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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The literature analyzed matches the UniProt target Q9H9K5, encoding the endogenous retroviral envelope protein HEMO, whose gene is ERVMER34-1 (synonym HEMO) in Homo sapiens. The defining primary reference explicitly identifies HEMO as a MER34-derived env gene at chromosome 4q12 and characterizes its Env-like features, placental expression, and shedding into maternal blood, aligning with the UniProt description (heidmann2017hemoanancestral pages 2-3, heidmann2017hemoanancestral pages 1-1).
ERVMER34-1 (HEMO) is a co-opted (domesticated) endogenous retroviral envelope (Env)-like gene. Unlike classical exogenous retroviral Env proteins that mediate viral entry and often require proteolytic processing into SU (surface) and TM (transmembrane) subunits, HEMO exhibits unusual processing dominated by ectodomain shedding rather than canonical SU–TM cleavage (heidmann2017hemoanancestral pages 4-4, heidmann2017hemoanancestral pages 2-3).
Heidmann et al. report HEMO as a 563-aa Env-like precursor with multiple canonical gamma-type Env hallmarks, including:
- N-terminal signal peptide (secretory pathway targeting) (heidmann2017hemoanancestral pages 2-3)
- SU-region motif (CWLC) (heidmann2017hemoanancestral pages 2-3)
- TM-region signatures, including an immunosuppressive-domain (ISD)-like segment and a C-X6-CC motif, plus a hydrophobic transmembrane segment and cytoplasmic tail (heidmann2017hemoanancestral pages 2-3)
However, key canonical fusogenic features are disrupted:
- The furin cleavage motif is mutated (CTQG instead of R-X-R/K-R) (heidmann2017hemoanancestral pages 2-3)
- An adjacent hydrophobic fusion peptide is absent, consistent with non-fusogenic behavior (heidmann2017hemoanancestral pages 2-3)
These sequence-level features frame current understanding: HEMO is Env-like, but likely not a classical membrane-fusion protein (heidmann2017hemoanancestral pages 8-9, heidmann2017hemoanancestral pages 2-3).
A central concept for HEMO is ectodomain shedding: HEMO is synthesized as a membrane-anchored precursor but is proteolytically cleaved upstream of the TM domain, releasing a soluble extracellular form (heidmann2017hemoanancestral pages 1-1, heidmann2017hemoanancestral pages 4-4). This differs from “simple secretion” of a protein that is never membrane anchored.
HEMO is made as an Env-like precursor but is predominantly observed as:
- A cell-associated full-length SU–TM form (~58 kDa), and
- A major shed/soluble form (~48 kDa) found in supernatants and in vivo samples (heidmann2017hemoanancestral pages 4-4, heidmann2017hemoanancestral pages 4-5).
Key processing details include:
- The mature shed form begins near residue 27 after signal peptide cleavage (heidmann2017hemoanancestral pages 4-4).
- Mass spectrometry mapped C-terminal truncation/cleavage mainly at Q432 and R433 (about 4:1 ratio), placing cleavage within/near the predicted ISD region (heidmann2017hemoanancestral pages 4-4).
- Membrane anchoring is required for efficient shedding: constructs truncated before the TM are not shed efficiently (heidmann2017hemoanancestral pages 4-4).
- Shedding is consistent with metalloproteinase-mediated processing and is inhibited by broad-spectrum ADAM/MMP inhibitors (Batimastat, Marimastat, GM6001; dose range shown ~0.1–10 μM) in transfected cells (heidmann2017hemoanancestral pages 4-5, heidmann2017hemoanancestral pages 8-9).
These biochemical observations are directly supported by Western blot and cleavage-mapping figure evidence (heidmann2017hemoanancestral media 5d20d2f9).
Placenta and pregnancy circulation are the most firmly established physiological contexts:
- In first-trimester placenta, immunohistochemistry shows strongest staining in villous cytotrophoblasts (CT) and extravillous trophoblasts (EVT), with more diffuse syncytiotrophoblast staining, consistent with release toward maternal circulation (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral media 5d20d2f9).
