Affinage

MOAP1

Modulator of apoptosis 1 · UniProt Q96BY2

Length
351 aa
Mass
39.5 kDa
Annotated
2026-04-28
59 papers in source corpus 15 papers cited in narrative 15 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MOAP-1 (PNMA4) is a short-lived, mitochondria-enriched effector of intrinsic apoptosis, autophagy, and innate antiviral signaling, whose cellular levels are tightly controlled by ubiquitin-mediated degradation. Under basal conditions, MOAP-1 is constitutively polyubiquitinated and degraded via the proteasome by the E3 ligases APC/C(Cdh1) and UBR5, whereas apoptotic stimuli inhibit its ubiquitination—an effect reinforced by the stabilizing E3 ligase TRIM39—leading to MOAP-1 accumulation at mitochondria, where it directly associates with Bax (through a BH3-like domain), drives Bax conformational change and mitochondrial insertion, promotes tBid recruitment via MTCH2, and triggers cytochrome c release and caspase activation (PMID:11060313, PMID:16199525, PMID:17535899, PMID:22529100, PMID:27721409, PMID:19100260, PMID:27320914). RASSF1A, recruited to death-receptor complexes upon TNFα/TRAIL stimulation, relieves an intramolecular autoinhibition in MOAP-1 to license Bax binding, and activated K-Ras synergizes with this pathway (PMID:15949439, PMID:16344548). Beyond apoptosis, MOAP-1 binds LC3 through an N-terminal LIR motif to promote phagophore closure during starvation-induced autophagy (PMID:33783314), and enhances RIG-I–MAVS antiviral signaling by facilitating TRIM25-mediated K63-ubiquitination of RIG-I, as demonstrated by increased susceptibility of PNMA4-knockout mice to RNA virus infection (PMID:40929959).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2000 High

    Identification of MOAP-1 as a Bax-associating protein with a BH3-like domain established it as a candidate apoptosis regulator, resolving the question of how Bax is engaged by a novel cofactor.

    Evidence Yeast two-hybrid screen, reciprocal Co-IP, mutagenesis of BH3-like domain and Bax BH domains in mammalian cells

    PMID:11060313

    Open questions at the time
    • Physiological context of interaction unknown—Bax binding was constitutive in overexpression systems
    • No subcellular localization data for endogenous MOAP-1
    • Mechanism linking MOAP-1/Bax binding to downstream apoptosis undefined
  2. 2005 High

    Demonstration that MOAP-1 is mitochondria-enriched, required for Bax conformational change and translocation, and that its loss phenocopies Bax deficiency in anchorage-independent growth, established MOAP-1 as a necessary upstream activator of Bax in the intrinsic apoptotic pathway.

    Evidence siRNA knockdown, subcellular fractionation, isolated mitochondria cytochrome c release assay in HCT116 cells

    PMID:16199525

    Open questions at the time
    • How apoptotic signals trigger the MOAP-1/Bax interaction remained unclear
    • No in vivo model
  3. 2005 High

    Discovery that RASSF1A, recruited to TNFα/TRAIL receptor complexes, relieves an autoinhibitory interaction within MOAP-1 to enable Bax binding resolved how death-receptor signals are transduced through MOAP-1 to mitochondria, with activated K-Ras synergizing with RASSF1A.

    Evidence Co-IP, shRNA knockdown of RASSF1A and MOAP-1, Bax conformational change and cytochrome c release assays; mutagenesis of RASSF1A tumor-derived mutant

    PMID:15949439 PMID:16344548

    Open questions at the time
    • Structural basis of the intramolecular autoinhibition not defined
    • Contribution of K-Ras effector pathway to RASSF1A–MOAP-1 axis not fully dissected
  4. 2007 High

    Showing that MOAP-1 is an extremely short-lived protein (t½ ~25 min) whose polyubiquitination is inhibited by apoptotic stimuli revealed a post-translational stabilization mechanism as the primary mode of MOAP-1 regulation.

    Evidence Cycloheximide chase, in vivo ubiquitination assay, isolated mitochondria reconstitution with in vitro-translated MOAP-1

    PMID:17535899

    Open questions at the time
    • Identity of the responsible E3 ligase(s) was unknown
    • Signal that blocks polyubiquitination was uncharacterized
  5. 2008 High

    Identification of TRIM39 as a stabilizer of MOAP-1 that inhibits its polyubiquitination answered how MOAP-1 escapes constitutive degradation to accumulate at mitochondria and promote Bax-dependent apoptosis.

