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organism_full: Homo sapiens (Human).
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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: Q96GC9
• Protein Description: RecName: Full=Vacuole membrane protein 1 {ECO:0000305}; AltName: Full=Transmembrane protein 49;
• Gene Information: Name=VMP1 {ECO:0000303|PubMed:28890335, ECO:0000312|HGNC:HGNC:29559}; Synonyms=TDC1 {ECO:0000303|Ref.1}, TMEM49 {ECO:0000312|HGNC:HGNC:29559}; ORFNames=HSPC292;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the VMP1 family. .
• Key Domains: Not specified in UniProt

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "VMP1" 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 'VMP1' 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 VMP1 (gene ID: VMP1, UniProt: Q96GC9) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Q96GC9
• Protein Description: RecName: Full=Vacuole membrane protein 1 {ECO:0000305}; AltName: Full=Transmembrane protein 49;
• Gene Information: Name=VMP1 {ECO:0000303|PubMed:28890335, ECO:0000312|HGNC:HGNC:29559}; Synonyms=TDC1 {ECO:0000303|Ref.1}, TMEM49 {ECO:0000312|HGNC:HGNC:29559}; ORFNames=HSPC292;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the VMP1 family. .
• Key Domains: Not specified in UniProt

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "VMP1" 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 'VMP1' 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 VMP1 (gene ID: VMP1, UniProt: Q96GC9) 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.

Comprehensive Research Report: Human VMP1 (TMEM49; UniProt Q96GC9)

Plan and verification
We verified that the target is human Vacuole membrane protein 1 (VMP1), also known as TMEM49, an ER-resident, multi-pass membrane protein in the VMP1/DedA family. Literature reviewed below uses the human VMP1/TMEM49 nomenclature consistent with UniProt Q96GC9 (VMP1; TMEM49 synonyms) (renna2024decodingtheversatile pages 2-3, tong2024vmp1amultifaceted pages 1-2).

1) Key concepts and definitions
- Identity and synonyms: VMP1 (Vacuole membrane protein 1), also annotated as TMEM49; human gene symbol VMP1; multi-pass ER membrane protein of ~406 aa. Identified originally in pancreatitis models and later characterized as a core autophagy protein (review synthesis) (renna2024decodingtheversatile pages 2-3, tong2024vmp1amultifaceted pages 1-2). URL: https://doi.org/10.3390/ijms25073758 (Mar 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).
- Protein family/domain: VMP1 belongs to the DedA/VTT-domain-containing superfamily; predicted to contain two facing reentrant loops typical of DedA folds (mechanistic review) (hama2022regulationofer‐derived pages 3-5). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Molecular function: An ER phospholipid scramblase able to scramble PC, PS, and PE in an ATP- and Ca2+-independent manner; collaborates with TMEM41B and ATG9 scramblases and ATG2 lipid transfer protein during autophagosome biogenesis and broader ER-derived membrane dynamics (authoritative mechanistic review) (hama2022regulationofer‐derived pages 3-5). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).

2) Recent developments and latest research (priority 2023–2024)
- 2024 thematic reviews summarize expanded roles of VMP1 in autophagy (initiation through maturation), ER–phagophore contacts, lipid handling/scrambling, ER Ca2+ control, and disease links across cancer, pancreatitis, neurodegeneration, viral infection; updates include post-translational regulation (palmitoylation, ubiquitination) and miRNA-mediated regulation (miR-21 located within the VMP1/TMEM49 locus) (tong2024vmp1amultifaceted pages 1-2, tong2024vmp1amultifaceted pages 3-4, tong2024vmp1amultifaceted pages 8-8). URLs: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).
- Scramblase paradigm and DedA/VTT structural model reinforced by mechanistic analyses: VMP1/TMEM41B scramble phospholipids to support ATG2-mediated lipid flow from ER to isolation membrane; ATG9 scrambles the phagophore membrane (pre-2023, but definitive mechanistic context still current) (hama2022regulationofer‐derived pages 3-5). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).

3) Molecular function and substrate specificity
- VMP1 functions as a lipid scramblase at the ER, moving phospholipids between bilayer leaflets to equilibrate composition. Substrate scope includes PC, PS, and PE; activity is ATP- and Ca2+-independent in vitro, consistent with in vivo subcellular distribution effects (hama2022regulationofer‐derived pages 3-5). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Functional partners and pathway placement: VMP1 supports ATG2 (bulk lipid transfer) and complements scramblase activities of TMEM41B (ER) and ATG9 (autophagosomal membrane), coordinating lipid supply and leaflet equilibration required for autophagosome expansion (hama2022regulationofer‐derived pages 3-5, tong2024vmp1amultifaceted pages 1-2). URLs: https://doi.org/10.15252/embr.202153894 (Jan 2022); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).

