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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:** Q9Y6X1
- **Protein Description:** RecName: Full=Stress-associated endoplasmic reticulum protein 1; AltName: Full=Ribosome-attached membrane protein 4;
- **Gene Information:** Name=SERP1; Synonyms=RAMP4;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the RAMP4 family. .
- **Key Domains:** ER_stress-assoc. (IPR010580); RAMP4 (PF06624)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "SERP1" 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 'SERP1' 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 **SERP1** (gene ID: SERP1, UniProt: Q9Y6X1) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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:** Q9Y6X1
- **Protein Description:** RecName: Full=Stress-associated endoplasmic reticulum protein 1; AltName: Full=Ribosome-attached membrane protein 4;
- **Gene Information:** Name=SERP1; Synonyms=RAMP4;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the RAMP4 family. .
- **Key Domains:** ER_stress-assoc. (IPR010580); RAMP4 (PF06624)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "SERP1" 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 'SERP1' 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 **SERP1** (gene ID: SERP1, UniProt: Q9Y6X1) 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.

# Research Report: Human **SERP1** (RAMP4) — Functional Annotation (UniProt Q9Y6X1)

## Executive summary
Human **SERP1** (UniProt **Q9Y6X1**), also known as **RAMP4** (ribosome-attached membrane protein 4), is a **small tail-anchored ER membrane protein** that associates tightly with **ribosome–Sec61 translocon** complexes. Recent structural work (2024) supports a direct mechanistic role in **modulating Sec61 channel gating** by **intercalating into the Sec61 lateral gate**, widening the pore and contributing to a more hydrophilic lumenal funnel—features consistent with SERP1’s established connection to **ER stress adaptation and proteostasis**. (lewis2024structuralanalysisof pages 1-2, lewis2024structuralanalysisof pages 4-6)

A compact evidence map with key claims, quantitative data, and URLs is provided below.

