC6 module that provides a hydrophilic vestibule for insertion. (pleiner2020structuralbasisfor pages 1-3, pleiner2023aselectivityfilter pages 4-6)

EMC4 contributes in three experimentally supported ways:
1. Vestibule enclosure and geometry: the vestibule is “partially enclosed” by EMC4/7/10 TMDs; EMC4 loss can impair incorporation of EMC7 and EMC10 into EMC, consistent with EMC4’s architectural role. (pleiner2023aselectivityfilter pages 4-6)
2. Direct substrate proximity: in substrate mapping, site-specific photocrosslinking and disulfide crosslinking detect substrate contacts not only with EMC3 but also with EMC4, consistent with EMC4 forming part of the client-facing surface of the vestibule. (pleiner2023aselectivityfilter pages 2-4, pleiner2023aselectivityfilter pages 19-23)
3. Functional requirement for tail-anchored biogenesis: EMC4 is required for biogenesis/insertion of the tail-anchored substrate squalene synthase (SQS/FDFT1) in the Pleiner et al. reporter systems. (pleiner2023aselectivityfilter pages 19-23, pleiner2023aselectivityfilter pages 23-26)

2.4 EMC selectivity filter (2023 mechanistic development)

Pleiner et al. (J Cell Biol, 2023-05) propose that the EMC hydrophilic vestibule acts as a selectivity filter that limits misinsertion/mislocalization by using charge-based discrimination.

Key points supported by experiments:
* The vestibule is positively charged and can repel substrates with positively charged soluble domains, helping enforce correct topology (“positive-inside” considerations) and preventing inappropriate ER insertion of mitochondrial tail-anchored proteins. (pleiner2023aselectivityfilter pages 6-8, pleiner2023aselectivityfilter pages 8-10)
* This work includes a sequence-scale analysis of 709 human GPCR sequences, and shows that even one added positive charge to an SQS reporter C-terminus can markedly reduce ER integration in cells and in vitro. (pleiner2023aselectivityfilter pages 6-8)

EMC4’s role here is primarily structural (enclosing the vestibule and contributing substrate-facing surfaces), whereas the most explicitly tested selectivity residues in text are on EMC3 (e.g., R31/R180). (pleiner2023aselectivityfilter pages 4-6, pleiner2023aselectivityfilter pages 8-10)

3) Recent developments (prioritizing 2023–2024)

3.1 2023: EMC4 resolved as a 3-TMD vestibule-enclosing subunit and mapped in substrate crosslinking

The 2023 J Cell Biol study improved assignment of EMC4 TMDs and provides multiple crosslinking modalities showing substrates can contact EMC4 at the vestibule side. (pleiner2023aselectivityfilter pages 4-6, pleiner2023aselectivityfilter pages 2-4, pleiner2023aselectivityfilter pages 19-23)

3.2 2023: EMC acts as a chaperone/holdase during CaV channel assembly; EMC4 participates

Chen et al. (Nature, 2023-05-) determined cryo-EM structures of an EMC-bound assembly intermediate for voltage-gated calcium channel CaV1.2, concluding that EMC functions as a holdase/chaperone during assembly. The EMC–CaV1.2(ΔC)–CaVβ3 complex is reported as ~0.6 MDa and solved at 3.4 Å and 3.3 Å overall. (chen2023emcchaperone–cavstructure pages 3-4, chen2023emcchaperone–cavstructure pages 1-3)

EMC4 is part of EMC’s client-engaging architecture in this system:
* The cytoplasmic chaperone module that engages CaV includes EMC2, EMC3, EMC4, EMC5 and EMC8. (chen2023emcchaperone–cavstructure pages 3-4)
* A lumenal subassembly comprising EMC1/EMC4/EMC7/EMC10 is implicated in supporting a transmembrane docking region during channel assembly. (chen2023emcchaperone–cavstructure pages 11-13)

3.3 2024: EMC4 and ER–mitochondria contact-site biology (VDAC interaction)

Li et al. (Aging, 2024-03) report cryo-EM structures of human EMC and a VDAC-bound state, suggesting EMC can engage VDAC proteins at mitochondria–ER contact sites and that a “gating plug” inside the vestibule changes conformation between apo and VDAC-bound conditions. In that analysis, EMC4 forms part of the ordered three-TMH bundle shaping the vestibule sidewall. (li2024structuralinsightsinto pages 1-3)