4) Subcellular localization and membrane topology
- Localization: ER-resident, enriched at ER–isolation membrane (phagophore) contact sites during autophagosome biogenesis (renna2024decodingtheversatile pages 2-3, hama2022regulationofer‐derived pages 3-5). URLs: https://doi.org/10.3390/ijms25073758 (Mar 2024); https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Topology: Multi-pass membrane protein with DedA/VTT domain architecture featuring two reentrant loops; this topology is thought to underlie scramblase activity (hama2022regulationofer‐derived pages 3-5). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).

5) Roles in autophagy and lipid transport
- Autophagosome biogenesis: VMP1 is essential for early steps of autophagosome formation. Depletion leads to accumulation of immature LC3-positive vesicles that fail to mature. VMP1 interacts functionally with the Beclin-1/PI3KC3 complex and participates in autophagosome closure; knockout phenotypes show open, non-closed autophagosomes (review synthesis of primary data) (renna2024decodingtheversatile pages 2-3). URL: https://doi.org/10.3390/ijms25073758 (Mar 2024).
- Lipid supply and leaflet equilibration model: VMP1/TMEM41B scramble ER lipids to balance bilayer leaflets as ATG2 transfers bulk lipids to the expanding isolation membrane, while ATG9 scrambles the recipient membrane, enabling efficient membrane expansion and closure (hama2022regulationofer‐derived pages 3-5, tong2024vmp1amultifaceted pages 1-2). URLs: https://doi.org/10.15252/embr.202153894 (Jan 2022); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).
- Broader ER-derived membrane dynamics: VMP1 contributes to lipid droplet biogenesis, hepatic lipoprotein release into the ER lumen, and formation of viral replication double-membrane vesicles (DMVs) (hama2022regulationofer‐derived pages 6-7). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).

6) Regulation and interaction with cellular signaling
- ER Ca2+ handling: VMP1 binds SERCA and its regulators phospholamban (PLN) and sarcolipin (SLN), suppressing inhibitory complexes and activating SERCA; VMP1 deficiency enhances SERCA–PLN/SLN interaction, reducing SERCA activity and altering ER Ca2+ signaling (hama2022regulationofer‐derived pages 6-7). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).
- miRNA regulation: miR-21 maps within the TMEM49/VMP1 locus and is described in an autoregulatory loop context for VMP1; additional miRNAs (e.g., miR-210, miR-124) have been implicated in cancer-related regulation of VMP1 expression (reviewed) (tong2024vmp1amultifaceted pages 3-4, tong2024vmp1amultifaceted pages 8-8). URLs: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).
- Post-translational modifications: Palmitoylation (reported sites Cys263/Cys278; palmitoyltransferase ZDHHC3) affects localization and small extracellular vesicle secretion; ubiquitination via CRL4–DCAF2 impacts autophagy in tumor cells (review synthesis) (tong2024vmp1amultifaceted pages 3-4). URL: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).

7) Disease involvement and translational relevance
- Pancreatitis: VMP1 is rapidly induced in experimental acute pancreatitis; loss of pancreatic acinar VMP1 is linked to spontaneous pancreatitis phenotypes in mice, with associated ER stress and autophagy defects (reviewed synthesis of primary studies) (tong2024vmp1amultifaceted pages 1-2, tong2024vmp1amultifaceted pages 8-9). URLs: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).
- Cancer: Context-dependent roles across tumor types. In pancreatic cancer, VMP1 is linked to KRAS-driven biology and gemcitabine-induced autophagy via an E2F1–EP300–VMP1 axis; reviews detail nuanced pro/anti-tumor roles across colorectal, breast, and hepatocellular carcinoma, including reported RPS6KB1–VMP1 fusions (renna2024decodingtheversatile pages 2-3, tong2024vmp1amultifaceted pages 8-8). URLs: https://doi.org/10.3390/ijms25073758 (Mar 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).
- Neurodegeneration and infection: VMP1 deficiency in dopaminergic neurons is linked to Parkinsonian phenotypes in models; VMP1 acts as a host factor contributing to formation of coronavirus and flavivirus replication organelles (DMVs), consistent with its role in ER lipid remodeling (tong2024vmp1amultifaceted pages 3-4, hama2022regulationofer‐derived pages 6-7). URLs: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024); https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Human genetics and metabolism: Intronic SNPs in VMP1 have been associated with altered circulating LDL levels, linking VMP1 to systemic lipid metabolism (reviewed) (hama2022regulationofer‐derived pages 6-7). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).