| Topic | Key evidence/claim | Quantitative details | Primary sources |
|---|---|---|---|
| Identity / localization | SERP1 is the same protein as RAMP4 and is a small tail-anchored endoplasmic reticulum (ER) membrane protein associated with ribosome-bound Sec61 translocon complexes in human cells. Structural work places it at the ER ribosome–translocon interface rather than as a soluble stress factor (lewis2024structuralanalysisof pages 1-2, lewis2024structuralanalysisof pages 4-6, lewis2024structuralanalysisof pages 28-29). | Human RAMP4 sequence shown in structural study; TMD length ~25 aa; occupancy enriched in non-MPT RTCs (see quantitative row) (lewis2024structuralanalysisof pages 4-6, lewis2024structuralanalysisof pages 6-8). | Lewis 2024 eLife. https://doi.org/10.1101/2023.12.22.572959; Gemmer & Förster 2020 Journal of Cell Science. https://doi.org/10.1242/jcs.231340 |
| Structure & mechanism | 2024 cryo-EM/AF2 analysis shows RAMP4 has a ribosome-binding domain plus a kinked transmembrane helix that intercalates into Sec61’s lateral gate, widens the pore, and helps form a more hydrophilic lumenal funnel without displacing the plug helix. Authors propose RAMP4 can stabilize an open-but-plugged Sec61 state and may act as a surrogate signal peptide after substrate SP release (lewis2024structuralanalysisof pages 4-6, lewis2024structuralanalysisof pages 9-11, lewis2024structuralanalysisof pages 1-2, lewis2024structuralanalysisof pages 28-29). | TMD kink ~40° at a conserved glycine; RAMP4 present in ~81% of non-MPT RTCs; ~85% of Sec61•TRAP•OSTA RTCs and ~53% of Sec61•TRAP RTCs (lewis2024structuralanalysisof pages 6-8, lewis2024structuralanalysisof pages 4-6). | Lewis 2024 eLife. https://doi.org/10.1101/2023.12.22.572959 |
| ER stress regulation | SERP1/RAMP4 is stress inducible and functionally linked to ER proteostasis. In cell/animal injury and infection models, increased SERP1 accompanies ER stress, whereas SERP1 overexpression dampens ER-stress markers and apoptosis/inflammation, supporting a protective role during ER stress (tian2019adenguevirus pages 1-3, cai2022serp1reducesinchoate pages 3-5). | DENV-2 infection/replicon: SERP1 expression increased 34.5-fold; acute hepatic injury study reported LPS-induced SERP1 increase and reduction of GRP78/GRP94/CHOP with SERP1 overexpression; in liver study, Torin1 not used here, but 4-PBA-like protective effect noted (tian2019adenguevirus pages 1-3, cai2022serp1reducesinchoate pages 3-5). | Tian 2019 Viruses. https://doi.org/10.3390/v11090787; Cai 2022 Molecular Medicine Reports. https://doi.org/10.3892/mmr.2022.12709 |
| Interacting partners | SERP1/RAMP4 interacts with Sec61α and Sec61β and directly contacts the ribosome. Structural mapping places its ribosome-binding domain against 28S rRNA helices and ribosomal proteins, while functional virology work identified interaction with DENV-2 NS4B, linking SERP1 to ER-associated viral replication biology (lewis2024structuralanalysisof pages 4-6, tian2019adenguevirus pages 1-3). | Ribosome contacts include 28S rRNA helices 47, 57, 59 and proteins eL19, eL22, eL31; DENV-2 NS4B overexpression alleviated SERP1-mediated inhibition of replication (lewis2024structuralanalysisof pages 4-6, tian2019adenguevirus pages 1-3). | Lewis 2024 eLife. https://doi.org/10.1101/2023.12.22.572959; Tian 2019 Viruses. https://doi.org/10.3390/v11090787 |
| ER-phagy reporter applications | SERP1/RAMP4 is used as an ER-targeting module in reticulophagy/ER-phagy reporters. Tandem fluorescent SERP1/RAMP4 reporters exploit acid-sensitive GFP loss with retained mCherry/RFP signal after ER fragments reach lysosomes, enabling imaging- or flow-based ER-phagy readouts; 2024 methodological work also highlights caveats from reporter overexpression and recommends knock-in/endogenous-tagging strategies for in vivo use (sang2024visualizingerphagyand pages 2-3, liu2025theepsteinbarrvirus pages 9-10, sang2024visualizingerphagyand pages 1-2, sang2024visualizingerphagyand pages 22-25). | Keima excitation shift ~440 nm to ~586 nm in acidic lysosomes; Torin1 induction example 100 nM for 4 h; quantification used 20–30 cells/condition; readout is red-only puncta or GFP loss relative to mCherry (sang2024visualizingerphagyand pages 2-3, sang2024visualizingerphagyand pages 22-25). | Sang 2024 Journal of Cell Biology. https://doi.org/10.1083/jcb.202408061; Liu 2025 Autophagy. https://doi.org/10.1080/15548627.2024.2440846 |
| Disease / biomarker associations | SERP1 has emerging disease relevance mainly through expression- and signature-based evidence rather than established causal clinical genetics in this corpus. It appears in a 12-gene ER-stress prognostic signature for pancreatic cancer and is described as a risk-associated factor; Open Targets also lists weaker literature/animal-model/genetic-association links to neoplasm, liver disease, drug allergy, dystonia 33, and Marinesco-Sjögren syndrome (chen2023arisksignature pages 3-6, OpenTargets Search: -SERP1, chen2023arisksignature pages 12-13, chen2023arisksignature pages 8-12, chen2023arisksignature pages 6-8). | Pancreatic cancer model coefficient for SERP1: 0.496637586; signature AUC ~0.79; low- vs high-risk survival difference p < 0.0001; multivariate HR = 3.613, p < 0.001 for risk level (chen2023arisksignature pages 6-8). | Chen 2023 Frontiers in Molecular Biosciences. https://doi.org/10.3389/fmolb.2023.1298077; Open Targets Platform evidence summary (OpenTargets Search: -SERP1) |
| Quantitative stats | Available quantitative evidence consistently supports a translocon-centered, stress-responsive role. Structurally, RAMP4 is abundant in non-MPT RTCs; functionally, perturbing SERP1 changes viral replication and prognostic models; assay literature provides explicit doses/timings for reporter use (lewis2024structuralanalysisof pages 6-8, tian2019adenguevirus pages 1-3, chen2023arisksignature pages 6-8, sang2024visualizingerphagyand pages 22-25). | RTC occupancy: ~85% Sec61•TRAP•OSTA, ~53% Sec61•TRAP, ~81% non-MPT RTCs; DENV-2: SERP1 induction 34.5-fold, viral yields reduced ~37-fold by overexpression, increased ~3.4-fold after shRNA knockdown and ~16-fold after knockout; ER-phagy assay: Torin1 100 nM, 4 h, 20–30 cells/condition (lewis2024structuralanalysisof pages 6-8, tian2019adenguevirus pages 1-3, sang2024visualizingerphagyand pages 22-25). | Lewis 2024 eLife. https://doi.org/10.1101/2023.12.22.572959; Tian 2019 Viruses. https://doi.org/10.3390/v11090787; Chen 2023 Frontiers in Molecular Biosciences. https://doi.org/10.3389/fmolb.2023.1298077; Sang 2024 Journal of Cell Biology. https://doi.org/10.1083/jcb.202408061 |