    Evidence Co-IP, ubiquitination assay, cycloheximide chase, isolated mitochondria cytochrome c release, siRNA knockdown

    PMID:19100260

    Open questions at the time
    • Mechanism by which TRIM39 (itself a RING E3) inhibits rather than promotes ubiquitination was unclear
    • Identity of the E3 ligase degrading MOAP-1 still unknown
  6. 2012 High

    Identification of APC/C(Cdh1) as the E3 ligase that ubiquitylates MOAP-1, and demonstration that TRIM39 directly inhibits APC/C(Cdh1) activity toward MOAP-1, resolved the constitutive degradation pathway and the mechanism of TRIM39-mediated stabilization.

    Evidence In vitro ubiquitylation assay with purified APC/C(Cdh1), Cdh1 siRNA stabilizing MOAP-1, Bax activation assay

    PMID:22529100

    Open questions at the time
    • Whether additional E3 ligases contribute to MOAP-1 turnover was unresolved
    • Degron motif on MOAP-1 recognized by APC/C(Cdh1) not mapped
  7. 2016 High

    Identification of UBR5/Dyrk2 as a second E3-kinase axis that ubiquitylates and degrades MOAP-1 revealed a parallel degradation pathway and showed that UBR5 loss sensitizes cisplatin-resistant cancer cells to apoptosis through MOAP-1 accumulation.

    Evidence In vitro ubiquitylation reconstitution, Co-IP, siRNA of UBR5 in ovarian cancer cells

    PMID:27721409

    Open questions at the time
    • Whether APC/C(Cdh1) and UBR5 act redundantly or in distinct cell-cycle phases was not determined
    • Dyrk2 phosphorylation site on MOAP-1 not mapped
  8. 2016 High

    Using MOAP-1 knockout mice, MOAP-1 was shown to be required in vivo for Fas-induced hepatocellular apoptosis and to facilitate tBid recruitment to mitochondria via the outer membrane protein MTCH2, expanding its role beyond direct Bax activation.

    Evidence MOAP-1 knockout mouse, Fas agonist antibody injection, Co-IP identifying MOAP-1–MTCH2 interaction, mitochondrial fractionation

    PMID:27320914

    Open questions at the time
    • Whether MOAP-1–MTCH2 interaction is independent of MOAP-1–Bax interaction was unclear
    • Role in tissues other than liver not characterized in vivo
  9. 2021 High

    Discovery that MOAP-1 binds LC3 through an N-terminal LIR motif and is required for phagophore closure during autophagy established a function for MOAP-1 beyond apoptosis.

    Evidence MOAP-1 knockout cells, Halo-LC3 autophagosome completion assay, proteinase K protection assay, LIR mutant rescue

    PMID:33783314

    Open questions at the time
    • Mechanistic basis of how LC3 binding promotes membrane closure not defined
    • Whether the autophagy function is connected to or independent of Bax-binding activity
  10. 2021 High

    Crystal structure determination confirmed MOAP-1 as a domesticated retroviral Gag-derived protein with a capsid-like fold, providing the first structural framework for understanding its protein interactions.

    Evidence X-ray crystallography of a stably folded domain, structural comparison to retroviral CA domains

    PMID:34357660

    Open questions at the time
    • No structure of MOAP-1 in complex with Bax, RASSF1A, or LC3
    • Functional significance of the Gag-like fold for its apoptotic or autophagic activities not tested
  11. 2025 High

    Identification of MOAP-1/PNMA4 as a MAVS-interacting protein that enhances RIG-I K63-ubiquitination by TRIM25 and is required for antiviral immunity in vivo extended its functions to innate immune signaling.

    Evidence BioID proximity labeling, Co-IP, K63-ubiquitination assay, Pnma4 knockout mouse RNA virus infection model

    PMID:40929959

    Open questions at the time
    • Whether the RIG-I signaling function depends on the same protein domains as apoptosis/autophagy is unknown
    • How MOAP-1 facilitates TRIM25 access to RIG-I mechanistically is not resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis of MOAP-1 autoinhibition and its relief by RASSF1A, the relationship between the Gag-like capsid fold and membrane-remodeling functions in apoptosis and autophagy, and whether the apoptotic, autophagic, and antiviral roles of MOAP-1 are coordinated or independently regulated.
  • No structure of MOAP-1 in an autoinhibited versus activated conformation
  • Functional integration of apoptosis, autophagy, and innate immunity roles not tested
  • Post-translational regulation (ubiquitination, phosphorylation) of MOAP-1 in contexts beyond apoptosis is largely unexplored

