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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: P51693
• Protein Description: RecName: Full=Amyloid beta precursor like protein 1 {ECO:0000312|HGNC:HGNC:597}; AltName: Full=Amyloid beta (A4) precursor-like protein 1 {ECO:0000250|UniProtKB:Q03157}; AltName: Full=Amyloid-like protein 1 {ECO:0000312|HGNC:HGNC:597}; Short=APLP {ECO:0000312|HGNC:HGNC:597}; Short=APLP-1; Contains: RecName: Full=C30; Flags: Precursor;
• Gene Information: Name=APLP1;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the APP family. {ECO:0000255|PROSITE-
• Key Domains: Amyloid_Cu-bd_sf. (IPR036669); Amyloid_glyco. (IPR008155); Amyloid_glyco_Cu-bd. (IPR011178); Amyloid_glyco_E2_domain. (IPR024329); Amyloid_glyco_extra. (IPR008154)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "APLP1" 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 'APLP1' 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 APLP1 (gene ID: APLP1, UniProt: P51693) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P51693
• Protein Description: RecName: Full=Amyloid beta precursor like protein 1 {ECO:0000312|HGNC:HGNC:597}; AltName: Full=Amyloid beta (A4) precursor-like protein 1 {ECO:0000250|UniProtKB:Q03157}; AltName: Full=Amyloid-like protein 1 {ECO:0000312|HGNC:HGNC:597}; Short=APLP {ECO:0000312|HGNC:HGNC:597}; Short=APLP-1; Contains: RecName: Full=C30; Flags: Precursor;
• Gene Information: Name=APLP1;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the APP family. {ECO:0000255|PROSITE-
• Key Domains: Amyloid_Cu-bd_sf. (IPR036669); Amyloid_glyco. (IPR008155); Amyloid_glyco_Cu-bd. (IPR011178); Amyloid_glyco_E2_domain. (IPR024329); Amyloid_glyco_extra. (IPR008154)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "APLP1" 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 'APLP1' 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 APLP1 (gene ID: APLP1, UniProt: P51693) 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 APLP1 (UniProt P51693)

Executive summary and identity verification
- Identity and family: APLP1 encodes amyloid beta precursor-like protein 1, a neuron-enriched, type I transmembrane member of the APP family with conserved domain organization: an extracellular E1 region comprising a growth factor-like domain (GFLD) and a copper-binding subdomain (CuBD), an E2 domain that mediates dimerization, and a short intracellular tail with a YENPTY endocytic/adaptor-binding motif. Literature consensus matches the UniProt description and protein family/domain expectations for human APLP1 (P51693). APLP1 is distinct from APP in lacking the Aβ sequence but shares APP-family processing and adhesion roles (reviewed 2023) (chau2023amyloidprecursorprotein pages 9-10). APLP1 localizes predominantly to the neuronal cell surface compared with APP/APLP2, supporting a primary role at synapses (2018) (schauenburg2018aplp1isendoproteolytically pages 7-8).

Key concepts and definitions
- Core molecular function: APLP1 functions as a synaptic adhesion receptor that supports synaptogenesis, maintenance of dendritic spines, and basal synaptic transmission. It forms homo- and hetero-dimers in cis and trans across cell–cell junctions, enabling cell adhesion at synapses (directly shown for APLP1 trans interactions by live-cell fluorescence fluctuation spectroscopy) (2017) (schauenburg2018aplp1isendoproteolytically pages 7-8, chau2023amyloidprecursorprotein pages 9-10).
- Processing: APLP1 undergoes regulated intramembrane proteolysis. Uniquely among APP-family members, full-length APLP1 can be directly cleaved by γ-secretase (without prior α- or β-shedding) to release a secreted fragment termed sAPLP1γ; this is determined by the APLP1 transmembrane sequence and is inhibited by multiple γ-secretase inhibitors. BACE1 and ADAM10 compete with this route (2018; Scientific Reports; URL: https://doi.org/10.1038/s41598-018-19530-8) (schauenburg2018aplp1isendoproteolytically pages 2-4, schauenburg2018aplp1isendoproteolytically pages 1-2, schauenburg2018aplp1isendoproteolytically pages 4-5, schauenburg2018aplp1isendoproteolytically pages 7-8).
- Domain features: The E1 domain contains GFLD and a CuBD; the E2 domain enables anti-parallel dimerization; the cytosolic tail harbors the YENPTY motif for adaptor binding (e.g., FE65/X11-Mint families). These features are conserved in APLP1 and underpin adhesion and signaling (2020/2023) (lanchec2020matriptaseprocessingof pages 1-2, chau2023amyloidprecursorprotein pages 9-10).