8) Current applications and real-world implementations
- Biomarker and therapeutic targeting: Reviews highlight VMP1 as a potential biomarker for diagnosis, prognosis, and therapy response across pancreatitis, cancers, neurodegeneration, hepatitis, and viral infections; however, clinical implementation remains preliminary and context-dependent (tong2024vmp1amultifaceted pages 6-7, renna2024decodingtheversatile pages 2-3). URLs: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024); https://doi.org/10.3390/ijms25073758 (Mar 2024).
- Antiviral and metabolic disease relevance: As a host factor supporting DMV formation and a regulator of lipoprotein secretion and lipid droplets, VMP1 is a conceptual target in antiviral strategies and metabolic liver disease, but translational studies are nascent (hama2022regulationofer‐derived pages 6-7). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).

9) Quantitative data points and statistics (from recent studies where available)
- Autophagy and lipid scrambling: Mechanistic evidence shows ATP- and Ca2+-independent scrambling of PC/PS/PE by VMP1/TMEM41B and reduced PC translocation to the ER lumen in TMEM41B-deficient cells; these data underpin the accepted model for VMP1 function though detailed kinetic constants are not reported in the reviewed excerpts (hama2022regulationofer‐derived pages 3-5). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Human genetics: Association of intronic VMP1 variants with circulating LDL is reported qualitatively in review; effect sizes and p-values were not captured in the present excerpts (hama2022regulationofer‐derived pages 6-7). URL: https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Disease models: Reviews compile multiple primary findings (e.g., pancreatitis models, cancer cell signaling axes), but quantitative statistics (hazard ratios, fold-changes) are not provided in the excerpts and should be consulted in the primary literature referenced by the reviews (renna2024decodingtheversatile pages 2-3, tong2024vmp1amultifaceted pages 1-2).

10) Expert opinions and synthesis
- Consensus view: VMP1 is a core ER scramblase that underpins autophagosome membrane biogenesis by cooperating with ATG2 and ATG9 and is broadly required for ER-derived membrane remodeling, including lipid droplets, lipoproteins, and viral DMVs (hama2022regulationofer‐derived pages 3-5, hama2022regulationofer‐derived pages 6-7). URLs: https://doi.org/10.15252/embr.202153894 (Jan 2022); https://doi.org/10.15252/embr.202153894 (Jan 2022).
- Emerging nuances (2023–2024): Disease-context regulation via miRNAs (notably miR-21 within the TMEM49/VMP1 locus) and PTMs (palmitoylation, ubiquitination) shape VMP1’s localization and function; overlap and partial redundancy with TMEM41B may complicate therapeutic strategies, suggesting combination targeting or pathway-level modulation might be needed (tong2024vmp1amultifaceted pages 3-4, tong2024vmp1amultifaceted pages 6-7). URLs: https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).