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4
Localization
GO:0005739 mitochondrion 5
Pathway
R-HSA-5357801 Programmed Cell Death 9 R-HSA-168256 Immune System 1 R-HSA-9612973 Autophagy 1
Partners
BAXMAVSMTCH2RACK1RASSF1ATRIM25TRIM39UBR5
Complex memberships
MOAP-1–Bax complexRASSF1A–MOAP-1 complex

Evidence

Reading pass · 15 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 MOAP-1 (MAP-1, Modulator of Apoptosis) was identified as a Bax-associating protein containing a BH3-like motif. It homodimerizes and associates with proapoptotic Bax and prosurvival Bcl-2/Bcl-XL in vitro and in vivo. The BH3-like domain is required for Bax association and apoptosis induction but not for Bcl-XL binding. Bax binding requires all three BH domains (BH1, BH2, BH3) of Bax. Yeast two-hybrid screen, Co-IP, in vitro binding assays, mutagenesis The Journal of biological chemistry High 11060313
2005 MOAP-1 is a mitochondria-enriched protein that associates with Bax only upon apoptotic induction, coinciding with cytochrome c release. siRNA-mediated knockdown of MOAP-1 selectively inhibits Bax-mediated apoptosis, blocks Bax conformational change and translocation, and impairs recombinant Bax- or tBid-mediated cytochrome c release from isolated mitochondria. MOAP-1-deficient cells show aggressive anchorage-independent growth similar to Bax-deficient cells. siRNA knockdown, subcellular fractionation, isolated mitochondria cytochrome c release assay, anchorage-independent growth assay Proceedings of the National Academy of Sciences of the United States of America High 16199525
2005 RASSF1A is required for death receptor (TNFα/TRAIL)-induced Bax conformational change and apoptosis. TNFα or TRAIL stimulation recruits RASSF1A and MOAP-1 to receptor complexes and promotes RASSF1A/MOAP-1 complex formation. RASSF1A binding to MOAP-1 relieves an intramolecular inhibitory interaction in MOAP-1, enabling MOAP-1 to associate with Bax and trigger Bax conformational change, mitochondrial membrane insertion, and cytochrome c release. Co-IP, shRNA knockdown, Bax conformational change assay, cytochrome c release assay Molecular cell High 15949439
2005 RASSF1A and MOAP-1 interact directly, and this interaction is enhanced by activated K-Ras. RASSF1A activates Bax via MOAP-1, and activated K-Ras, RASSF1A, and MOAP-1 synergize to induce Bax activation and cell death. A tumor-derived RASSF1A point mutant defective for MOAP-1 interaction fails to activate Bax. Co-IP, pulldown, shRNA knockdown, Bax activation assay, mutagenesis The Journal of biological chemistry High 16344548
2007 MOAP-1 is a short-lived protein (t1/2 ~25 min) constitutively degraded by the ubiquitin-proteasome system. Apoptotic stimuli rapidly upregulate MOAP-1 by inhibiting its polyubiquitination. Elevated MOAP-1 promotes recombinant Bax-mediated cytochrome c release from isolated mitochondria, and in vitro-translated MOAP-1 can restore Bax-mediated cytochrome c release in mitochondria depleted of short-lived proteins. Cycloheximide chase, ubiquitination assay, isolated mitochondria cytochrome c release assay, in vitro translation Proceedings of the National Academy of Sciences of the United States of America High 17535899
2008 TRIM39 was identified as a MOAP-1-binding protein that stabilizes MOAP-1 by inhibiting its polyubiquitination. TRIM39 overexpression extends MOAP-1 half-life, elevates MOAP-1 in mitochondria, and promotes cytochrome c release from isolated mitochondria stimulated by recombinant Bax. TRIM39 knockdown reduces sensitivity to etoposide-induced apoptosis. Co-IP, ubiquitination assay, cycloheximide chase, isolated mitochondria cytochrome c release assay, siRNA knockdown Experimental cell research High 19100260
