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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
ERLIN1 (ER lipid raft–associated protein 1; UniProt O75477) is an endoplasmic-reticulum (ER) membrane protein in the SPFH/band7 (prohibitin/PHB-domain) superfamily and forms high–molecular-weight oligomers with its close paralog ERLIN2 in cholesterol-rich, detergent-resistant ER nanodomains (“ER lipid rafts”). (manganelli2021roleoferlins pages 1-2, manganelli2021roleoferlins pages 3-5, veronese2024erlin12scaffoldsbridge pages 1-2)
Operationally in the recent literature, “ERLIN1/2 complex” refers to hetero-oligomeric ERLIN1+ERLIN2 scaffolds that (i) recruit specific client proteins and (ii) organize lipid/protein microdomains that couple lipid homeostasis with protein quality control and membrane trafficking. (veronese2024erlin12scaffoldsbridge pages 4-6, veronese2024erlin12scaffoldsbridge pages 1-2)
A 2024 mechanistic study (Life Science Alliance; publication month May 2024) provides direct experimental evidence that ERLIN1 (with ERLIN2) forms ER scaffolds/nanodomains that:
Quantitatively, this study reports: (i) interaction/proteomics work at the scale of 2,742 proteins in a post-nuclear supernatant dataset and N=4 biological replicates for key proteomics comparisons; (ii) a tendency to increased SOAT1 abundance in ERLIN double knockout cells (SOAT1 log2FC = 0.40; q = 0.07); and (iii) rescue of lipid-droplet accumulation phenotypes using a SOAT1 inhibitor (avasimibe). (veronese2024erlin12scaffoldsbridge pages 4-6, veronese2024erlin12scaffoldsbridge pages 12-12, veronese2024erlin12scaffoldsbridge pages 2-4)
URL / date: Veronese et al. “ERLIN1/2 scaffolds bridge TMUB1 and RNF170 and restrict cholesterol esterification to regulate the secretory pathway.” Life Science Alliance (May 2024). https://doi.org/10.26508/lsa.202402620 (veronese2024erlin12scaffoldsbridge pages 1-2)
Visual evidence: the ERLIN1/2–RNF170–TMUB1-L scaffold model is depicted in a schematic (Figure 3A). (veronese2024erlin12scaffoldsbridge media 40d635ea)
Multiple sources converge on a core pathway-level role for ERLIN1/2 in IP3 receptor (IP3R) turnover via ERAD:
A particularly specific quantitative statement highlighted in that 2024 disease analysis is that unique ablation of ERLIN1 expression is sufficient to increase IP3R1 levels by ~73% in vitro, consistent with reduced IP3R ERAD and altered ER Ca2+ release dynamics. (cogan2024biallelicvariantsin pages 12-16)
URL / date: Cogan et al. “Biallelic variants in ERLIN1: a series of 13 individuals with spastic paraparesis.” Human Genetics (Oct 2024). https://doi.org/10.1007/s00439-024-02702-0 (cogan2024biallelicvariantsin pages 1-6)
ERLIN1 can function at specialized ER subdomains, including mitochondria-associated membranes (MAMs). A detailed review synthesizing primary evidence reports that:
These data support a model where ERLIN1 contributes to microdomain-dependent recruitment/organization of autophagy initiation machinery at ER–mitochondria contact sites.