Summary table
| Category | Key Points | Primary Sources (with year) | URLs |
|---|---|---:|---|
| Identity & synonyms | Human Vacuole membrane protein 1 (VMP1), also annotated as TMEM49; UniProt Q96GC9; ~406 aa multi-pass ER membrane protein. | Renna et al., 2024 (review) (renna2024decodingtheversatile pages 2-3), Tong et al., 2024 (tong2024vmp1amultifaceted pages 1-2) | https://doi.org/10.3390/ijms25073758, https://doi.org/10.3389/fcell.2024.1436420 |
| Protein family / domain (DedA/VTT) | Member of DedA / VTT-domain–containing family; predicted topology with reentrant loops consistent with DedA fold. | Hama et al., 2022 (EMBO Reports) (hama2022regulationofer‐derived pages 3-5) | https://doi.org/10.15252/embr.202153894 |
| Molecular function (scramblase) | ER-localized phospholipid scramblase activity; scrambles PC, PS, PE (ATP/Ca2+ independent); cooperates functionally with TMEM41B, ATG9, and ATG2 in lipid handling. | Hama et al., 2022 (hama2022regulationofer‐derived pages 3-5), Tong et al., 2024 (tong2024vmp1amultifaceted pages 1-2) | https://doi.org/10.15252/embr.202153894, https://doi.org/10.3389/fcell.2024.1436420 |
| Subcellular localization & topology | Endoplasmic reticulum (ER) resident; multi-pass transmembrane with reentrant loop topology; localizes to ER–phagophore/isolation membrane contact sites. | Renna et al., 2024 (renna2024decodingtheversatile pages 2-3), Hama et al., 2022 (hama2022regulationofer‐derived pages 3-5) | https://doi.org/10.3390/ijms25073758, https://doi.org/10.15252/embr.202153894 |
| Role in autophagy | Required for autophagosome initiation/expansion/closure; interacts functionally with Beclin‑1/PI3KC3 complex and supports ATG2-mediated lipid flow from ER to isolation membrane. | Renna et al., 2024 (renna2024decodingtheversatile pages 2-3), Hama et al., 2022 (hama2022regulationofer‐derived pages 3-5) | https://doi.org/10.3390/ijms25073758, https://doi.org/10.15252/embr.202153894 |
| Lipid metabolism roles | Regulates lipid droplet biogenesis, lipoprotein secretion, and formation of viral double‑membrane replication organelles (DMVs); cooperates/partially redundant with TMEM41B in lipid homeostasis. | Hama et al., 2022 (hama2022regulationofer‐derived pages 6-7), Tong et al., 2024 (tong2024vmp1amultifaceted pages 8-9) | https://doi.org/10.15252/embr.202153894, https://doi.org/10.3389/fcell.2024.1436420 |
| Regulation | Intronic miR‑21 is encoded within TMEM49/VMP1 locus (autoregulation reported); post‑translational regulation includes palmitoylation and ubiquitination (CRL4–DCAF2 pathway); modulates SERCA/ER Ca2+ handling via interactions that affect SERCA–PLN/SLN. | Renna et al., 2024 (renna2024decodingtheversatile pages 2-3), Tong et al., 2024 (tong2024vmp1amultifaceted pages 3-4), Hama et al., 2022 (hama2022regulationofer‐derived pages 6-7) | https://doi.org/10.3390/ijms25073758, https://doi.org/10.3389/fcell.2024.1436420, https://doi.org/10.15252/embr.202153894 |
| Disease links | Loss in pancreatic acinar cells → spontaneous pancreatitis in mouse models; altered expression/roles reported in pancreatic cancer (KRAS context), colorectal/liver cancers, neurodegeneration and viral infection contexts. | Tong et al., 2024 (tong2024vmp1amultifaceted pages 8-9), Renna et al., 2024 (renna2024decodingtheversatile pages 2-3) | https://doi.org/10.3389/fcell.2024.1436420, https://doi.org/10.3390/ijms25073758 |
| Recent reviews / updates (2023–2024) | 2024 comprehensive reviews summarize VMP1 roles in autophagy, lipid scrambling, ER Ca2+ regulation, PTMs, and disease links; 2022–2023 mechanistic work established scramblase activity and DedA/VTT domain model. | Renna et al., 2024 (renna2024decodingtheversatile pages 2-3); Tong et al., 2024 (tong2024vmp1amultifaceted pages 1-2); Hama et al., 2022 (hama2022regulationofer‐derived pages 3-5) | https://doi.org/10.3390/ijms25073758, https://doi.org/10.3389/fcell.2024.1436420, https://doi.org/10.15252/embr.202153894 |

Table: Compact, cited summary of human VMP1 (UniProt Q96GC9) covering identity, domain, molecular function, localization, autophagy/lipid roles, regulation, disease links, and recent 2023–2024 reviews; useful as a quick reference with primary sources and URLs.

Notes on verification and ambiguity
- The symbol VMP1 overlaps historically with TMEM49; both refer to the human gene encoding Vacuole membrane protein 1 (UniProt Q96GC9). The reviewed sources consistently match the human ER multi-pass scramblase defined here. If literature appears to refer to non-human orthologs or unrelated “VMP1” entities, ensure the presence of human TMEM49/VMP1 and ER-scramblase/autophagy context to avoid confusion (renna2024decodingtheversatile pages 2-3, tong2024vmp1amultifaceted pages 1-2).