2012 MOAP-1 is a substrate of the APC/C(Cdh1) ubiquitin ligase. TRIM39, a RING domain E3 ligase, directly inhibits APC/C(Cdh1)-mediated ubiquitylation of MOAP-1 (not just competing for substrate), thereby stabilizing MOAP-1. Cdh1 siRNA knockdown stabilizes MOAP-1 and enhances etoposide-induced Bax activation and apoptosis. In vitro ubiquitylation assay, siRNA knockdown of Cdh1, Co-IP, Bax activation assay The Journal of cell biology High 22529100
2012 miR-1228 targets MOAP-1 mRNA, reduces MOAP-1 protein expression, and delays stress-induced apoptosis. Rescue experiments showed that miR-1228 inhibition of apoptosis is attenuated by repressing MOAP-1 expression, establishing MOAP-1 as a direct target. miRNA overexpression, siRNA, apoptosis assays Apoptosis : an international journal on programmed cell death Medium 22434376
2016 UBR5, a HECT family E3 ubiquitin ligase, physically interacts with MOAP-1, ubiquitylates MOAP-1 in vitro, and destabilizes MOAP-1 in cultured cells. Dyrk2 kinase cooperates with UBR5 in mediating MOAP-1 ubiquitylation. UBR5 knockdown increases MOAP-1 levels, enhances Bax activation, and sensitizes cisplatin-resistant ovarian cancer cells to apoptosis. Co-IP, in vitro ubiquitylation assay, siRNA knockdown, Bax activation assay Oncogene High 27721409
2016 MOAP-1-deficient mice are resistant to Fas-induced hepatocellular apoptosis and lethality. MOAP-1 facilitates tBid recruitment to mitochondria by binding to the outer mitochondrial membrane protein MTCH2; in MOAP-1-deficient cells, MTCH2 fails to engage tBid, impairing tBid mitochondrial accumulation and downstream Bax/Bak activation. MOAP-1 knockout mouse model, Co-IP, mitochondrial fractionation, Fas-induced apoptosis assay Cell reports High 27320914
2018 RACK1 associates with MOAP-1 via electrostatic interactions (similar to MOAP-1/RASSF1A and MOAP-1/TNF-R1 interactions) and recruits the E3 ligase TRAF2 to MOAP-1, resulting in K63-linked ubiquitination of MOAP-1. Co-IP, ubiquitination assay (K63-linkage specific) Biochimica et biophysica acta. Molecular cell research Medium 29470995
2021 MOAP-1 binds LC3 via an LC3-interacting region (LIR) motif at its N-terminus and promotes phagophore closure during starvation-induced autophagy. MOAP-1-deficient cells show impaired autophagy with predominantly unclosed phagophores rather than closed autophagosomes upon EBSS treatment. Re-expression of wild-type MOAP-1 but not LIR-mutant MOAP-1 restores autophagy, demonstrating that LC3 binding is required for this function. MOAP-1 knockout cells, Halo-tagged LC3 autophagosome completion assay, Co-IP, proteinase K protection assay, mutagenesis of LIR motif Autophagy High 33783314
2021 X-ray crystal structures of a stably folded domain of MOAP-1 show high structural similarity to the C-terminal capsid (CA) domain of retroviral Gag proteins, confirming MOAP-1 as a domesticated Gag-derived protein. X-ray crystallography, structural comparison Proteins High 34357660
2021 Influenza A virus PB1-F2 protein interacts with human MOAP-1, as demonstrated by yeast two-hybrid, GST pulldown, and Co-IP assays. PB1-F2 upregulates exogenous MOAP-1 protein levels. Yeast two-hybrid, GST pulldown, Co-IP, Western blot Wei sheng wu xue bao = Acta microbiologica Sinica Medium 23236846
2025 PNMA4/MOAP-1 was identified as a MAVS-interacting protein at the mitochondria using proximity-based labeling. PNMA4 enhances RIG-I–MAVS interaction and facilitates K63-linked polyubiquitination of RIG-I at K657 by TRIM25, positively regulating antiviral signaling. PNMA4-knockout mice are more susceptible to RNA virus infection. Proximity-based labeling (BioID), Co-IP, ubiquitination assay, Pnma4 knockout mouse infection model International immunopharmacology High 40929959