- HEMO is detected in placental blood and in peripheral blood of pregnant women, reflecting its shed extracellular form (heidmann2017hemoanancestral pages 4-4, heidmann2017hemoanancestral pages 4-5).
A 2023 placental ERV review independently reiterates that ERVMER34-1/HEMO is expressed in CT and EVT in early gestation and is detectable in blood of pregnant females, and notes it has no fusion activity (shimode2023acquisitionandexaptation pages 6-7).
Early embryo and pluripotent cells: HEMO expression is also linked to “stemness” contexts:
- RNA-seq analyses indicate expression from the eight-cell to blastocyst stage and maintenance in derived ESCs (passages 0–10) (heidmann2017hemoanancestral pages 5-6).
- During reprogramming of CD34+ cells to iPSCs, HEMO is upregulated in parallel with OCT4, and the ~48 kDa shed protein is detected in iPSC supernatants (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 6-7).
Other normal tissues: qRT-PCR across a tissue panel suggests placenta-dominant expression and limited expression outside placenta, particularly kidney (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 2-3).
In the retrieved evidence set, there is no direct demonstration for HEMO of:
- A specific host receptor or binding partner mediating signaling (HEMO is contrasted with other Env-derived proteins like Suppressyn that bind ASCT2) (shimode2023acquisitionandexaptation pages 6-7).
- A validated signal transduction pathway triggered by HEMO.
- Direct, HEMO-specific immunosuppressive activity in vitro or in vivo.
Thus, current annotation should emphasize processing/localization/expression as primary experimentally supported properties, with function remaining an open question (heidmann2017hemoanancestral pages 8-9, shimode2023acquisitionandexaptation pages 6-7).
A 2023 review of ERV exaptation in placenta places ERVMER34-1/HEMO among multiple ERV env-derived proteins expressed in trophoblast lineages, reiterating: early-gestation CT/EVT expression, blood detectability, and lack of fusion activity, and proposes a possible anti-fusion role based on localization similarity to Suppressyn (shimode2023acquisitionandexaptation pages 6-7).
- Publication (review): Shimode, Biomolecules (Oct 2023). URL: https://doi.org/10.3390/biom13101482 (shimode2023acquisitionandexaptation pages 6-7)
A 2024 ribosome profiling study emphasizes that the protein-coding capacity of HERVs remains incompletely characterized and cites HEMO as an example of an ERV envelope protein expressed in placenta/pluripotent cells/tumors and detectable in blood (via the 2017 PNAS study) (dopkins2024ribosomalprofilingof pages 7-7).
- Publication: Dopkins et al., BMC Genomics (Jan 2024). URL: https://doi.org/10.1186/s12864-023-09909-x (dopkins2024ribosomalprofilingof pages 7-7)
HEMO is detectable in maternal blood and rises during gestation, with an estimated peak concentration in the 1–10 nM range, supporting feasibility as a pregnancy-associated circulating biomarker (though clinical sensitivity/specificity and disease stratification were not provided in the extracted evidence) (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 4-5).
Primary data (2017): HEMO shows heterogeneous transcript expression across tumors, with particularly notable findings in ovarian cancer, where expression is histotype-dependent and HEMO protein is detected by IHC in clear cell ovarian carcinoma (heidmann2017hemoanancestral pages 5-6).
Recent synthesis (2023 review): A comprehensive 2023 HERV–cancer review describes ERVMER34-1/HEMO as:
- Inducible by γ-radiation in head and neck squamous cell carcinoma (HNSCC) cell lines, suggested as a potential target to overcome radioresistance, and
- “Hailed as a pan-cancer target” across many solid tumors and leukemias (review-level claim) (stricker2023hervsandcancer—a pages 28-29).
This reflects a shift toward considering HERV-derived proteins as immunotherapy targets, but the review also notes that clinical validation remains limited (stricker2023hervsandcancer—a pages 28-29).