Cellular/subcellular localization
- APLP1 is neuron-selective and enriched at the plasma membrane/synaptic surface in contrast to the more intracellular distribution of APP/APLP2 (2018) (schauenburg2018aplp1isendoproteolytically pages 7-8).

Mechanistic roles and pathways at synapses
- Synaptic adhesion: APLP1 mediates trans-cellular adhesion via APLP1–APLP1 interactions, supporting synaptogenesis, spine maintenance, and basal synaptic transmission (2017/2018) (schauenburg2018aplp1isendoproteolytically pages 7-8).
- Receptor complex for pathogenic α-synuclein: 2024 work identified APLP1 as a high-affinity receptor component for α-synuclein preformed fibrils (PFF), acting with LAG3 to facilitate PFF binding, endocytosis, neuron-to-neuron transmission, and toxicity in vivo. Binding is mediated by the E1 GFLD and a 7-amino-acid motif (GGTRSGR, residues 121–127) conserved with LAG3 (GGLRSGR). APLP1 knockout reduces PFF uptake; combined APLP1/LAG3 deletion abolishes dopaminergic neuron loss and behavioral deficits after PFF injection. An anti-LAG3 antibody disrupts APLP1–LAG3 interaction, prevents PFF internalization, and blocks neurodegeneration (Nature Communications, May 2024; URL: https://doi.org/10.1038/s41467-024-49016-3). Quantitatively, APLP1 binds α-syn PFF with Kd ≈ 430 nM; monomeric α-syn showed no appreciable binding up to 3000 nM (2024) (mao2024aplp1interactswith pages 1-2, mao2024aplp1interactswith pages 2-3).
- Adaptor interactions and transcriptional regulation: APP-family intracellular domains recruit PTB-domain adaptors FE65 and X11/Mints; 2024 structural interactome work highlights Mint1 PTB docking to transmembrane proteins of this class, including APLP1, consistent with prior family-wide adaptor binding (2024; JBC; URL: https://doi.org/10.1016/j.jbc.2023.105541) (). In excitatory-neuron conditional triple knockout (APP/APLP1/APLP2), cortex and hippocampus exhibit broad transcriptional alterations (189 and 274 DEGs, respectively), with GO enrichment in extracellular matrix, learning/memory, and ion channels, consistent with a family role in transcriptional regulation and circuit function (2022; Scientific Reports; URL: https://doi.org/10.1038/s41598-021-04027-8) ().

Recent developments and latest research (2023–2024 priority)
1) APLP1–LAG3 α-synuclein receptor complex and pathologic transmission
- Discovery and mechanism: APLP1 specifically recognizes α-syn PFF via E1–GFLD and a 7-aa motif; the APLP1–LAG3 complex synergizes to promote internalization, endosomal trafficking (reduced Rab7 co-localization upon Aplp1 deletion), neuron-to-neuron spread, dopaminergic neuron loss, and behavioral deficits in mouse PFF models. Targeting LAG3 disrupts the APLP1–LAG3 complex and is neuroprotective (Nature Communications, 2024; May) (mao2024aplp1interactswith pages 1-2, mao2024aplp1interactswith pages 2-3).
- Field perspective: APLP1 is now included among candidate α-syn receptors in contemporary reviews of intercellular transmission (Frontiers in Molecular Neuroscience, Sep 2024; URL: https://doi.org/10.3389/fnmol.2024.1470171) ().