Source papers

Stage 0 corpus · 59 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 The bZIP transcription factor MoAP1 mediates the oxidative stress response and is critical for pathogenicity of the rice blast fungus Magnaporthe oryzae. PLoS pathogens 246 21383978
1984 Widespread distribution of the major polypeptide component of MAP 1 (microtubule-associated protein 1) in the nervous system. The Journal of cell biology 241 6368569
2005 The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death. Molecular cell 148 15949439
1983 Low molecular weight microtubule-associated proteins are light chains of microtubule-associated protein 1 (MAP 1). Proceedings of the National Academy of Sciences of the United States of America 133 6572393
2005 The RASSF1A tumor suppressor activates Bax via MOAP-1. The Journal of biological chemistry 118 16344548
2000 MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains. The Journal of biological chemistry 118 11060313
2005 MAP-1 is a mitochondrial effector of Bax. Proceedings of the National Academy of Sciences of the United States of America 100 16199525
1985 Microtubule-associated proteins (MAPs): a monoclonal antibody to MAP 1 decorates microtubules in vitro but stains stress fibers and not microtubules in vivo. Proceedings of the National Academy of Sciences of the United States of America 82 3883359
1988 Estramustine binds a MAP-1-like protein to inhibit microtubule assembly in vitro and disrupt microtubule organization in DU 145 cells. The Journal of cell biology 81 3060470
1984 Widespread occurrence of polypeptides related to neurotubule-associated proteins (MAP-1 and MAP-2) in non-neuronal cells and tissues. The EMBO journal 68 6376120
1983 Differential distribution of microtubule-associated proteins MAP-1 and MAP-2 in neurons of rat brain and association of MAP-1 with microtubules of neuroblastoma cells (clone N2A). The EMBO journal 62 6641705
2016 Downregulation of the proapoptotic protein MOAP-1 by the UBR5 ubiquitin ligase and its role in ovarian cancer resistance to cisplatin. Oncogene 58 27721409
1987 18 kDa microtubule-associated protein: identification as a new light chain (LC-3) of microtubule-associated protein 1 (MAP-1). FEBS letters 56 3803603
2012 The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1. The Journal of cell biology 54 22529100
2007 Inhibition of ubiquitin-mediated degradation of MOAP-1 by apoptotic stimuli promotes Bax function in mitochondria. Proceedings of the National Academy of Sciences of the United States of America 54 17535899
2008 TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. Experimental cell research 48 19100260
1985 Microheterogeneity of microtubule-associated proteins, MAP-1 and MAP-2, and differential phosphorylation of individual subcomponents. The Journal of biological chemistry 46 2985613
2022 Polystyrene micro(nano)plastics damage the organelles of RBL-2H3 cells and promote MOAP-1 to induce apoptosis. Journal of hazardous materials 39 35999725
2019 Host-Induced Gene Silencing of MoAP1 Confers Broad-Spectrum Resistance to Magnaporthe oryzae. Frontiers in plant science 39 31024598
2016 The thioredoxin MoTrx2 protein mediates reactive oxygen species (ROS) balance and controls pathogenicity as a target of the transcription factor MoAP1 in Magnaporthe oryzae. Molecular plant pathology 38 27560036
1986 Identification of a 34-kD polypeptide as a light chain of microtubule-associated protein-1 (MAP-1) and its association with a MAP-1 peptide that binds to microtubules. The Journal of cell biology 32 3512577
1985 Expression of microtubule-associated proteins, MAP-1 and MAP-2, in human neuroblastomas and differential diagnosis of immature neuroblasts. Laboratory investigation; a journal of technical methods and pathology 31 3906271
2009 Modular architecture and evolution of the map-1 gene family in the root-knot nematode Meloidogyne incognita. Molecular genetics and genomics : MGG 30 19787376
2009 Degradation of methamidophos by Hyphomicrobium species MAP-1 and the biochemical degradation pathway. Biodegradation 30 19960233
1988 Heat-stable microtubule protein MAP-1 binds to microtubules and induces microtubule assembly. FEBS letters 30 3130274
2012 Crystal structure and functional characterization of the complement regulator mannose-binding lectin (MBL)/ficolin-associated protein-1 (MAP-1). The Journal of biological chemistry 29 22854970
2012 miR-1228 prevents cellular apoptosis through targeting of MOAP1 protein. Apoptosis : an international journal on programmed cell death 28 22434376
2016 MOAP-1 Mediates Fas-Induced Apoptosis in Liver by Facilitating tBid Recruitment to Mitochondria. Cell reports 27 27320914
2015 Modulator of apoptosis 1 (MOAP-1) is a tumor suppressor protein linked to the RASSF1A protein. The Journal of biological chemistry 26 26269600
