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## Question

# Gene Research for Functional Annotation

## ⚠️ CRITICAL: Gene/Protein Identification Context

**BEFORE YOU BEGIN RESEARCH:** You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

### Target Gene/Protein Identity (from UniProt):
- **UniProt Accession:** P43307
- **Protein Description:** RecName: Full=Translocon-associated protein subunit alpha; Short=TRAP-alpha; AltName: Full=Signal sequence receptor subunit alpha; Short=SSR-alpha; Flags: Precursor;
- **Gene Information:** Name=SSR1; Synonyms=TRAPA; ORFNames=PSEC0262;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the TRAP-alpha family. .
- **Key Domains:** TRAP_alpha. (IPR005595); TRAP_alpha (PF03896)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "SSR1" matches the protein description above**
2. **Verify the organism is correct:** Homo sapiens (Human).
3. **Check if protein family/domains align with what you find in literature**
4. **If you find literature for a DIFFERENT gene with the same or similar symbol, STOP**

### If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

**DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE.** Instead:
- State clearly: "The gene symbol 'SSR1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

### Research Target:

Please provide a comprehensive research report on the gene **SSR1** (gene ID: SSR1, UniProt: P43307) in human.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

## Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

# Gene Research for Functional Annotation

## ⚠️ CRITICAL: Gene/Protein Identification Context

**BEFORE YOU BEGIN RESEARCH:** You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

### Target Gene/Protein Identity (from UniProt):
- **UniProt Accession:** P43307
- **Protein Description:** RecName: Full=Translocon-associated protein subunit alpha; Short=TRAP-alpha; AltName: Full=Signal sequence receptor subunit alpha; Short=SSR-alpha; Flags: Precursor;
- **Gene Information:** Name=SSR1; Synonyms=TRAPA; ORFNames=PSEC0262;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the TRAP-alpha family. .
- **Key Domains:** TRAP_alpha. (IPR005595); TRAP_alpha (PF03896)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "SSR1" matches the protein description above**
2. **Verify the organism is correct:** Homo sapiens (Human).
3. **Check if protein family/domains align with what you find in literature**
4. **If you find literature for a DIFFERENT gene with the same or similar symbol, STOP**

### If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

**DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE.** Instead:
- State clearly: "The gene symbol 'SSR1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

### Research Target:

Please provide a comprehensive research report on the gene **SSR1** (gene ID: SSR1, UniProt: P43307) in human.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan and verification
- Identity and nomenclature: The human SSR1 gene encodes TRAP-α (also called signal sequence receptor subunit α), a subunit of the heterotetrameric translocon-associated protein (TRAP) complex composed of SSR1–SSR4 (TRAP-α, -β, -γ, -δ) that binds the Sec61 translocon on the endoplasmic reticulum (ER) membrane (Pauwels et al., Science Advances, 3 Mar 2023, https://doi.org/10.1126/sciadv.adf0797) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3). The articles cited below use mammalian, including human, ribosome–Sec61–TRAP assemblies and explicitly identify the TRAP subunits by the SSR1–SSR4 nomenclature, satisfying organism and symbol verification (Pauwels 2023; Karki et al., EMBO Reports, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3, karki2023molecularviewof pages 1-2).
- Family/domains: Recent structures and reviews align with UniProt’s TRAP-α family assignment and domain features: a large luminal glycoprotein domain and a single long transmembrane helix for TRAP-α, as detailed below (Karki 2023; Russo 2020) (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 1-2, russo2020understandingthemammalian pages 5-6).

Key concepts and definitions
- What is TRAP-α/SSR1? TRAP-α is the α subunit of the ER-resident TRAP complex that stably associates with the Sec61 protein-conducting channel and the ribosome, assisting co‑translational translocation of secretory and membrane proteins, especially those with weak or atypical signal peptides (Pauwels 2023; Russo 2020) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3, russo2020understandingthemammalian pages 5-6).
- Structure and domains: Cryo‑EM/ET reveals that TRAP-α contains a prominent luminal domain positioned directly beneath the Sec61α channel exit and a long, diagonal transmembrane helix that contacts Sec61 at the hinge/backside region; its luminal domain bears N‑glycosylation sites (e.g., Asn136, Asn191) and is poised for nascent chain interactions (Karki 2023, EMBO Reports, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5). In the assembled TRAP, a seven-helix membrane bundle forms from TRAP-γ’s four helices plus one C‑terminal helix each from TRAP-α/β/δ, positioning the luminal TRAP-α/β/δ “crescent” adjacent to Sec61 (Pauwels 2023, 3 Mar 2023, https://doi.org/10.1126/sciadv.adf0797) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3).
- Localization and topology: TRAP-α is an ER membrane single-pass type I membrane glycoprotein with a large luminal N‑terminal domain and a short cytosolic C‑terminus; its luminal mass sits under the Sec61 pore, while the C‑terminal cytosolic tail localizes near ribosomal proteins (Karki 2023) (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 1-2).