URL / date: Manganelli et al. “Role of ERLINs in the Control of Cell Fate through Lipid Rafts.” Cells (Sep 2021). https://doi.org/10.3390/cells10092408 (manganelli2021roleoferlins pages 1-2)
The Veronese et al. 2024 work materially advances functional annotation by showing ERLIN1/2 are not only “markers” of ER rafts but active organizers of an ER nanodomain network that:
This provides a more mechanistic explanation for how ERLIN1 variants might cause disease beyond a single-client ERAD model—i.e., by perturbing an integrated lipid–proteostasis–trafficking hub. (veronese2024erlin12scaffoldsbridge pages 12-12)
Cogan et al. (Oct 2024) report the largest series of biallelic ERLIN1 variants to date: 13 individuals from 6 families with early-onset spastic paraparesis. (cogan2024biallelicvariantsin pages 1-6, cogan2024biallelicvariantsin pages 6-9)
Key statistics and clinical features:
Mechanistically, variants were interpreted as impairing ERLIN1/2 cage formation (PHB/SPFH region), consistent with disruption of IP3R ERAD/Ca2+ signaling and potentially broader ER microdomain functions. (cogan2024biallelicvariantsin pages 9-12, cogan2024biallelicvariantsin pages 12-16)
The 2024 SPG62 series demonstrates direct real-world implementation of ERLIN1 knowledge in diagnostic genomics:
The 2024 ERLIN scaffold study provides a blueprint for experimental implementation:
A well-controlled cell-culture study shows that ERLIN1 is required for efficient HCV infection and particle production:
URL / date: Whitten-Bauer et al. “The Host Factor Erlin-1 is Required for Efficient Hepatitis C Virus Infection.” Cells (Dec 2019). https://doi.org/10.3390/cells8121555 (whittenbauer2019thehostfactor pages 1-3)
A transcriptome-mining plus validation study reports that ERLIN1 is consistently upregulated in septic immune contexts, especially neutrophil-associated settings:
URL / date: Huang et al. “Transcriptome and Literature Mining Highlight the Differential Expression of ERLIN1 in Immune Cells during Sepsis.” Biology (Aug 2021). https://doi.org/10.3390/biology10080755 (huang2021transcriptomeandliterature pages 1-2)
The combined 2024 mechanistic and 2024 clinical-genetic evidence supports a coherent primary functional annotation:
ERLIN1’s association with MAM raft-like microdomains and AMBRA1 suggests ERLIN1 scaffolds can be repurposed at ER contact sites to support autophagy initiation, potentially by organizing lipid microdomains that recruit core autophagy regulators. (manganelli2021roleoferlins pages 7-9)
| Function/pathway | Key mechanistic role | Key interaction partners | Subcellular localization/microdomain | Evidence type | Quantitative/other notable data | Key citations (context IDs) and source (authors, year, DOI URL) |
|---|---|---|---|---|---|---|
| ERLIN1 identity and core complex biology | Human ERLIN1 (UniProt O75477; ER lipid raft-associated protein 1) is a ~40 kDa ER membrane SPFH/PHB-family protein that hetero-oligomerizes with ERLIN2 to form large ring/cage-like scaffolds in cholesterol-rich ER nanodomains | ERLIN2 | Endoplasmic reticulum; detergent-resistant/lipid raft-like ER membrane domains; MAMs under some conditions | Review synthesis; biochemical fractionation; structural/topology inference | ERLIN1/2 described as ~40 kDa transmembrane glycoproteins; ERLIN1 is 348 aa; complexes reported as ~1000 kDa or ~40-subunit/ring-like assemblies depending on method/model | (manganelli2021roleoferlins pages 1-2, manganelli2021roleoferlins pages 3-5, veronese2024erlin12scaffoldsbridge pages 1-2, cogan2024biallelicvariantsin pages 1-6) Manganelli et al., 2021, https://doi.org/10.3390/cells10092408; Veronese et al., 2024, https://doi.org/10.26508/lsa.202402620; Cogan et al., 2024, https://doi.org/10.1007/s00439-024-02702-0 |