1986 Molecular aspects of MAP-1 and MAP-2: microheterogeneity, in vitro localization and distribution in neuronal and nonneuronal cells. Annals of the New York Academy of Sciences 21 3460414
2012 The map-1 gene family in root-knot nematodes, Meloidogyne spp.: a set of taxonomically restricted genes specific to clonal species. PloS one 20 22719916
2001 MAP-1 and IAP-1, two novel AAA proteases with catalytic sites on opposite membrane surfaces in mitochondrial inner membrane of Neurospora crassa. Molecular biology of the cell 20 11553723
2022 Alpha-Mangostin Activates MOAP-1 Tumor Suppressor and Mitochondrial Signaling in MCF-7 Human Breast Cancer Cells. Evidence-based complementary and alternative medicine : eCAM 16 35082905
2016 RASSF1A Site-Specific Methylation Hotspots in Cancer and Correlation with RASSF1C and MOAP-1. Cancers 15 27294960
2020 Tricistronic expression of MOAP-1, Bax and RASSF1A in cancer cells enhances chemo-sensitization that requires BH3L domain of MOAP-1. Journal of cancer research and clinical oncology 13 32377840
1986 Rapid proteolysis of brain MAP-1 related cytoskeleton-associated 350kd protein by purified calpain. Cell structure and function 12 3021343
2021 Human Cytomegalovirus miR-UL70-3p Downregulates the H2O2-Induced Apoptosis by Targeting the Modulator of Apoptosis-1 (MOAP1). International journal of molecular sciences 11 35008453
2018 RACK1/TRAF2 regulation of modulator of apoptosis-1 (MOAP-1). Biochimica et biophysica acta. Molecular cell research 11 29470995
1985 Developmental changes in components of chick brain microtubule-associated protein-1 (MAP-1) and tau proteins. Journal of biochemistry 10 3924904
2021 The BAX-binding protein MOAP1 associates with LC3 and promotes closure of the phagophore. Autophagy 9 33783314
2018 Chimeric Proteins Containing MAP-1 and Functional Domains of C4b-Binding Protein Reveal Strong Complement Inhibitory Capacities. Frontiers in immunology 9 30210498
2022 Revealing the Roles of MOAP1 in Diseases: A Review. Cells 8 35269511
2015 Genetically engineered fusion of MAP-1 and factor H domains 1-5 generates a potent dual upstream inhibitor of both the lectin and alternative complement pathways. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 8 26260032
2021 Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins. Proteins 7 34357660
2024 Adenovirus-mediated expression of MOAP-1, Bax and RASSF1A antagonizes chemo-drug resistance of human breast cancer cells expressing cancer stem cell markers. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 6 38810399
1988 Vesikin, a vesicle associated ATPase from squid axoplasm and optic lobe, has characteristics in common with vertebrate brain MAP 1 and MAP 2. Cell motility and the cytoskeleton 6 2460257
1986 Distinction of G0 cells from senescent cells in cultures of non-cycling human fetal lung fibroblasts by anti-MAP-1 monoclonal antibody staining. Experimental cell research 6 3956580
2019 Combining MAP-1:CD35 or MAP-1:CD55 fusion proteins with pattern-recognition molecules as novel targeted modulators of the complement cascade. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 5 31469600
2025 The retrotransposon-derived capsid genes PNMA1 and PNMA4 maintain reproductive capacity. Nature aging 3 40263616
2018 Recombination and purifying and balancing selection determine the evolution of major antigenic protein 1 (map 1) family genes in Ehrlichia ruminantium. Gene 2 30316923
2026 KORE-Map 1.1: Korean medicine omics resource extension map on transcriptome data of dyspepsia herbal medicine. BMC genomic data 0 41618141
2026 Increased MAP-1 and lectin complement activation capacity in Klinefelter syndrome. The Journal of clinical endocrinology and metabolism 0 41873701
2026 Rare coding and noncoding variants map 1,342 diseases and biomarkers in 490,549 whole genomes. medRxiv : the preprint server for health sciences 0 41929321
2026 Lectin pathway of complement in SLE: MAP-1 as a marker of haematological manifestations and elevated type I interferon activity. Lupus science & medicine 0 41956715
2025 Long non-coding RNA AK007111 mediates mast cells apoptosis via targeting of protein MOAP1. The Journal of asthma : official journal of the Association for the Care of Asthma 0 39969102
2025 PNMA4 enhances anti-RNA virus immunity by promoting RIG-I signaling pathway. International immunopharmacology 0 40929959
2024 The retrotransposon - derived capsid genes PNMA1 and PNMA4 maintain reproductive capacity. bioRxiv : the preprint server for biology 0 38798495
2024 The retrotransposon-derived capsid genes PNMA1 and PNMA4 maintain reproductive capacity. Research square 0 39041030
2012 [PB1-F2 protein of influenza A virus interacts with human MOAP-1 protein]. Wei sheng wu xue bao = Acta microbiologica Sinica 0 23236846