Molecular function and pathways
- Co‑translational translocation: TRAP-α, within the TRAP complex, stabilizes the ribosome–Sec61 assembly and facilitates insertion/translocation of nascent polypeptides, particularly those with below‑average hydrophobicity or Gly/Pro‑rich signal peptides that would otherwise inefficiently open Sec61’s lateral gate (Pauwels 2023; Gemmer et al., Life Science Alliance, 12 Jun 2024, https://doi.org/10.26508/lsa.202302496) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3, gemmer2024exploringthemolecular pages 1-3). Karki 2023 further demonstrates in atomistic MD and cellular assays that TRAP strengthens ribosome anchoring and supports preproinsulin translocation, with TRAP-α perturbation impairing this pathway (Karki 2023, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5).
- Substrate specificity: Multiple recent studies converge that TRAP dependency correlates with weakly hydrophobic and Gly/Pro‑rich signal peptides; TRAP-α’s luminal proximity to the exit likely helps “ratchet” such sequences into the ER and prevent back‑sliding (Pauwels 2023; Gemmer 2024; Russo 2020) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3, gemmer2024exploringthemolecular pages 1-3, russo2020understandingthemammalian pages 5-6).
- Coordination with N‑glycosylation: TRAP’s luminal surface lies adjacent to the oligosaccharyltransferase (OST) active site; structures and modeling support a role for TRAP-α in positioning nascent chains for initial N‑linked glycosylation during co‑translational translocation (Pauwels 2023; Karki 2023) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3, karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 1-2). This spatial coupling explains why defects in TRAP subunits can present with glycosylation abnormalities (Karki 2023) (karki2023molecularviewof pages 1-2).
- ER membrane remodeling: Cryo‑EM/MD indicates that Sec61/TRAP locally thins and curves the ER luminal leaflet, reduces local lipid order, and increases lipid flip‑flops; this remodeling likely tunes lateral‑gate dynamics to promote engagement of challenging signal sequences (Karki 2023, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5).
- ERQC/UPR connections: TRAP abundance and association with the ribosome–Sec61 assembly vary with translational state and ER stress, situating TRAP-α within ER quality control networks that influence substrate selection and processing; reviews emphasize TRAP integration with ERAD/UPR pathways (Gemmer 2024; Russo 2020) (gemmer2024exploringthemolecular pages 1-3, russo2020understandingthemammalian pages 5-6).

Recent developments (2023–2024)
- High-resolution architectures: Two 2023 cryo‑EM studies established the ribosome–Sec61–TRAP organization and details of TRAP-α placement and interfaces, including a seven‑TMH bundle incorporating the α/β/δ C‑terminal helices around TRAP-γ (Pauwels 2023, Science Advances, 3 Mar 2023, https://doi.org/10.1126/sciadv.adf0797) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3). Karki 2023 provided a ribosome‑bound Sec61/TRAP reconstruction with MD that explains how TRAP reshapes the ER membrane to aid translocation and highlighted TRAP-α’s role in preproinsulin biogenesis (EMBO Reports, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5).
- Native-membrane context: Cryo‑ET/subtomogram averaging in 2024 showed TRAP’s substoichiometric association with multipass translocons and higher abundance on non‑translating ribosome–MPTs; luminal TRAP contacts bridge to back‑of‑Sec61 factors, supporting a modular assembly that adapts to translational state (Gemmer 2024, 12 Jun 2024, https://doi.org/10.26508/lsa.202302496) (gemmer2024exploringthemolecular pages 1-3).
- Mechanistic implications: Together, these studies substantiate that TRAP-α’s luminal domain is spatially poised to influence nascent chain handling and N‑glycosylation, while its TM helix and complex interfaces modulate Sec61 conformation and the local membrane to expand the repertoire of efficiently translocated substrates (Pauwels 2023; Karki 2023) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3, karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5).