*Table: This table summarizes functional annotation evidence for human SERP1/RAMP4 (UniProt Q9Y6X1), including localization, mechanism, stress biology, applications, disease associations, and key quantitative findings. It is useful as a traceable, citation-linked overview of the strongest gathered evidence.*

## 1. Key concepts and definitions (current understanding)

### 1.1 Correct gene/protein identity (mandatory verification)
The target gene **SERP1** corresponds to the ER protein commonly called **RAMP4**, and the literature retrieved here explicitly uses “SERP1 (RAMP4)” as a unified identity. (tian2019adenguevirus pages 1-3, lewis2024structuralanalysisof pages 1-2)

### 1.2 What SERP1/RAMP4 is (molecular description)
SERP1/RAMP4 is described as a **tail-anchored ER membrane protein**. A 2024 cryo-EM/structure-prediction analysis resolves distinct architectural features: a **ribosome-binding domain (RBD)** connected through a linker to a **kinked transmembrane domain (TMD)** that engages the Sec61 lateral gate. (lewis2024structuralanalysisof pages 4-6)

### 1.3 What SERP1/RAMP4 does (functional definition)
The best-supported primary function from mechanistic evidence is that SERP1/RAMP4 acts as a **translocon-associated factor** that **directly modulates Sec61 channel conformation** and therefore influences **co-translational translocation and membrane protein/secretory protein biogenesis** at the ER. (lewis2024structuralanalysisof pages 4-6, lewis2024structuralanalysisof pages 1-2)

## 2. Subcellular localization and core molecular mechanism

### 2.1 Localization: ER membrane at ribosome–translocon complexes
SERP1/RAMP4 is associated with **ribosome-bound ER translocon complexes**. Reviews and structural work identify it among “ribosome-associated membrane proteins (RAMPs)” recovered from ER microsomes and linked to Sec61-containing assemblies. (gemmer2020aclearerpicture pages 2-3, lewis2024structuralanalysisof pages 1-2)

### 2.2 2024 structural mechanism: occupancy and Sec61 gating model
**Major 2024 advance (Lewis et al., eLife, May 2024):** RAMP4 is frequently observed **intercalated into Sec61’s lateral gate**, and this configuration **widens the Sec61 pore** and contributes to a more hydrophilic pore interior. (lewis2024structuralanalysisof pages 1-2)

Mechanistic details include:
- The RBD contacts the ribosome (28S rRNA helices and ribosomal proteins), and the TMD occupies the lateral gate. (lewis2024structuralanalysisof pages 4-6)
- The pore ring is widened, while the plug helix can remain present (open-but-plugged conformation). (lewis2024structuralanalysisof pages 4-6, lewis2024structuralanalysisof pages 28-29)
- **Quantitative occupancy** in native ribosome–translocon complexes (RTCs): ~**85%** of Sec61•TRAP•OSTA RTCs and ~**53%** of Sec61•TRAP RTCs contain RAMP4, corresponding to ~**81%** of **non-MPT** RTCs. (lewis2024structuralanalysisof pages 6-8)

**Expert interpretation (from the authors’ mechanistic hypotheses):** the structure supports the idea that RAMP4 can function as a **regulatory translocon component**, potentially including a “surrogate signal peptide” role that stabilizes an open channel state after substrate signal peptide dissociation. (lewis2024structuralanalysisof pages 9-11)

## 3. SERP1 as an ER-stress-associated proteostasis factor

### 3.1 Evidence for ER-stress inducibility
In a DENV-2 infection/replicon system, SERP1 mRNA showed a **34.5-fold induction** in Huh7.5 cells under viral conditions that impose ER stress. (tian2019adenguevirus pages 1-3)