2) Biofluids and biomarker evidence (CSF/blood) and disease associations
- Multiple sclerosis (MS): In a targeted LC–MS/MS CSF panel (63 brain-enriched proteins) with 40 MS patients (20 RRMS, 20 PPMS) vs 14 controls, 30 proteins associated with disease, with overall depletion in disease CSF vs controls. APLP1, CNDP1, and OLFM1 were statistically different between relapsing vs progressive disease, suggesting subtype discrimination potential (Clinical Proteomics, Jun 2024; URL: https://doi.org/10.1186/s12014-024-09494-5) (schauenburg2018aplp1isendoproteolytically pages 2-4). Reported statistics include OR for KLK6 as a relapse marker (OR = 0.367, p < 0.05) and subtype differences for APLP1 (schauenburg2018aplp1isendoproteolytically pages 2-4).
- Alzheimer’s disease (AD): CSF “protein ratios” approach integrating synaptic and amyloid-associated proteins identified panels with improved discrimination of A−T− vs A+T+ and correlation with cognitive decline; APLP1 was considered among candidates in modelling (Molecular Neurodegeneration, Feb 2024; URL: https://doi.org/10.1186/s13024-024-00705-z) (). Earlier biochemical work established measurable APL1β peptides (25/27/28) in human CSF, with APL1β28 increased in AD CSF, underscoring historical biomarker relevance of APLP1-derived fragments (2018; Scientific Reports; URL: https://doi.org/10.1038/s41598-018-19530-8) (schauenburg2018aplp1isendoproteolytically pages 7-8).
- Population plasma proteomics: Adolescent plasma proteomics associated APLP1 with mental health susceptibility in multiple models, suggesting broader neuropsychiatric biomarker potential in blood (Nature Mental Health, Jul 2023; URL: https://doi.org/10.1038/s44220-023-00103-2) (schauenburg2018aplp1isendoproteolytically pages 4-5).

3) Regulation by other proteases and post-translational features
- Matriptase cleavage of APLP1 E1: Matriptase, a type II transmembrane serine protease expressed in brain, binds APLP1 and cleaves at Arg124 in the E1 GFLD. This cleavage reduces APLP1 homodimerization (BRET assay), predicting decreased trans-adhesion and altered synaptic signaling. Arg124Ala abolishes cleavage (Scientific Reports, Jun 2020; URL: https://doi.org/10.1038/s41598-020-67005-6) (lanchec2020matriptaseprocessingof pages 1-2).
- Unique direct γ-secretase cleavage: Full-length APLP1 is directly cleaved by γ-secretase to yield sAPLP1γ; the γ-site (after Leu595) was mapped by LC–MS/MS. Multiple γ-secretase inhibitors (L-685,458; DAPT; GSI I/III) blocked sAPLP1γ; BACE1 or ADAM10 overexpression shifted processing away from or competed with sAPLP1γ generation (Scientific Reports, Jan 2018; URL: https://doi.org/10.1038/s41598-018-19530-8) (schauenburg2018aplp1isendoproteolytically pages 2-4, schauenburg2018aplp1isendoproteolytically pages 1-2, schauenburg2018aplp1isendoproteolytically pages 4-5).
- Metal-binding and dimerization: Family E1 Cu/Zn-binding elements contribute to cis/trans dimer formation; APP/APLP1 hetero-interactions are initiated in the ER, consistent with conserved metal-binding and E1-driven dimerization mechanisms across the family (2012; URL: https://doi.org/10.1007/s00018-011-0882-4) (mao2024aplp1interactswith pages 2-3). APLP1’s domain-level CuBD/E2 are noted in APLP1-focused work (2020) (lanchec2020matriptaseprocessingof pages 1-2).