- Publication: Stricker et al., Biomedicines (Mar 2023). URL: https://doi.org/10.3390/biomedicines11030936 (stricker2023hervsandcancer—a pages 28-29)
The broader cancer immunology literature summarized in 2023–2024 sources supports that HERV-derived peptides can be presented on HLA and recognized by T cells, motivating interest in HERV proteins (including HEMO) as tumor antigens (stricker2023hervsandcancer—a pages 28-29, dopkins2024ribosomalprofilingof pages 7-7). However, direct evidence of successful HEMO-targeted immunotherapy was not present in the retrieved excerpts (dopkins2024ribosomalprofilingof pages 7-7).
A key mechanistic insight is that HEMO is unusual among ERV-derived genes in being transcribed from a CpG-rich, non-LTR promoter:
- Transcript start site mapped by RACE to a CpG-rich region (heidmann2017hemoanancestral pages 2-3).
- A ~760 bp promoter fragment drove >500-fold luciferase activity (heidmann2017hemoanancestral pages 2-3).
- DNA methylation status correlated with expression across cell lines and could be derepressed by 5-Aza-dC (heidmann2017hemoanancestral pages 2-3).
This supports an annotation of ERVMER34-1 as an ERV-derived coding sequence under host-like promoter regulation, including epigenetic control.
Heidmann et al. infer that capture/retention of the HEMO locus likely occurred >100 million years ago, before the Laurasiatheria–Euarchontoglires split, with purifying selection maintaining a full-length ORF in simians and conserved shedding capacity (heidmann2017hemoanancestral pages 1-1, heidmann2017hemoanancestral pages 8-8). The paper frames HEMO as a rare example of a very ancient env-derived ORF that remains functional in expression and processing (heidmann2017hemoanancestral pages 1-1).
The following table compiles the most important evidence-backed points (structure, processing, expression, and applications) with quantitative details and source URLs:
| Aspect | Key findings | Evidence type/method | Source |
|---|---|---|---|
| Identity | ERVMER34-1 encodes HEMO, a human endogenous MER34 Env-like protein from the MER34 locus on chromosome 4q12; literature consistently maps HEMO to the human ERVMER34-1 gene/protein corresponding to UniProt Q9H9K5. | Primary gene/protein characterization; locus mapping; comparative annotation | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 1-1, heidmann2017hemoanancestral pages 2-3) |
| Structure/domains | HEMO is a 563-aa Env-like precursor with an N-terminal signal peptide; SU contains a CWLC motif; TM contains an immunosuppressive-domain-like region, a C-X6-CC motif, a 23-aa hydrophobic transmembrane domain, and a C-terminal cytoplasmic tail. The canonical furin cleavage motif is mutated to CTQG, and an adjacent hydrophobic fusion peptide is absent. | Sequence/domain analysis from primary paper | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 2-3) |
| Processing/shedding | HEMO is synthesized as a classical Env precursor; the mature shed form begins at residue 27 after signal peptide cleavage. A major secreted glycosylated species runs at ~48 kDa; MS mapped C-terminal truncation/cleavage mainly at Q432 and R433 (about 4:1 ratio). Full-length SU-TM is ~58 kDa and mainly cell-associated. Efficient shedding requires membrane anchoring; mutants truncated before the TM are not shed. A furin-engineered mutant (H-fur+) yields a smaller ~37-kDa SU-like product. | Transient transfection, Western blot, PNGase F deglycosylation, mass spectrometry, mutagenesis | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 4-4, heidmann2017hemoanancestral pages 8-9, heidmann2017hemoanancestral media 5d20d2f9) |
| Localization | HEMO is extracellularly shed and detectable in placental blood and maternal circulation during pregnancy. In first-trimester placenta, immunostaining is strongest in villous cytotrophoblasts (CTs) and extravillous trophoblasts (EVTs), with more diffuse syncytiotrophoblast staining, consistent with release toward maternal blood. | Immunohistochemistry, WGA enrichment, Western blot of placental blood/tissue | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 4-4, heidmann2017hemoanancestral media 5d20d2f9); Shimode, 2023, Biomolecules, doi: https://doi.org/10.3390/biom13101482 (shimode2023acquisitionandexaptation pages 6-7) |
| Expression (placenta) | Placenta is the dominant normal expression site. qRT-PCR across 20 tissues and 16 cell lines used placenta values as means from 12 first-trimester placentas; RNA-seq also showed significant placental expression with limited normal-tissue expression outside placenta, especially kidney. Placental samples analyzed included first-trimester tissues at 8–12 weeks gestation. | qRT-PCR, RNA-seq reanalysis, RACE, placental tissue profiling | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 2-3, heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 8-9) |