In an acute hepatic injury model (LPS/D-GalN in vivo; LPS in hepatocytes), SERP1 expression increased alongside ER stress markers, and SERP1 overexpression reduced ER stress markers (GRP78/GRP94/CHOP) and decreased apoptosis/inflammation readouts. (cai2022serp1reducesinchoate pages 3-5)

### 3.2 Interacting partners relevant to its function
Functional virology work reports SERP1/RAMP4 interacts with **Sec61α and Sec61β**, supporting a direct relationship to the Sec61 translocation machinery. (tian2019adenguevirus pages 1-3)

## 4. Recent developments and latest research (prioritizing 2023–2024)

### 4.1 2024: Structural integration into the Sec61 lateral gate
Lewis et al. (2024; eLife; publication month May 2024) provide the most direct mechanistic update: RAMP4 is physically located within the Sec61 lateral gate in a large fraction of RTCs, and the model predicts effects on pore hydrophilicity and gating states. URL: https://doi.org/10.1101/2023.12.22.572959 (lewis2024structuralanalysisof pages 1-2, lewis2024structuralanalysisof pages 4-6)

### 4.2 2024: SERP1/RAMP4 as an ER-phagy (reticulophagy) reporter module
A 2024 Journal of Cell Biology methods-focused study emphasizes how ER-phagy reporters are interpreted and flags caveats of RAMP4 overexpression, motivating **knock-in/endogenous-tagging** approaches for in vivo work. It cites RAMP4-based reporters (e.g., GFP-mCherry-RAMP4; RAMP4-Keima) and explains their readouts. URL: https://doi.org/10.1083/jcb.202408061 (sang2024visualizingerphagyand pages 2-3)

### 4.3 2023: Bioinformatic evidence as part of ER-stress prognostic signatures
A 2023 pancreatic cancer study includes SERP1 in a 12-gene ER-stress-associated risk score; the risk formula includes a SERP1 coefficient (**0.496637586 × SERP1**) and reports predictive performance (AUC ~**0.79**) for the composite signature, with strong risk-group survival differences (p < 0.0001). URL: https://doi.org/10.3389/fmolb.2023.1298077 (chen2023arisksignature pages 6-8)

## 5. Current applications and real-world implementations

### 5.1 Cell-based and in vivo ER-phagy/reticulophagy assays using SERP1/RAMP4
SERP1/RAMP4 is used as an ER-targeting module in dual fluorescence reporters that quantify ER-to-lysosome flux via **pH-dependent GFP loss** relative to mCherry/RFP.

Examples of implemented designs:
- A Dox-regulated stable HCT116 line expressing an in-frame **SERP1/RAMP4–eGFP–mCherry** fusion reporter; interpretation: ER insertion yields dual signal; lysosomal delivery yields loss of GFP relative to mCherry. (liu2025theepsteinbarrvirus pages 9-10)
- RAMP4-based and related ratiometric reporter strategies described for ER-phagy flux estimation, including Keima-based excitation shift (~440 nm to ~586 nm) and tandem FP “red-only puncta” scoring. (sang2024visualizingerphagyand pages 2-3)

Practical assay parameters reported in 2024 methods include **Torin1 100 nM for 4 h** to induce autophagy/ER-phagy, and quantification approaches using lysosomal colocalization and ImageJ, with **20–30 cells per condition** in one described analysis. (sang2024visualizingerphagyand pages 22-25)

### 5.2 Biomarker-style use in cancer transcriptomic models
SERP1 is used as one feature in multi-gene ER-stress signatures for prognosis stratification in pancreatic cancer, suggesting potential application as a component of composite biomarkers (rather than a standalone validated clinical biomarker based on this corpus). (chen2023arisksignature pages 6-8, chen2023arisksignature pages 3-6)

## 6. Disease associations: current evidence level and interpretation

### 6.1 Open Targets overview (evidence-type aware)
Open Targets lists SERP1 associations with disease terms including **neoplasm**, **liver disease**, **drug allergy**, **dystonia 33**, and **Marinesco-Sjögren syndrome**, with evidence types including literature, animal model, and genetic association (source-dependent). This indicates heterogeneous, generally low-to-moderate strength associations in the platform snapshot retrieved here. (OpenTargets Search: -SERP1)