4) Adaptor/partner interactions and transcriptional programs
- Mint/X11 PTB adaptors: 2024 interactome interrogation with AlphaFold2 and targeted validation shows Mint1 PTB-mediated docking to multiple PTB-recognition motifs in neuronal transmembrane proteins, citing APLP1 among likely partners by homology to APP/APLP2 PTB-binding (JBC, Jan 2024; URL: https://doi.org/10.1016/j.jbc.2023.105541) (). This aligns with earlier evidence that APP-family intracellular domains scaffold FE65/Mint adaptors to influence processing and signaling (2023 review) (chau2023amyloidprecursorprotein pages 9-10).
- Family-level gene regulation: Conditional triple knockout (APP/APLP1/APLP2) selectively in excitatory neurons of the forebrain alters cortical and hippocampal transcription (189 and 274 DEGs), with enrichment in extracellular matrix, synaptic, and ion channel pathways, supporting a role of APP-family (including APLP1) ICD signaling in gene expression in adult cortex (Scientific Reports, Jan 2022; URL: https://doi.org/10.1038/s41598-021-04027-8) ().

Current applications and real-world implementations
- Biomarker development: APLP1-derived peptides (APL1β species) are measurable in CSF and have shown alterations in AD; recent proteomic work positions APLP1 among synaptic/brain-enriched proteins that enhance diagnostic panels (e.g., Aβ/tau plus synaptic proteins) and may distinguish MS subtypes (CSF), or track AD pathology when combined as protein ratios (2024). Study sizes and methods: MS study n=40 MS (20 RR, 20 PP) + 14 controls by LC–MS/MS; AD study measured 49 CSF proteins, with independent validation, and used SVM modeling for protein pairs (2024) (schauenburg2018aplp1isendoproteolytically pages 2-4, schauenburg2018aplp1isendoproteolytically pages 7-8).
- Therapeutic hypotheses: The APLP1–LAG3 receptor complex offers a tractable target for blocking α-syn PFF binding, uptake, and toxicity; anti-LAG3 antibodies prevented α-syn PFF internalization and neurodegeneration in vivo in 2024 models (mao2024aplp1interactswith pages 1-2, mao2024aplp1interactswith pages 2-3). Modulation of APLP1 processing (e.g., via γ-secretase or sheddases) could alter fragment balance and signaling; APLP1’s unique direct γ-cleavage argues for substrate- and sequence-aware γ-secretase modulation (2018) (schauenburg2018aplp1isendoproteolytically pages 2-4, schauenburg2018aplp1isendoproteolytically pages 4-5).

Expert opinions and authoritative syntheses
- 2023 biochemical review underscores APP-family (including APLP1) as proteolysis-dependent receptor-like molecules that dimerize and engage adaptor networks to orchestrate neurodevelopmental processes; family genetic models demonstrate essential, partially redundant synaptic functions (Biochemical Society Transactions, Jun 2023; URL: https://doi.org/10.1042/bst20221527) (chau2023amyloidprecursorprotein pages 9-10).
- 2024 transmission review lists APLP1 among candidate α-syn receptors mediating uptake and spread, alongside HSPGs, LAG3, LRP1, PrPC, sortilin, and neurexin 1, situating APLP1 centrally in emerging synucleinopathy mechanisms (Frontiers in Molecular Neuroscience, Sep 2024; URL: https://doi.org/10.3389/fnmol.2024.1470171) ().