3.4 2024: Lipid scrambling hypothesis—Emc4 implicated among insertases

Li et al. (PNAS, 2024-04) propose that lipid scrambling is a general feature of protein insertases, and report coarse-grained MD evidence localizing EMC scrambling activity specifically to Emc3 and Emc4. They tested >150 proteins/complexes in silico and quantified lipid scrambling with an angular criterion (>125° for upper-leaflet lipids; <55° for lower-leaflet lipids). (li2024lipidscramblingis pages 3-5, li2024lipidscramblingis pages 7-8)

While this is not yet a definitive demonstration of human EMC4 scramblase activity in cells, it is a mechanistically coherent proposal because the same hydrophilic pathway used for protein insertion could allow lipid flip-flop. (li2024lipidscramblingis pages 3-5)

4) Biological processes, pathways, and client/substrate classes (functional annotation)

4.1 Primary function (best-supported)

The best-supported “primary” function for EMC4 is as a structural and mechanistic subunit of the EMC insertase/chaperone machinery that promotes membrane protein biogenesis in the ER by:
* shaping/enclosing the hydrophilic vestibule used for insertion, and
* participating in client engagement surfaces (crosslinking evidence), and
* enabling downstream folding/assembly steps for complex multipass clients (e.g., CaV channels). (pleiner2023aselectivityfilter pages 4-6, pleiner2023aselectivityfilter pages 2-4, chen2023emcchaperone–cavstructure pages 3-4)

EMC4 is not an enzyme with a known catalytic reaction; rather, it is a membrane biogenesis factor contributing to a proteinaceous insertion/chaperone environment.

4.2 Substrate/client examples and classes

Across the retrieved sources, EMC clients include:
* Tail-anchored proteins with weakly hydrophobic TMDs, including SQS/FDFT1 (a canonical EMC-dependent TA in multiple studies). (pleiner2020structuralbasisfor pages 7-11, pleiner2023aselectivityfilter pages 19-23)
* Multipass membrane proteins, enriched for transporters in proteomic datasets, and including ion channels. (shurtleff2018theermembrane pages 8-10, chen2023emcchaperone–cavstructure pages 3-4)
* Voltage-gated calcium channels: EMC binds an assembly intermediate and supports maturation/functional expression. (chen2023emcchaperone–cavstructure pages 3-4)

Quantitative proteomics in mammalian cells reported 11 proteins decreased ≥2-fold upon both EMC2 and EMC4 depletion (10/11 with at least one TMD), consistent with an effect on a subset of membrane proteins rather than global translation changes. (shurtleff2018theermembrane pages 8-10)

5) Real-world applications and implementations

5.1 Antiviral biology: EMC4 as a host dependency factor

Multiple viruses exploit ER biogenesis machinery. EMC4 is experimentally validated as a proviral host factor for several viruses:

Flaviviruses (dengue, yellow fever, Zika)
* EMC4 knockout/targeting reduces infectivity and virus production, with effects reported as ~5–20-fold reductions in infectivity (YFV imaging assays) and up to 3 log10 reduced extracellular YFV titers at 33.5 h post infection; for DENV2/DENV4, virus output fell below detection in EMC4 KO lines in the described assays. (barrows2019dualrolesfor pages 3-5)
* EMC4 depletion in a ZIKV replicon context reduced replicon RNA by ~54–55% and EMC4 protein levels by 73% or 94% (two siRNAs), with downstream reductions in multiple viral proteins. (barrows2019dualrolesfor pages 9-10)
* Biochemically, EMC4 is used for co-immunoprecipitation assays in which EMC associates with flavivirus non-structural multipass proteins such as NS4B, consistent with a direct role in viral membrane-protein biogenesis. (lin2019theermembrane pages 13-14)

Polyomavirus SV40 entry
EMC4 and EMC7 promote late endosome-to-ER targeting of SV40 during entry. EMC4 engages Rab7 (late endosome) and syntaxin18 (ER fusion machinery) and is proposed to act as a tether stabilizing LE–ER contacts that facilitate viral transport; EMC4-FLAG rescue experiments support specificity. (bagchi2020selectiveemcsubunits pages 1-2)

These findings create a plausible translational direction—targeting host insertion/trafficking dependencies—although the retrieved evidence does not yet provide a clinically validated EMC4-specific inhibitor or trial.