### 6.2 Primary literature in this corpus (expression/prognosis focus)
In the pancreatic cancer study, SERP1 contributes to a multi-gene risk score associated with overall survival, but the same work also notes SERP1 alone was not significantly differentially expressed in one tumor-vs-normal comparison figure, illustrating that its importance may be multivariate/context-specific. (chen2023arisksignature pages 3-6, chen2023arisksignature pages 6-8)

## 7. Relevant statistics and data (from recent and foundational studies)

- **RAMP4 occupancy in RTC subclasses (2024 cryo-EM):** ~85% in Sec61•TRAP•OSTA RTCs; ~53% in Sec61•TRAP RTCs; ~81% in non-MPT RTCs. (lewis2024structuralanalysisof pages 6-8)
- **ER stress induction magnitude (2019 infection model):** SERP1 mRNA induced **34.5-fold** in DENV-2 infected/replicon-transfected Huh7.5 cells. (tian2019adenguevirus pages 1-3)
- **Prognostic model coefficient & performance (2023):** SERP1 coefficient **0.496637586** in risk score; signature AUC ~**0.79**; risk-group OS p < 0.0001; multivariate HR **3.613** for risk level (not SERP1 alone). (chen2023arisksignature pages 6-8)
- **ER-phagy assay implementation detail (2024 methods):** Torin1 **100 nM, 4 h**; quantification across **20–30 cells/condition** in an example workflow. (sang2024visualizingerphagyand pages 22-25)

## 8. Limitations and confidence notes
- The strongest direct mechanistic evidence for SERP1/RAMP4 function comes from **structural biology (2024)** and places SERP1 at **Sec61 gating**; functional stress-protection studies exist but are more context dependent (viral infection, liver injury models) and may not fully isolate direct translocon-gating effects from downstream signaling. (lewis2024structuralanalysisof pages 4-6, cai2022serp1reducesinchoate pages 3-5)
- Many disease links in this corpus are **bioinformatic/prognostic** or platform-aggregated rather than causal human genetics; these should be treated as hypothesis-generating without additional validation. (OpenTargets Search: -SERP1, chen2023arisksignature pages 6-8)

## Selected primary sources (URLs; publication dates as retrieved)
- Lewis AJO et al. **May 2024**. *Structural analysis of the dynamic ribosome-translocon complex* (eLife). https://doi.org/10.1101/2023.12.22.572959 (lewis2024structuralanalysisof pages 1-2)
- Sang Y et al. **Nov 2024**. *Visualizing ER-phagy and ER architecture in vivo* (J Cell Biol). https://doi.org/10.1083/jcb.202408061 (sang2024visualizingerphagyand pages 2-3)
- Chen H et al. **Nov 2023**. *A risk signature based on endoplasmic reticulum stress-associated genes predicts prognosis and immunity in pancreatic cancer* (Front Mol Biosci). https://doi.org/10.3389/fmolb.2023.1298077 (chen2023arisksignature pages 6-8)
- Gemmer M & Förster F. **Feb 2020**. *A clearer picture of the ER translocon complex* (J Cell Sci). https://doi.org/10.1242/jcs.231340 (gemmer2020aclearerpicture pages 2-3)
- Tian J-N et al. **Aug 2019**. *DENV-2 NS4B-interacting host factor SERP1 reduces DENV-2 production…* (Viruses). https://doi.org/10.3390/v11090787 (tian2019adenguevirus pages 1-3)
- Cai J et al. **Apr 2022**. *SERP1 reduces inchoate acute hepatic injury…* (Mol Med Rep). https://doi.org/10.3892/mmr.2022.12709 (cai2022serp1reducesinchoate pages 3-5)


References

1. (lewis2024structuralanalysisof pages 1-2): Aaron J. O. Lewis, Frank Zhong, Robert J. Keenan, and Ramanujan S. Hegde. Structural analysis of the dynamic ribosome-translocon complex. eLife, May 2024. URL: https://doi.org/10.1101/2023.12.22.572959, doi:10.1101/2023.12.22.572959. This article has 23 citations and is from a domain leading peer-reviewed journal.

2. (lewis2024structuralanalysisof pages 4-6): Aaron J. O. Lewis, Frank Zhong, Robert J. Keenan, and Ramanujan S. Hegde. Structural analysis of the dynamic ribosome-translocon complex. eLife, May 2024. URL: https://doi.org/10.1101/2023.12.22.572959, doi:10.1101/2023.12.22.572959. This article has 23 citations and is from a domain leading peer-reviewed journal.