| Cholesterol esterification control and secretory pathway regulation | ERLIN1/2 scaffolds bridge TMUB1-L and RNF170 at ER nanodomains, restricting cholesterol esterification, favoring ER-to-Golgi cholesterol transport, and maintaining ER/Golgi architecture and secretory trafficking | ERLIN2, TMUB1-L, RNF170, TMEM259, RNF185, FAF2, VCP, ARF1/4, SOAT1 | ER membrane nanodomains; detergent-resistant membranes; ER-Golgi contact-associated regions | CRISPR/Cas9 ERLIN1/2 double KO; MS-IP; reciprocal co-IP; AlphaFold-Multimer modeling; proteomics; DRM flotation; rescue experiments | Loss of ERLINs completely prevented TMUB1-RNF170 interaction; proteomics quantified 2,742 proteins and identified 34 significant hits; SOAT1 tended to increase in DKO (log2FC 0.40, q=0.07); ERLIN loss caused ER tubule collapse, Golgi fragmentation, lipid droplet accumulation, impaired post-Golgi trafficking and migration defects; N=4 biological replicates in key proteomics | (veronese2024erlin12scaffoldsbridge pages 4-6, veronese2024erlin12scaffoldsbridge pages 12-12, veronese2024erlin12scaffoldsbridge pages 2-4, veronese2024erlin12scaffoldsbridge pages 1-2, veronese2024erlin12scaffoldsbridge media 40d635ea) Veronese et al., 2024, https://doi.org/10.26508/lsa.202402620 |
| ERAD of activated IP3 receptors and Ca2+ signaling | ERLIN1/2 complex recruits or scaffolds RNF170 to promote ubiquitination and ER-associated degradation of activated IP3 receptors, thereby shaping ER Ca2+ release signaling | ERLIN2, RNF170, IP3R/IP3R1 | ER membrane lipid raft-like microdomains; MAM-associated Ca2+ signaling domains | Foundational mechanistic literature summarized in reviews and disease papers; patient-genetic interpretation | In disease-oriented synthesis, unique ERLIN1 ablation was noted to increase IP3R1 levels by ~73% in vitro; disturbed IP3R degradation is proposed to impair Ca2+ signaling relevant to long-axon vulnerability | (cogan2024biallelicvariantsin pages 12-16, cogan2024biallelicvariantsin pages 1-6, veronese2024erlin12scaffoldsbridge pages 12-12, huang2021transcriptomeandliterature pages 9-11, huang2021transcriptomeandliterature pages 11-13) Cogan et al., 2024, https://doi.org/10.1007/s00439-024-02702-0; Veronese et al., 2024, https://doi.org/10.26508/lsa.202402620; Huang et al., 2021, https://doi.org/10.3390/biology10080755 |
| MAM lipid raft microdomains and autophagy initiation | ERLIN1 associates with AMBRA1 in ganglioside-rich raft-like MAM microdomains; this interaction supports starvation-induced autophagosome formation and couples ER-mitochondria membrane organization to autophagy initiation | AMBRA1, MFN2, GD3/ganglioside pathway components, BECN1 | Mitochondria-associated ER membranes (MAMs); raft-like microdomains enriched in cholesterol/gangliosides | Co-immunoprecipitation; FRET; knockdown of ERLIN1, MFN2, and GD3-synthase; autophagy assays | ERLIN1-AMBRA1 interaction increased with autophagy induction; depletion of ERLIN1 impaired nutrient-deprivation-induced autophagy; interaction depended on GD3 and MFN2 integrity | (manganelli2021roleoferlins pages 7-9, manganelli2021roleoferlins pages 1-2, manganelli2021roleoferlins pages 3-5) Manganelli et al., 2021, https://doi.org/10.3390/cells10092408; Manganelli et al., 2021, https://doi.org/10.1080/15548627.2020.1834207 |
| Hereditary spastic paraplegia SPG62 / patient genetics | Biallelic ERLIN1 variants disrupt splicing or the PHB/SPFH structural region, likely destabilizing ERLIN1/2 oligomers and perturbing IP3R ERAD/Ca2+ homeostasis in motor-system disease | ERLIN2; functionally linked RNF170 and IP3R1 | ER membrane complex in neurons and other cells | Human cohort genetics; RNA-seq/RT-PCR splice validation; structural modeling | Largest reported series: 13 individuals from 6 families; early onset mean 1.8 years (range 9 months-4 years); recurrent c.430+3_430+6del in 6 individuals from 4 families; thin corpus callosum in 5/13 (~40%); gait ataxia in 6/13; aid for walking typically needed 10-15 years after onset | (cogan2024biallelicvariantsin pages 18-27, cogan2024biallelicvariantsin pages 9-12, cogan2024biallelicvariantsin pages 12-16, cogan2024biallelicvariantsin pages 1-6, cogan2024biallelicvariantsin pages 6-9) Cogan et al., 2024, https://doi.org/10.1007/s00439-024-02702-0 |