5.2 Membrane-protein proteostasis engineering

Structural mechanistic definition of EMC (including EMC4’s vestibule enclosure and CaV chaperone role) informs biotechnological strategies aimed at improving expression/assembly of difficult multipass proteins (e.g., channels and GPCRs) in cell systems by modulating EMC function. (pleiner2023aselectivityfilter pages 4-6, chen2023emcchaperone–cavstructure pages 3-4)

6) Expert opinions / authoritative synthesis

A recurring expert view is that EMC is built around a deeply conserved insertase core and has additional roles in folding/assembly that extend beyond insertion alone. Structural and mechanistic studies emphasize that distinct EMC regions contribute to different client classes (tail-anchored vs multipass), consistent with EMC being a multifunctional membrane biogenesis machine. (millervedam2020structuralandmechanistic pages 7-10, pleiner2020structuralbasisfor pages 7-11, millervedam2020structuralandmechanistic pages 18-21)

In this context, EMC4 is best interpreted as a “peripheral-but-mechanistically-relevant” subunit: depletion of EMC4 may leave other EMC subunits largely stable (suggesting it is not the sole assembly scaffold), yet it is required for specific biogenesis functions and contributes to the vestibule/client interface. (shurtleff2018theermembrane pages 8-10, pleiner2023aselectivityfilter pages 4-6)

7) Disease associations and human genetics (current evidence limits)

Direct, well-established monogenic human diseases caused by EMC4 variants were not identified in the retrieved full-text evidence. However, aggregated evidence in Open Targets links EMC4 to multiple disease categories (including neurodegenerative diseases and dengue disease) with modest scores and evidence size = 5 for each shown association; this should be interpreted as hypothesis-generating and often driven by functional genomics screens rather than causal human genetics. (OpenTargets Search: -EMC4)

8) Visual evidence supporting EMC4’s structural role

The following retrieved figure crops from Pleiner et al. (J Cell Biol, 2023) visually support the claim that EMC4’s 3 TMDs enclose the EMC3/6 insertase core hydrophilic vestibule and that EMC10 contributes additional enclosure density. (pleiner2023aselectivityfilter media 2fbee94e, pleiner2023aselectivityfilter media bf0f9cf4, pleiner2023aselectivityfilter media ac5195ae)

Evidence map (compact summary)

Table: This table summarizes the main experimentally supported roles of human EMC4 within the ER membrane protein complex, including structure, mechanism, client classes, and disease-relevant phenotypes. It is useful as a compact evidence map linking EMC4-specific findings to broader EMC biology.

Key source list (URLs; publication dates)

• Pleiner T. et al. A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER. J Cell Biol (published 2023-05). https://doi.org/10.1083/jcb.202212007 (pleiner2023aselectivityfilter pages 4-6, pleiner2023aselectivityfilter pages 2-4, pleiner2023aselectivityfilter pages 6-8)
• Chen Z. et al. EMC chaperone–CaV structure reveals an ion channel assembly intermediate. Nature 619 (published 2023-05). https://doi.org/10.1038/s41586-023-06175-5 (chen2023emcchaperone–cavstructure pages 3-4, chen2023emcchaperone–cavstructure pages 1-3)
• Li M. et al. Structural insights into human EMC and its interaction with VDAC. Aging (Albany NY) (published 2024-03). https://doi.org/10.18632/aging.205660 (li2024structuralinsightsinto pages 1-3)
• Li D. et al. Lipid scrambling is a general feature of protein insertases. PNAS (published 2024-04). https://doi.org/10.1073/pnas.2319476121 (li2024lipidscramblingis pages 3-5, li2024lipidscramblingis pages 7-8)
• Pleiner T. et al. Structural basis for membrane insertion by the human ER membrane protein complex. Science (published 2020-07). https://doi.org/10.1126/science.abb5008 (pleiner2020structuralbasisfor pages 1-3)
• O’Donnell J.P. et al. The architecture of EMC reveals a path for membrane protein insertion. eLife (published 2020-05). https://doi.org/10.7554/elife.57887 (odonnell2020thearchitectureof pages 1-2)
• Barrows N.J. et al. Dual roles for the ER membrane protein complex in flavivirus infection: viral entry and protein biogenesis. Sci Rep (published 2019-07). https://doi.org/10.1038/s41598-019-45910-9 (barrows2019dualrolesfor pages 3-5, barrows2019dualrolesfor pages 9-10)
• Bagchi P. et al. Selective EMC subunits act as molecular tethers of intracellular organelles exploited during viral entry. Nat Commun (published 2020-02). https://doi.org/10.1038/s41467-020-14967-w (bagchi2020selectiveemcsubunits pages 1-2)