Current applications and real-world implementations
- Translocon inhibitors: Pauwels 2023 identified the cyclotriazadisulfonamide derivative CK147 as a Sec61 inhibitor that binds near the lumenal plug; resistance mutations cluster around the lateral gate/plug. This provides a structural foothold for rational design of translocon inhibitors with potential antiviral or anticancer applications (Science Advances, 3 Mar 2023, https://doi.org/10.1126/sciadv.adf0797) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3).
- Host dependency in viral infection: Genetic and mechanistic studies indicate that ER translocon modules (including TRAP subunits SSR1–SSR4) are host factors for flaviviruses; comprehensive CRISPR screens and recent reviews highlight reliance on the mammalian translocon for dengue/Zika replication and ER processes (Marceau et al., Nature, 22 Jun 2016, https://doi.org/10.1038/nature18631; Verhaegen & Vermeire, npj Viruses, 6 Jun 2024, https://doi.org/10.1038/s44298-024-00031-7) (, ). These insights motivate host-directed antiviral strategies targeting translocon/OST modules.
- Endocrine relevance: Building on 2021–2023 evidence that SSR1/TRAP‑α affects insulin biogenesis, recent mechanistic work indicates that TRAP-α supports preproinsulin translocation and early folding steps, linking TRAP function to glycemic control; this provides a conceptual framework for potential biomarkers/interventions in metabolic disease (Karki 2023, EMBO Reports, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2).

Expert perspectives and authoritative syntheses
- A focused review (Russo 2020) consolidates the view of TRAP (including TRAP‑α/SSR1) as a substrate‑selective facilitator in co‑translational translocation, located to couple with OST and influence ERQC/UPR, anticipating the detailed structural confirmations published in 2023–2024 (Open Biology, 20 May 2020, https://doi.org/10.1098/rsob.190244) (russo2020understandingthemammalian pages 5-6).
- A 2024 native-membrane structural analysis (Gemmer 2024) argues for dynamic association of TRAP with multipass translocons and variable stoichiometry depending on translation state, shaping current models of how accessory factors tune ER translocation in situ (Life Science Alliance, 12 Jun 2024, https://doi.org/10.26508/lsa.202302496) (gemmer2024exploringthemolecular pages 1-3).
- A 2024 virology review (Verhaegen & Vermeire) frames TRAP within the ER hub exploited across the flavivirus lifecycle and discusses ER‑targeting antiviral strategies, underscoring translational relevance (npj Viruses, 6 Jun 2024, https://doi.org/10.1038/s44298-024-00031-7) ().

Relevant statistics and data
- Structural resolutions and architecture: Pauwels 2023 resolved ribosome–Sec61–TRAP architecture and a seven‑helix TM bundle positioning luminal TRAP-α/β/δ; CK147 binding site mapped at the Sec61 plug/lateral gate region (Science Advances, 3 Mar 2023, https://doi.org/10.1126/sciadv.adf0797) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3). Karki 2023 provided a high‑resolution ribosome‑bound Sec61/TRAP map and multi‑microsecond MD showing local ER membrane thinning/curvature and lipid disorder increases near TRAP (EMBO Reports, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5).
- Translational-state dependence: Cryo‑ET indicates TRAP is substoichiometric within multipass translocons and most abundant in complexes with non‑translating ribosomes, implying regulated engagement with MPTs (Gemmer 2024, 12 Jun 2024, https://doi.org/10.26508/lsa.202302496) (gemmer2024exploringthemolecular pages 1-3).
- Substrate class: Across studies, TRAP dependence associates with signal peptides of lower hydrophobicity and higher Gly/Pro content, consistent with a role in enabling otherwise inefficient Sec61 gating and nascent chain handling (Pauwels 2023; Gemmer 2024; Russo 2020) (pauwels2023structuralinsightsinto pages 1-2, gemmer2024exploringthemolecular pages 1-3, russo2020understandingthemammalian pages 5-6).

Human disease links
- Congenital disorders of glycosylation (CDG): Germline mutations in TRAP subunits produce glycosylation phenotypes, mechanistically consistent with TRAP’s spatial coupling to OST and role in early translocation (Karki 2023, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 1-2).
- Infection biology: TRAP components are host dependency factors for dengue/Zika and related flaviviruses, with genetic screens and reviews implicating mammalian translocon function in viral RNA replication complexes (Marceau 2016, 22 Jun 2016, https://doi.org/10.1038/nature18631; Verhaegen 2024, 6 Jun 2024, https://doi.org/10.1038/s44298-024-00031-7) (, ).
- Endocrine/metabolic disease: TRAP‑α supports preproinsulin translocation; perturbation compromises insulin biogenesis and can contribute to ER stress in β cells, suggesting mechanistic ties to dysglycemia (Karki 2023, EMBO Reports, 20 Nov 2023, https://doi.org/10.15252/embr.202357910) (karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2).