Limitations and open questions
- While scramblase function and ER–phagophore roles are well supported, high-resolution structures of human VMP1 have not yet been detailed in the present sources, and many quantitative parameters (scrambling rates, binding affinities, genetic effect sizes) require consultation of the primary studies cited within the 2024 reviews and 2022 mechanistic papers (hama2022regulationofer‐derived pages 3-5, renna2024decodingtheversatile pages 2-3, tong2024vmp1amultifaceted pages 1-2). URLs: https://doi.org/10.15252/embr.202153894 (Jan 2022); https://doi.org/10.3390/ijms25073758 (Mar 2024); https://doi.org/10.3389/fcell.2024.1436420 (Jul 2024).

References

1. (renna2024decodingtheversatile pages 2-3): Felipe J. Renna, Claudio D. Gonzalez, and Maria I. Vaccaro. Decoding the versatile landscape of autophagic protein vmp1 in cancer: a comprehensive review across tissue types and regulatory mechanisms. International Journal of Molecular Sciences, 25:3758, Mar 2024. URL: https://doi.org/10.3390/ijms25073758, doi:10.3390/ijms25073758. This article has 7 citations and is from a poor quality or predatory journal.

2. (tong2024vmp1amultifaceted pages 1-2): Jia Tong, Qianqian Wang, Ziyan Gao, Yang Liu, and Chengbiao Lu. Vmp1: a multifaceted regulator of cellular homeostasis with implications in disease pathology. Frontiers in Cell and Developmental Biology, Jul 2024. URL: https://doi.org/10.3389/fcell.2024.1436420, doi:10.3389/fcell.2024.1436420. This article has 8 citations and is from a poor quality or predatory journal.

3. (hama2022regulationofer‐derived pages 3-5): Yutaro Hama, Hideaki Morishita, and Noboru Mizushima. Regulation of er‐derived membrane dynamics by the deda domain‐containing proteins vmp1 and tmem41b. EMBO reports, Jan 2022. URL: https://doi.org/10.15252/embr.202153894, doi:10.15252/embr.202153894. This article has 38 citations and is from a highest quality peer-reviewed journal.

4. (tong2024vmp1amultifaceted pages 3-4): Jia Tong, Qianqian Wang, Ziyan Gao, Yang Liu, and Chengbiao Lu. Vmp1: a multifaceted regulator of cellular homeostasis with implications in disease pathology. Frontiers in Cell and Developmental Biology, Jul 2024. URL: https://doi.org/10.3389/fcell.2024.1436420, doi:10.3389/fcell.2024.1436420. This article has 8 citations and is from a poor quality or predatory journal.

5. (tong2024vmp1amultifaceted pages 8-8): Jia Tong, Qianqian Wang, Ziyan Gao, Yang Liu, and Chengbiao Lu. Vmp1: a multifaceted regulator of cellular homeostasis with implications in disease pathology. Frontiers in Cell and Developmental Biology, Jul 2024. URL: https://doi.org/10.3389/fcell.2024.1436420, doi:10.3389/fcell.2024.1436420. This article has 8 citations and is from a poor quality or predatory journal.

6. (hama2022regulationofer‐derived pages 6-7): Yutaro Hama, Hideaki Morishita, and Noboru Mizushima. Regulation of er‐derived membrane dynamics by the deda domain‐containing proteins vmp1 and tmem41b. EMBO reports, Jan 2022. URL: https://doi.org/10.15252/embr.202153894, doi:10.15252/embr.202153894. This article has 38 citations and is from a highest quality peer-reviewed journal.

7. (tong2024vmp1amultifaceted pages 8-9): Jia Tong, Qianqian Wang, Ziyan Gao, Yang Liu, and Chengbiao Lu. Vmp1: a multifaceted regulator of cellular homeostasis with implications in disease pathology. Frontiers in Cell and Developmental Biology, Jul 2024. URL: https://doi.org/10.3389/fcell.2024.1436420, doi:10.3389/fcell.2024.1436420. This article has 8 citations and is from a poor quality or predatory journal.

8. (tong2024vmp1amultifaceted pages 6-7): Jia Tong, Qianqian Wang, Ziyan Gao, Yang Liu, and Chengbiao Lu. Vmp1: a multifaceted regulator of cellular homeostasis with implications in disease pathology. Frontiers in Cell and Developmental Biology, Jul 2024. URL: https://doi.org/10.3389/fcell.2024.1436420, doi:10.3389/fcell.2024.1436420. This article has 8 citations and is from a poor quality or predatory journal.

Citations

1. renna2024decodingtheversatile pages 2-3
2. https://doi.org/10.3390/ijms25073758
3. https://doi.org/10.3389/fcell.2024.1436420
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