References

1. (OpenTargets Search: -EMC4): Open Targets Query (-EMC4, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

2. (pleiner2020structuralbasisfor pages 7-11): Tino Pleiner, Giovani Pinton Tomaleri, Kurt Januszyk, Alison J. Inglis, Masami Hazu, and Rebecca M. Voorhees. Structural basis for membrane insertion by the human er membrane protein complex. Jul 2020. URL: https://doi.org/10.1126/science.abb5008, doi:10.1126/science.abb5008. This article has 192 citations and is from a highest quality peer-reviewed journal.

3. (pleiner2020structuralbasisfor pages 1-3): Tino Pleiner, Giovani Pinton Tomaleri, Kurt Januszyk, Alison J. Inglis, Masami Hazu, and Rebecca M. Voorhees. Structural basis for membrane insertion by the human er membrane protein complex. Jul 2020. URL: https://doi.org/10.1126/science.abb5008, doi:10.1126/science.abb5008. This article has 192 citations and is from a highest quality peer-reviewed journal.

4. (odonnell2020thearchitectureof pages 1-2): John P O'Donnell, Ben P Phillips, Yuichi Yagita, Szymon Juszkiewicz, Armin Wagner, Duccio Malinverni, Robert J Keenan, Elizabeth A Miller, and Ramanujan S Hegde. The architecture of emc reveals a path for membrane protein insertion. May 2020. URL: https://doi.org/10.7554/elife.57887, doi:10.7554/elife.57887. This article has 121 citations and is from a domain leading peer-reviewed journal.

5. (odonnell2020thearchitectureof pages 2-4): John P O'Donnell, Ben P Phillips, Yuichi Yagita, Szymon Juszkiewicz, Armin Wagner, Duccio Malinverni, Robert J Keenan, Elizabeth A Miller, and Ramanujan S Hegde. The architecture of emc reveals a path for membrane protein insertion. May 2020. URL: https://doi.org/10.7554/elife.57887, doi:10.7554/elife.57887. This article has 121 citations and is from a domain leading peer-reviewed journal.

6. (pleiner2023aselectivityfilter pages 4-6): Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Vy N. Nguyen, Kurt Januszyk, and Rebecca M. Voorhees. A selectivity filter in the er membrane protein complex limits protein misinsertion at the er. The Journal of Cell Biology, May 2023. URL: https://doi.org/10.1083/jcb.202212007, doi:10.1083/jcb.202212007. This article has 28 citations.

7. (pleiner2023aselectivityfilter pages 2-4): Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Vy N. Nguyen, Kurt Januszyk, and Rebecca M. Voorhees. A selectivity filter in the er membrane protein complex limits protein misinsertion at the er. The Journal of Cell Biology, May 2023. URL: https://doi.org/10.1083/jcb.202212007, doi:10.1083/jcb.202212007. This article has 28 citations.

8. (pleiner2023aselectivityfilter pages 19-23): Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Vy N. Nguyen, Kurt Januszyk, and Rebecca M. Voorhees. A selectivity filter in the er membrane protein complex limits protein misinsertion at the er. The Journal of Cell Biology, May 2023. URL: https://doi.org/10.1083/jcb.202212007, doi:10.1083/jcb.202212007. This article has 28 citations.

9. (li2024structuralinsightsinto pages 1-3): Mingyue Li, Chunli Zhang, Yuntao Xu, Shaobai Li, Chenhui Huang, Jian Wu, and Ming Lei. Structural insights into human emc and its interaction with vdac. Aging (Albany NY), 16:5501-5525, Mar 2024. URL: https://doi.org/10.18632/aging.205660, doi:10.18632/aging.205660. This article has 6 citations.