| Viral infection biology (HCV host factor) | ERLIN1 is a positive host factor for efficient hepatitis C virus infection, acting after entry and primary translation to promote initiation of RNA replication and a later assembly-related step | HCV proteins/core, NS3, NS5A; lipid droplets; ERLIN2 was tested but not equivalent functionally | ER detergent-resistant membranes; cholesterol-rich ER microdomains | siRNA knockdown in Huh-7 cells; reporter replicons; pseudoparticle entry assays; infectivity titration; RT-qPCR; western blot; microscopy | ERLIN1 knockdown caused ~7-10-fold lower progeny virus production; ~2-3-fold lower intracellular HCV RNA in single-cycle infection; ~4-10-fold lower core/NS3/NS5A accumulation; ~50% lower reporter activity at 48-72 h and 30-60% of control at 96 h; no effect on entry or primary IRES translation | (whittenbauer2019thehostfactor pages 18-19, whittenbauer2019thehostfactor pages 9-12, whittenbauer2019thehostfactor pages 5-6, whittenbauer2019thehostfactor pages 6-9, whittenbauer2019thehostfactor pages 15-18, whittenbauer2019thehostfactor pages 12-15, whittenbauer2019thehostfactor pages 1-3) Whitten-Bauer et al., 2019, https://doi.org/10.3390/cells8121555 |
| Immune-cell modulation in sepsis | ERLIN1 is transcriptionally upregulated in sepsis-associated immune contexts, especially neutrophil-related settings, suggesting ER stress/proteostasis, Ca2+ signaling, and cholesterol-homeostasis roles in innate immune activation | Functionally linked RNF170, IP3R, SREBP-SCAP-INSIG axis; cell-context associations in neutrophils/monocytes/whole blood | Whole blood leukocytes; neutrophils; monocytes; HL60 neutrophil-like cells | Transcriptome mining across public datasets; RT-qPCR in stimulated whole blood; flow cytometry in leukocyte subsets and HL60 model | Public datasets showed 3.26-5.29-fold ERLIN1 increase overall; 5.29-fold increase in healthy neutrophils exposed to septic plasma; 2.6-fold increase in LPS/PGN-stimulated whole blood (p<0.01); additional examples included 1.34-fold in S. aureus infection, 1.18-fold in ICU sepsis, and 6.12-fold in neonatal sepsis; whole-blood donor experiment n=8; HL60 MFI fold changes 2.4, 1.06, and -2.36 at 6, 12, 24 h (n=3) | (huang2021transcriptomeandliterature pages 1-2, huang2021transcriptomeandliterature pages 9-11, huang2021transcriptomeandliterature pages 2-4, huang2021transcriptomeandliterature pages 7-9, huang2021transcriptomeandliterature pages 5-6, huang2021transcriptomeandliterature pages 11-13) Huang et al., 2021, https://doi.org/10.3390/biology10080755 |
Table: This table summarizes experimentally supported functions, pathways, interaction partners, localization, and disease relevance of human ERLIN1 (UniProt O75477). It highlights both foundational and recent studies, including 2024 work on ERLIN1/2 scaffolds in cholesterol homeostasis and secretory pathway regulation.
Veronese et al. provide a schematic model of the ERLIN1/2 scaffold bridging RNF170 and TMUB1-L at the ER membrane. (veronese2024erlin12scaffoldsbridge media 40d635ea)
The strongest 2023–2024 primary evidence obtained here is from two 2024 peer-reviewed studies: Veronese et al. (mechanistic cell biology) and Cogan et al. (clinical genetics). (veronese2024erlin12scaffoldsbridge pages 1-2, cogan2024biallelicvariantsin pages 1-6) Additional mechanistic context (autophagy/MAMs; infection biology; sepsis transcriptomics) is supported by 2019–2021 literature. (whittenbauer2019thehostfactor pages 1-3, manganelli2021roleoferlins pages 1-2, huang2021transcriptomeandliterature pages 1-2)
References
(manganelli2021roleoferlins pages 1-2): Valeria Manganelli, Agostina Longo, Vincenzo Mattei, Serena Recalchi, Gloria Riitano, Daniela Caissutti, Antonella Capozzi, Maurizio Sorice, Roberta Misasi, and Tina Garofalo. Role of erlins in the control of cell fate through lipid rafts. Cells, 10:2408, Sep 2021. URL: https://doi.org/10.3390/cells10092408, doi:10.3390/cells10092408. This article has 42 citations.
(manganelli2021roleoferlins pages 3-5): Valeria Manganelli, Agostina Longo, Vincenzo Mattei, Serena Recalchi, Gloria Riitano, Daniela Caissutti, Antonella Capozzi, Maurizio Sorice, Roberta Misasi, and Tina Garofalo. Role of erlins in the control of cell fate through lipid rafts. Cells, 10:2408, Sep 2021. URL: https://doi.org/10.3390/cells10092408, doi:10.3390/cells10092408. This article has 42 citations.