Concise mechanistic model
- Topology: TRAP-α is a single-pass ER glycoprotein with a luminal N‑terminal domain and a diagonal TM helix packing against Sec61 (Karki 2023) (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 3-5).
- Assembly: In the ribosome–Sec61–TRAP supercomplex, TRAP-γ anchors to rRNA and rpL38 and packs with α/β/δ helices; TRAP‑α/β/δ luminal domains form a crescent under Sec61’s luminal exit (Pauwels 2023) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3).
- Function: TRAP-α helps stabilize the ribosome exit tunnel and modulates Sec61 gating within a locally remodeled ER membrane, enabling efficient co‑translational translocation and coupling to OST for N‑glycosylation—particularly benefitting substrates with weak/atypical signal peptides (Karki 2023; Pauwels 2023; Gemmer 2024) (karki2023molecularviewof pages 5-7, pauwels2023structuralinsightsinto pages 1-2, gemmer2024exploringthemolecular pages 1-3).

Embedded key sources (with URLs and dates)
| Year | Citation (first author et al., journal) | Topic focus | Key finding(s) relevant to SSR1/TRAP-α (citation) | URL | Publication date (month/year) |
|------:|----------------------------------------|-------------|--------------------------------------------------|-----|----------------------------|
| 2023 | Pauwels et al., Science Advances | Cryo-EM of ribosome–Sec61–TRAP; translocon inhibition | Defines heterotetrameric TRAP architecture; positions TRAP-α (SSR1) lumenal trimer adjacent to Sec61 exit and a TM helix contacting Sec61; identifies CK147 binding site on Sec61 (translocon inhibitor) (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3) | https://doi.org/10.1126/sciadv.adf0797 | Mar/2023 |
| 2023 | Karki et al., EMBO Reports | Cryo-EM/MD of Sec61/TRAP; membrane remodeling; preproinsulin dependence | Atomic/modeling view of Sec61–TRAP–ribosome showing TRAP-α lumenal domain below Sec61 exit, ribosome anchoring, and TRAP-driven local ER membrane thinning/curvature that facilitates insertion of weak signal peptides; TRAP-α required for efficient preproinsulin translocation (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 5-7) | https://doi.org/10.15252/embr.202357910 | Nov/2023 |
| 2024 | Gemmer et al., Life Science Alliance | Cryo-ET of multipass translocon in native ER membranes | Subtomogram averages reveal compositional variability of multipass translocon; TRAP associates substoichiometrically and is enriched in non-translating ribosome-bound MPTs; luminal TRAP contacts a back-of-Sec61 subunit, supporting TRAP-α role in SP handling and coordination with OST (gemmer2024exploringthemolecular pages 1-3) | https://doi.org/10.26508/lsa.202302496 | Jun/2024 |
| 2020 | Russo et al., Open Biology (review) | Review of mammalian TRAP functions; ERQC/UPR links | Synthesizes functional evidence that TRAP (including SSR1/TRAP‑α) is a substrate‑selective co‑translational facilitator for weak/hydrophilic signal peptides, influences topology/insertion, and is positioned to coordinate with OST and ER‑quality control (russo2020understandingthemammalian pages 5-6) | https://doi.org/10.1098/rsob.190244 | May/2020 |
| 2017 | Pfeffer et al., Nature Communications | Molecular organization of the TRAP complex | Assigned positions of TRAP subunits within native translocon structures; established TRAP as integral Sec61 accessory that helps regulate signal peptide insertion and topology (see Pfeffer et al.; foundational architecture referenced in later cryo-EM work) (russo2020understandingthemammalian pages 5-6) | https://doi.org/10.1038/ncomms14516 | Feb/2017 |


*Table: Concise table of authoritative recent and foundational publications describing SSR1 (TRAP‑α) structure and function, with URLs, dates, and context‑ID citations for the evidence used.*

Notes on symbol ambiguity
- The symbol SSR1 is used in oncology literature for unrelated targets; here, all cited structural and mechanistic works explicitly define SSR1 as TRAP‑α/signal sequence receptor subunit α in Homo sapiens and place it in the TRAP complex with SSR2–SSR4, consistent with UniProt P43307 (Pauwels 2023; Karki 2023) (pauwels2023structuralinsightsinto pages 1-2, karki2023molecularviewof pages 1-2).