10. (pleiner2023aselectivityfilter pages 23-26): Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Vy N. Nguyen, Kurt Januszyk, and Rebecca M. Voorhees. A selectivity filter in the er membrane protein complex limits protein misinsertion at the er. The Journal of Cell Biology, May 2023. URL: https://doi.org/10.1083/jcb.202212007, doi:10.1083/jcb.202212007. This article has 28 citations.

11. (pleiner2023aselectivityfilter pages 6-8): Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Vy N. Nguyen, Kurt Januszyk, and Rebecca M. Voorhees. A selectivity filter in the er membrane protein complex limits protein misinsertion at the er. The Journal of Cell Biology, May 2023. URL: https://doi.org/10.1083/jcb.202212007, doi:10.1083/jcb.202212007. This article has 28 citations.

12. (pleiner2023aselectivityfilter pages 8-10): Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Vy N. Nguyen, Kurt Januszyk, and Rebecca M. Voorhees. A selectivity filter in the er membrane protein complex limits protein misinsertion at the er. The Journal of Cell Biology, May 2023. URL: https://doi.org/10.1083/jcb.202212007, doi:10.1083/jcb.202212007. This article has 28 citations.

13. (chen2023emcchaperone–cavstructure pages 3-4): Zhou Chen, Abhisek Mondal, Fayal Abderemane-Ali, Seil Jang, Sangeeta Niranjan, José L. Montaño, Balyn W. Zaro, and Daniel L. Minor. Emc chaperone–cav structure reveals an ion channel assembly intermediate. Nature, 619:410-419, May 2023. URL: https://doi.org/10.1038/s41586-023-06175-5, doi:10.1038/s41586-023-06175-5. This article has 77 citations and is from a highest quality peer-reviewed journal.

14. (chen2023emcchaperone–cavstructure pages 1-3): Zhou Chen, Abhisek Mondal, Fayal Abderemane-Ali, Seil Jang, Sangeeta Niranjan, José L. Montaño, Balyn W. Zaro, and Daniel L. Minor. Emc chaperone–cav structure reveals an ion channel assembly intermediate. Nature, 619:410-419, May 2023. URL: https://doi.org/10.1038/s41586-023-06175-5, doi:10.1038/s41586-023-06175-5. This article has 77 citations and is from a highest quality peer-reviewed journal.

15. (chen2023emcchaperone–cavstructure pages 11-13): Zhou Chen, Abhisek Mondal, Fayal Abderemane-Ali, Seil Jang, Sangeeta Niranjan, José L. Montaño, Balyn W. Zaro, and Daniel L. Minor. Emc chaperone–cav structure reveals an ion channel assembly intermediate. Nature, 619:410-419, May 2023. URL: https://doi.org/10.1038/s41586-023-06175-5, doi:10.1038/s41586-023-06175-5. This article has 77 citations and is from a highest quality peer-reviewed journal.

16. (li2024lipidscramblingis pages 3-5): Dazhi Li, Cristian Rocha-Roa, Matthew A. Schilling, Karin M. Reinisch, and Stefano Vanni. Lipid scrambling is a general feature of protein insertases. Proceedings of the National Academy of Sciences of the United States of America, Apr 2024. URL: https://doi.org/10.1073/pnas.2319476121, doi:10.1073/pnas.2319476121. This article has 70 citations and is from a highest quality peer-reviewed journal.

17. (li2024lipidscramblingis pages 7-8): Dazhi Li, Cristian Rocha-Roa, Matthew A. Schilling, Karin M. Reinisch, and Stefano Vanni. Lipid scrambling is a general feature of protein insertases. Proceedings of the National Academy of Sciences of the United States of America, Apr 2024. URL: https://doi.org/10.1073/pnas.2319476121, doi:10.1073/pnas.2319476121. This article has 70 citations and is from a highest quality peer-reviewed journal.

18. (shurtleff2018theermembrane pages 8-10): Matthew J Shurtleff, Daniel N Itzhak, Jeffrey A Hussmann, Nicole T Schirle Oakdale, Elizabeth A Costa, Martin Jonikas, Jimena Weibezahn, Katerina D Popova, Calvin H Jan, Pavel Sinitcyn, Shruthi S Vembar, Hilda Hernandez, Jürgen Cox, Alma L Burlingame, Jeffrey L Brodsky, Adam Frost, Georg HH Borner, and Jonathan S Weissman. The er membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins. eLife, May 2018. URL: https://doi.org/10.7554/elife.37018, doi:10.7554/elife.37018. This article has 257 citations and is from a domain leading peer-reviewed journal.