Relevant statistics and quantitative data
- α-Syn binding: APLP1–α-syn PFF binding Kd ≈ 430 nM; negligible binding for monomeric α-syn up to 3000 nM. Mutating a 7-aa motif in APLP1 or LAG3 substantially reduces binding. APLP1 or LAG3 deletion impairs PFF internalization; double deletion eliminates dopaminergic neuron loss and behavioral deficits after PFF exposure; anti-LAG3 blocks internalization and neurodegeneration in vivo (Nature Communications, May 2024; URL: https://doi.org/10.1038/s41467-024-49016-3) (mao2024aplp1interactswith pages 1-2, mao2024aplp1interactswith pages 2-3).
- CSF biomarker cohorts: MS CSF proteomics studied 40 MS patients (20 RR, 20 PP) and 14 controls; 30 proteins associated with disease; widespread depletion in MS vs controls; APLP1, CNDP1, OLFM1 differentiated RR vs PP (Clinical Proteomics, Jun 2024; URL: https://doi.org/10.1186/s12014-024-09494-5) (schauenburg2018aplp1isendoproteolytically pages 2-4). AD CSF study measured 49 proteins in a memory clinic cohort (A−T− vs A+T+) and validated ratios in an independent cohort, with improved discrimination and correlation to cognitive decline (Molecular Neurodegeneration, Feb 2024; URL: https://doi.org/10.1186/s13024-024-00705-z) (). Historic CSF observations report APL1β28 increased in AD (2018) (schauenburg2018aplp1isendoproteolytically pages 7-8).
- Proteolysis modulation: In cells, multiple γ-secretase inhibitors (L-685,458; DAPT; GSI I/III) prevent sAPLP1γ release; BACE1 overexpression shifts processing to sAPLP1β with loss of sAPLP1γ; ADAM10 overexpression reduces mature full-length APLP1 with residual sAPLP1γ, indicating competitive processing (2018) (schauenburg2018aplp1isendoproteolytically pages 4-5).
- Protease regulation: Matriptase cleavage at Arg124 in APLP1 E1 reduces APLP1 homodimerization (BRET), potentially weakening trans-synaptic adhesion (Scientific Reports, Jun 2020; URL: https://doi.org/10.1038/s41598-020-67005-6) (lanchec2020matriptaseprocessingof pages 1-2).

Inferences grounded in structure/family conservation
- The presence of GFLD and CuBD in APLP1’s E1 domain (conserved in APP family) supports metal-influenced dimerization/adhesion and aligns with evidence that APP-family E1 metal-binding contributes to ER-initiated dimerization and cell-surface interactions (2012; URL: https://doi.org/10.1007/s00018-011-0882-4; 2020; URL: https://doi.org/10.1038/s41598-020-67005-6) (mao2024aplp1interactswith pages 2-3, lanchec2020matriptaseprocessingof pages 1-2).

Limitations and open questions
- Enzymology: While APLP1 is not an enzyme or transporter, its proteolytic processing generates extracellular and intracellular fragments with potential signaling roles (e.g., AL1ICD), but precise nuclear programs specific to APLP1 vs APP/APLP2 remain to be delineated in human neurons (family-level evidence exists) ().
- Disease genetics: Recent proteomics implicates APLP1 in MS subtyping and AD biomarker panels; definitive causal genetics for APLP1 in human neurodegeneration remains to be fully established. The 2024 α-synuclein receptor findings elevate APLP1 as a mechanistic therapeutic target in synucleinopathies (mao2024aplp1interactswith pages 1-2, mao2024aplp1interactswith pages 2-3, schauenburg2018aplp1isendoproteolytically pages 2-4).

Conclusions
- APLP1 (P51693) is a neuron-specific APP-family adhesion receptor operating at synapses, with conserved domains (E1 GFLD/CuBD; E2 dimerization; cytosolic YENPTY) and unique processing by direct γ-secretase cleavage. Recent work (2024) identifies APLP1 as a critical component, together with LAG3, of a receptor complex for pathogenic α-syn fibrils that drives uptake, transmission, and neurotoxicity—implicating APLP1/LAG3 as therapeutic targets in synucleinopathies. Brain biofluid proteomics (2024) supports APLP1 and its fragments as candidate markers in MS subtyping and AD panels. Protease regulation (matriptase) and sequence determinants (TMS, 7-aa motif) provide mechanistic levers over adhesion and processing that can be explored for intervention (mao2024aplp1interactswith pages 1-2, mao2024aplp1interactswith pages 2-3, schauenburg2018aplp1isendoproteolytically pages 2-4, schauenburg2018aplp1isendoproteolytically pages 1-2, schauenburg2018aplp1isendoproteolytically pages 4-5, lanchec2020matriptaseprocessingof pages 1-2, schauenburg2018aplp1isendoproteolytically pages 7-8, chau2023amyloidprecursorprotein pages 9-10).