(veronese2024erlin12scaffoldsbridge pages 1-2): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge pages 4-6): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge pages 2-4): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge pages 12-12): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge media 40d635ea): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(cogan2024biallelicvariantsin pages 12-16): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(cogan2024biallelicvariantsin pages 1-6): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(manganelli2021roleoferlins pages 7-9): Valeria Manganelli, Agostina Longo, Vincenzo Mattei, Serena Recalchi, Gloria Riitano, Daniela Caissutti, Antonella Capozzi, Maurizio Sorice, Roberta Misasi, and Tina Garofalo. Role of erlins in the control of cell fate through lipid rafts. Cells, 10:2408, Sep 2021. URL: https://doi.org/10.3390/cells10092408, doi:10.3390/cells10092408. This article has 42 citations.
(cogan2024biallelicvariantsin pages 6-9): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(cogan2024biallelicvariantsin pages 9-12): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(cogan2024biallelicvariantsin pages 18-27): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(whittenbauer2019thehostfactor pages 5-6): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(whittenbauer2019thehostfactor pages 9-12): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(whittenbauer2019thehostfactor pages 15-18): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(whittenbauer2019thehostfactor pages 1-3): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(huang2021transcriptomeandliterature pages 1-2): Susie S. Y. Huang, Mohammed Toufiq, Luis R. Saraiva, Nicholas Van Panhuys, Damien Chaussabel, and Mathieu Garand. Transcriptome and literature mining highlight the differential expression of erlin1 in immune cells during sepsis. Biology, 10:755, Aug 2021. URL: https://doi.org/10.3390/biology10080755, doi:10.3390/biology10080755. This article has 8 citations.
(huang2021transcriptomeandliterature pages 7-9): Susie S. Y. Huang, Mohammed Toufiq, Luis R. Saraiva, Nicholas Van Panhuys, Damien Chaussabel, and Mathieu Garand. Transcriptome and literature mining highlight the differential expression of erlin1 in immune cells during sepsis. Biology, 10:755, Aug 2021. URL: https://doi.org/10.3390/biology10080755, doi:10.3390/biology10080755. This article has 8 citations.
(huang2021transcriptomeandliterature pages 9-11): Susie S. Y. Huang, Mohammed Toufiq, Luis R. Saraiva, Nicholas Van Panhuys, Damien Chaussabel, and Mathieu Garand. Transcriptome and literature mining highlight the differential expression of erlin1 in immune cells during sepsis. Biology, 10:755, Aug 2021. URL: https://doi.org/10.3390/biology10080755, doi:10.3390/biology10080755. This article has 8 citations.
(huang2021transcriptomeandliterature pages 5-6): Susie S. Y. Huang, Mohammed Toufiq, Luis R. Saraiva, Nicholas Van Panhuys, Damien Chaussabel, and Mathieu Garand. Transcriptome and literature mining highlight the differential expression of erlin1 in immune cells during sepsis. Biology, 10:755, Aug 2021. URL: https://doi.org/10.3390/biology10080755, doi:10.3390/biology10080755. This article has 8 citations.
(huang2021transcriptomeandliterature pages 11-13): Susie S. Y. Huang, Mohammed Toufiq, Luis R. Saraiva, Nicholas Van Panhuys, Damien Chaussabel, and Mathieu Garand. Transcriptome and literature mining highlight the differential expression of erlin1 in immune cells during sepsis. Biology, 10:755, Aug 2021. URL: https://doi.org/10.3390/biology10080755, doi:10.3390/biology10080755. This article has 8 citations.
(whittenbauer2019thehostfactor pages 18-19): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(whittenbauer2019thehostfactor pages 6-9): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(whittenbauer2019thehostfactor pages 12-15): Christina Whitten-Bauer, Josan Chung, Andoni Gómez-Moreno, Pilar Gomollón-Zueco, Michael D. Huber, Larry Gerace, and Urtzi Garaigorta. The host factor erlin-1 is required for efficient hepatitis c virus infection. Cells, 8:1555, Dec 2019. URL: https://doi.org/10.3390/cells8121555, doi:10.3390/cells8121555. This article has 9 citations.
(huang2021transcriptomeandliterature pages 2-4): Susie S. Y. Huang, Mohammed Toufiq, Luis R. Saraiva, Nicholas Van Panhuys, Damien Chaussabel, and Mathieu Garand. Transcriptome and literature mining highlight the differential expression of erlin1 in immune cells during sepsis. Biology, 10:755, Aug 2021. URL: https://doi.org/10.3390/biology10080755, doi:10.3390/biology10080755. This article has 8 citations.