3. (lewis2024structuralanalysisof pages 28-29): Aaron J. O. Lewis, Frank Zhong, Robert J. Keenan, and Ramanujan S. Hegde. Structural analysis of the dynamic ribosome-translocon complex. eLife, May 2024. URL: https://doi.org/10.1101/2023.12.22.572959, doi:10.1101/2023.12.22.572959. This article has 23 citations and is from a domain leading peer-reviewed journal.

4. (lewis2024structuralanalysisof pages 6-8): Aaron J. O. Lewis, Frank Zhong, Robert J. Keenan, and Ramanujan S. Hegde. Structural analysis of the dynamic ribosome-translocon complex. eLife, May 2024. URL: https://doi.org/10.1101/2023.12.22.572959, doi:10.1101/2023.12.22.572959. This article has 23 citations and is from a domain leading peer-reviewed journal.

5. (lewis2024structuralanalysisof pages 9-11): Aaron J. O. Lewis, Frank Zhong, Robert J. Keenan, and Ramanujan S. Hegde. Structural analysis of the dynamic ribosome-translocon complex. eLife, May 2024. URL: https://doi.org/10.1101/2023.12.22.572959, doi:10.1101/2023.12.22.572959. This article has 23 citations and is from a domain leading peer-reviewed journal.

6. (tian2019adenguevirus pages 1-3): Jia-Ni Tian, Chi-Chen Yang, Chiu-Kai Chuang, Ming-Han Tsai, Ren-Huang Wu, Chiung-Tong Chen, and Andrew Yueh. A dengue virus type 2 (denv-2) ns4b-interacting host factor, serp1, reduces denv-2 production by suppressing viral rna replication. Viruses, 11:787, Aug 2019. URL: https://doi.org/10.3390/v11090787, doi:10.3390/v11090787. This article has 19 citations.

7. (cai2022serp1reducesinchoate pages 3-5): Jie Cai, Zhenhua Sun, Lili Zhang, and Hongrui Xu. Serp1 reduces inchoate acute hepatic injury through regulation of endoplasmic reticulum stress via the gsk3β/β-catenin/tcf/lef signaling pathway. Molecular Medicine Reports, Apr 2022. URL: https://doi.org/10.3892/mmr.2022.12709, doi:10.3892/mmr.2022.12709. This article has 7 citations and is from a peer-reviewed journal.

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## Artifacts

- [Edison artifact artifact-00](SERP1-deep-research-falcon_artifacts/artifact-00.md)

## Citations

1. chen2023arisksignature pages 6-8
2. lewis2024structuralanalysisof pages 4-6
3. lewis2024structuralanalysisof pages 1-2
4. lewis2024structuralanalysisof pages 6-8
5. lewis2024structuralanalysisof pages 9-11
6. tian2019adenguevirus pages 1-3
7. sang2024visualizingerphagyand pages 2-3
8. liu2025theepsteinbarrvirus pages 9-10
9. sang2024visualizingerphagyand pages 22-25
10. gemmer2020aclearerpicture pages 2-3
11. lewis2024structuralanalysisof pages 28-29
12. sang2024visualizingerphagyand pages 1-2
13. chen2023arisksignature pages 3-6
14. chen2023arisksignature pages 12-13
15. chen2023arisksignature pages 8-12
16. https://doi.org/10.1101/2023.12.22.572959;
17. https://doi.org/10.1242/jcs.231340
18. https://doi.org/10.1101/2023.12.22.572959
19. https://doi.org/10.3390/v11090787;
20. https://doi.org/10.3892/mmr.2022.12709
21. https://doi.org/10.3390/v11090787
22. https://doi.org/10.1083/jcb.202408061;
23. https://doi.org/10.1080/15548627.2024.2440846
24. https://doi.org/10.3389/fmolb.2023.1298077;
25. https://doi.org/10.1083/jcb.202408061
26. https://doi.org/10.3389/fmolb.2023.1298077
27. https://doi.org/10.1101/2023.12.22.572959,
28. https://doi.org/10.3390/v11090787,
29. https://doi.org/10.3892/mmr.2022.12709,
30. https://doi.org/10.1083/jcb.202408061,
31. https://doi.org/10.1080/15548627.2024.2440846,
32. https://doi.org/10.3389/fmolb.2023.1298077,
33. https://doi.org/10.1242/jcs.231340,