19. (barrows2019dualrolesfor pages 3-5): Nicholas J. Barrows, Yesseinia Anglero-Rodriguez, Byungil Kim, Sharon F. Jamison, Caroline Le Sommer, Charles E. McGee, James L. Pearson, George Dimopoulos, Manuel Ascano, Shelton S. Bradrick, and Mariano A. Garcia-Blanco. Dual roles for the er membrane protein complex in flavivirus infection: viral entry and protein biogenesis. Scientific Reports, Jul 2019. URL: https://doi.org/10.1038/s41598-019-45910-9, doi:10.1038/s41598-019-45910-9. This article has 62 citations and is from a peer-reviewed journal.

20. (barrows2019dualrolesfor pages 9-10): Nicholas J. Barrows, Yesseinia Anglero-Rodriguez, Byungil Kim, Sharon F. Jamison, Caroline Le Sommer, Charles E. McGee, James L. Pearson, George Dimopoulos, Manuel Ascano, Shelton S. Bradrick, and Mariano A. Garcia-Blanco. Dual roles for the er membrane protein complex in flavivirus infection: viral entry and protein biogenesis. Scientific Reports, Jul 2019. URL: https://doi.org/10.1038/s41598-019-45910-9, doi:10.1038/s41598-019-45910-9. This article has 62 citations and is from a peer-reviewed journal.

21. (lin2019theermembrane pages 13-14): David L. Lin, Takamasa Inoue, Yu-Jie Chen, Aaron Chang, Billy Tsai, and Andrew W. Tai. The er membrane protein complex promotes biogenesis of dengue and zika virus non-structural multi-pass transmembrane proteins to support infection. Cell reports, 27:1666-1674.e4, May 2019. URL: https://doi.org/10.1016/j.celrep.2019.04.051, doi:10.1016/j.celrep.2019.04.051. This article has 115 citations and is from a highest quality peer-reviewed journal.

22. (bagchi2020selectiveemcsubunits pages 1-2): Parikshit Bagchi, Mauricio Torres, Ling Qi, and Billy Tsai. Selective emc subunits act as molecular tethers of intracellular organelles exploited during viral entry. Nature Communications, Feb 2020. URL: https://doi.org/10.1038/s41467-020-14967-w, doi:10.1038/s41467-020-14967-w. This article has 31 citations and is from a highest quality peer-reviewed journal.

23. (millervedam2020structuralandmechanistic pages 7-10): Lakshmi E. Miller-Vedam, Bastian Bräuning, Katerina D. Popova, Nicole T. Schirle Oakdale, Jessica L. Bonnar, Jesuraj Rajan Prabu, Elizabeth A. Boydston, Natalia Sevillano, Matthew J. Shurtleff, Robert M. Stroud, Charles S. Craik, Brenda A. Schulman, Adam Frost, and Jonathan S. Weissman. Structural and mechanistic basis of the emc-dependent biogenesis of distinct transmembrane clients. eLife, Sep 2020. URL: https://doi.org/10.1101/2020.09.02.280008, doi:10.1101/2020.09.02.280008. This article has 102 citations and is from a domain leading peer-reviewed journal.

24. (millervedam2020structuralandmechanistic pages 18-21): Lakshmi E. Miller-Vedam, Bastian Bräuning, Katerina D. Popova, Nicole T. Schirle Oakdale, Jessica L. Bonnar, Jesuraj Rajan Prabu, Elizabeth A. Boydston, Natalia Sevillano, Matthew J. Shurtleff, Robert M. Stroud, Charles S. Craik, Brenda A. Schulman, Adam Frost, and Jonathan S. Weissman. Structural and mechanistic basis of the emc-dependent biogenesis of distinct transmembrane clients. eLife, Sep 2020. URL: https://doi.org/10.1101/2020.09.02.280008, doi:10.1101/2020.09.02.280008. This article has 102 citations and is from a domain leading peer-reviewed journal.

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Artifacts

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