| Expression (embryo/ESC/iPSC) | HEMO is expressed from the eight-cell stage through blastocyst and maintained in derived ESCs (reported across passages 0–10). It is reactivated during CD34+ cell reprogramming to iPSCs in parallel with OCT4; a shed ~48-kDa HEMO band is detectable in iPSC supernatants. RNA-seq panels included 124 single-cell embryo/ESC samples and 28 reprogramming/iPSC-related samples. | Single-cell and bulk RNA-seq analyses; Western blot of iPSC supernatants | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 6-7) |
| Maternal blood abundance | HEMO is present at low levels in men and nonpregnant women but rises during gestation; peak concentration in pregnant blood was estimated at ~1–10 nM, approximately 1–2 orders of magnitude below peak hCG. | Comparative Western blot quantification of sera/plasma | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral media 5d20d2f9, heidmann2017hemoanancestral pages 4-5) |
| Tumor associations | Transcriptome screens found heterogeneous tumor expression with high-level signals in germ-line, liver, lung, breast, and ovary tumors. In ovarian cancer, expression showed histotype dependence: elevated in clear-cell carcinoma (n=60) and endometrioid cancers (n=96), but not clearly in serous (n=289) or mucinous (n=34) histotypes. HEMO protein was detected by IHC in clear-cell ovarian tumor cells. Dataset summaries included 1,033 normal and 2,315 neoplasm samples, plus 479 additional tumor samples. | Microarray/RNA-seq meta-analysis; ovarian tumor immunohistochemistry | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 5-6, heidmann2017hemoanancestral pages 1-1) |
| Regulatory mechanisms | Unlike many ERV genes, HEMO is transcribed from a non-LTR CpG-rich promoter. A 760-bp fragment around the start site showed strong promoter activity (>500-fold) in luciferase assays. CpG methylation inversely correlated with expression (methylated in 293T and BeWo; unmethylated in iPSC and CaCo-2), and 5-Aza-dC treatment derepressed transcription. | RACE-PCR, promoter luciferase assays, bisulfite methylation mapping, pharmacologic demethylation | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 2-3) |
| Evolutionary features | HEMO is described as the oldest captured full-length env in humans, with capture likely >100 Mya before the Laurasiatheria–Euarchontoglires split. The locus is highly degenerate as a provirus (no clear 5' LTR, truncated 3' LTR, degenerate pol), yet the env ORF is preserved in simians under purifying selection and retains shedding capacity. | Comparative genomics, synteny, phylogeny, selection analysis | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 1-1, heidmann2017hemoanancestral pages 2-3, heidmann2017hemoanancestral pages 8-8); Johnson, 2019, Nat Rev Microbiol, doi: https://doi.org/10.1038/s41579-019-0189-2 (timpona2018vsvvectorsas pages 38-43) |
| Hypothesized function | Direct function remains unresolved. Experimental evidence indicates HEMO has no detectable fusogenic activity. Because it localizes similarly to ERVH48-1/Suppressyn in CTs and EVTs and is shed into maternal blood, reviews have suggested it may act as a cell-fusion inhibitor or other secreted placental factor, but this remains hypothetical. No direct receptor-binding or immunosuppression assay for HEMO was reported in the cited contexts. | Negative functional assay for fusion; comparative interpretation in recent reviews | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 8-9, timpona2018vsvvectorsas pages 38-43); Shimode, 2023, Biomolecules, doi: https://doi.org/10.3390/biom13101482 (shimode2023acquisitionandexaptation pages 6-7) |
| Shedding mechanism | Shedding resembles proteolytic ectodomain release seen for some viral Env proteins and was inhibited dose-dependently in transfected cells by broad-spectrum ADAM/MMP inhibitors (Batimastat, Marimastat, GM6001; shown across ~0.1–10 µM), supporting metalloproteinase-mediated processing at the cell surface. | Inhibitor perturbation in transfected cells; Western blot readout | Heidmann et al., 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702204114 (heidmann2017hemoanancestral pages 8-9, heidmann2017hemoanancestral pages 4-5) |
Table: This table compiles evidence-backed findings for human ERVMER34-1/HEMO, including identity, structure, shedding, localization, expression, tumor associations, regulation, and proposed function. It highlights key quantitative details and the methods supporting each claim.