References (with direct links and publication dates)
- Pauwels E. et al. Structural insights into TRAP association with ribosome–Sec61 complex and translocon inhibition by a CADA derivative. Science Advances. 3 Mar 2023. https://doi.org/10.1126/sciadv.adf0797 (pauwels2023structuralinsightsinto pages 1-2, pauwels2023structuralinsightsinto pages 2-3).
- Karki S. et al. Molecular view of ER membrane remodeling by the Sec61/TRAP translocon. EMBO Reports. 20 Nov 2023. https://doi.org/10.15252/embr.202357910 (karki2023molecularviewof pages 2-3, karki2023molecularviewof pages 5-7, karki2023molecularviewof pages 1-2, karki2023molecularviewof pages 3-5).
- Gemmer M. et al. Exploring the molecular composition of the multipass translocon in its native membrane environment. Life Science Alliance. 12 Jun 2024. https://doi.org/10.26508/lsa.202302496 (gemmer2024exploringthemolecular pages 1-3).
- Russo A. Understanding the mammalian TRAP complex function(s). Open Biology. 20 May 2020. https://doi.org/10.1098/rsob.190244 (russo2020understandingthemammalian pages 5-6).
- Verhaegen M., Vermeire K. The ER: a crucial cellular hub in flavivirus infection and potential target site for antiviral interventions. npj Viruses. 6 Jun 2024. https://doi.org/10.1038/s44298-024-00031-7 ().
- Marceau C.D. et al. Genetic dissection of Flaviviridae host factors through genome-scale CRISPR screens. Nature. 22 Jun 2016. https://doi.org/10.1038/nature18631 ().

References

1. (pauwels2023structuralinsightsinto pages 1-2): Eva Pauwels, Neesha R. Shewakramani, Brent De Wijngaert, Anita Camps, Becky Provinciael, Joren Stroobants, Kai-Uwe Kalies, Enno Hartmann, Piet Maes, Kurt Vermeire, and Kalyan Das. Structural insights into trap association with ribosome-sec61 complex and translocon inhibition by a cada derivative. Science Advances, Mar 2023. URL: https://doi.org/10.1126/sciadv.adf0797, doi:10.1126/sciadv.adf0797. This article has 36 citations and is from a highest quality peer-reviewed journal.

2. (pauwels2023structuralinsightsinto pages 2-3): Eva Pauwels, Neesha R. Shewakramani, Brent De Wijngaert, Anita Camps, Becky Provinciael, Joren Stroobants, Kai-Uwe Kalies, Enno Hartmann, Piet Maes, Kurt Vermeire, and Kalyan Das. Structural insights into trap association with ribosome-sec61 complex and translocon inhibition by a cada derivative. Science Advances, Mar 2023. URL: https://doi.org/10.1126/sciadv.adf0797, doi:10.1126/sciadv.adf0797. This article has 36 citations and is from a highest quality peer-reviewed journal.

3. (karki2023molecularviewof pages 1-2): Sudeep Karki, Matti Javanainen, Shahid Rehan, Dale Tranter, Juho Kellosalo, Juha T Huiskonen, Lotta Happonen, and Ville Paavilainen. Molecular view of <scp>er</scp> membrane remodeling by the sec61/<scp>trap</scp> translocon. EMBO reports, Nov 2023. URL: https://doi.org/10.15252/embr.202357910, doi:10.15252/embr.202357910. This article has 17 citations and is from a highest quality peer-reviewed journal.

4. (karki2023molecularviewof pages 2-3): Sudeep Karki, Matti Javanainen, Shahid Rehan, Dale Tranter, Juho Kellosalo, Juha T Huiskonen, Lotta Happonen, and Ville Paavilainen. Molecular view of <scp>er</scp> membrane remodeling by the sec61/<scp>trap</scp> translocon. EMBO reports, Nov 2023. URL: https://doi.org/10.15252/embr.202357910, doi:10.15252/embr.202357910. This article has 17 citations and is from a highest quality peer-reviewed journal.

5. (russo2020understandingthemammalian pages 5-6): Antonietta Russo. Understanding the mammalian trap complex function(s). Open Biology, 10:190244, May 2020. URL: https://doi.org/10.1098/rsob.190244, doi:10.1098/rsob.190244. This article has 28 citations and is from a peer-reviewed journal.

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