References
(heidmann2017hemoanancestral pages 2-3): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(heidmann2017hemoanancestral pages 1-1): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(heidmann2017hemoanancestral pages 4-4): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(heidmann2017hemoanancestral pages 8-9): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(heidmann2017hemoanancestral pages 4-5): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(heidmann2017hemoanancestral media 5d20d2f9): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(heidmann2017hemoanancestral pages 5-6): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(shimode2023acquisitionandexaptation pages 6-7): Sayumi Shimode. Acquisition and exaptation of endogenous retroviruses in mammalian placenta. Biomolecules, 13:1482, Oct 2023. URL: https://doi.org/10.3390/biom13101482, doi:10.3390/biom13101482. This article has 15 citations.
(heidmann2017hemoanancestral pages 6-7): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(denner2026retrovirusinducedimmunosuppressiona pages 14-16): Joachim Denner. Retrovirus-induced immunosuppression: a comprehensive review. Unknown journal, May 2026. URL: https://doi.org/10.20944/preprints202605.0768.v1, doi:10.20944/preprints202605.0768.v1.
(dopkins2024ribosomalprofilingof pages 7-7): Nicholas Dopkins, Bhavya Singh, Stephanie Michael, Panpan Zhang, Jez L. Marston, Tongyi Fei, Manvendra Singh, Cedric Feschotte, Nicholas Collins, Matthew L. Bendall, and Douglas F. Nixon. Ribosomal profiling of human endogenous retroviruses in healthy tissues. BMC Genomics, Jan 2024. URL: https://doi.org/10.1186/s12864-023-09909-x, doi:10.1186/s12864-023-09909-x. This article has 13 citations and is from a peer-reviewed journal.
(stricker2023hervsandcancer—a pages 28-29): Erik Stricker, Erin C. Peckham-Gregory, and Michael E. Scheurer. Hervs and cancer—a comprehensive review of the relationship of human endogenous retroviruses and human cancers. Biomedicines, 11:936, Mar 2023. URL: https://doi.org/10.3390/biomedicines11030936, doi:10.3390/biomedicines11030936. This article has 58 citations.
(heidmann2017hemoanancestral pages 8-8): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.
(timpona2018vsvvectorsas pages 38-43): J Timpona. Vsv vectors as vaccines for emerging viruses and as probes for entry pathways. Unknown journal, 2018.
(heidmann2017hemoanancestral media 5246bf31): Odile Heidmann, Anthony Béguin, Janio Paternina, Raphaël Berthier, Marc Deloger, Olivia Bawa, and Thierry Heidmann. Hemo, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proceedings of the National Academy of Sciences, 114:E6642-E6651, Jul 2017. URL: https://doi.org/10.1073/pnas.1702204114, doi:10.1073/pnas.1702204114. This article has 92 citations and is from a highest quality peer-reviewed journal.