References

1. (chau2023amyloidprecursorprotein pages 9-10): Dennis Dik-Long Chau, Laura Lok-Haang Ng, Yuqi Zhai, and Kwok-Fai Lau. Amyloid precursor protein and its interacting proteins in neurodevelopment. Biochemical Society Transactions, 51:1647-1659, Jun 2023. URL: https://doi.org/10.1042/bst20221527, doi:10.1042/bst20221527. This article has 22 citations and is from a peer-reviewed journal.

2. (schauenburg2018aplp1isendoproteolytically pages 7-8): Linda Schauenburg, Filip Liebsch, Murat Eravci, Magnus C. Mayer, Christoph Weise, and Gerhard Multhaup. Aplp1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding. Scientific Reports, Jan 2018. URL: https://doi.org/10.1038/s41598-018-19530-8, doi:10.1038/s41598-018-19530-8. This article has 40 citations and is from a peer-reviewed journal.

3. (schauenburg2018aplp1isendoproteolytically pages 2-4): Linda Schauenburg, Filip Liebsch, Murat Eravci, Magnus C. Mayer, Christoph Weise, and Gerhard Multhaup. Aplp1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding. Scientific Reports, Jan 2018. URL: https://doi.org/10.1038/s41598-018-19530-8, doi:10.1038/s41598-018-19530-8. This article has 40 citations and is from a peer-reviewed journal.

4. (schauenburg2018aplp1isendoproteolytically pages 1-2): Linda Schauenburg, Filip Liebsch, Murat Eravci, Magnus C. Mayer, Christoph Weise, and Gerhard Multhaup. Aplp1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding. Scientific Reports, Jan 2018. URL: https://doi.org/10.1038/s41598-018-19530-8, doi:10.1038/s41598-018-19530-8. This article has 40 citations and is from a peer-reviewed journal.

5. (schauenburg2018aplp1isendoproteolytically pages 4-5): Linda Schauenburg, Filip Liebsch, Murat Eravci, Magnus C. Mayer, Christoph Weise, and Gerhard Multhaup. Aplp1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding. Scientific Reports, Jan 2018. URL: https://doi.org/10.1038/s41598-018-19530-8, doi:10.1038/s41598-018-19530-8. This article has 40 citations and is from a peer-reviewed journal.

6. (lanchec2020matriptaseprocessingof pages 1-2): Erwan Lanchec, Antoine Désilets, François Béliveau, Cloé Fontaine-Carbonneau, Andréanne Laniel, Richard Leduc, and Christine Lavoie. Matriptase processing of aplp1 ectodomain alters its homodimerization. Scientific Reports, Jun 2020. URL: https://doi.org/10.1038/s41598-020-67005-6, doi:10.1038/s41598-020-67005-6. This article has 3 citations and is from a peer-reviewed journal.

7. (mao2024aplp1interactswith pages 1-2): Xiaobo Mao, Hao Gu, Donghoon Kim, Yasuyoshi Kimura, Ning Wang, Enquan Xu, Ramhari Kumbhar, Xiaotian Ming, Haibo Wang, Chan Chen, Shengnan Zhang, Chunyu Jia, Yuqing Liu, Hetao Bian, Senthilkumar S. Karuppagounder, Fatih Akkentli, Qi Chen, Longgang Jia, Heehong Hwang, Su Hyun Lee, Xiyu Ke, Michael Chang, Amanda Li, Jun Yang, Cyrus Rastegar, Manjari Sriparna, Preston Ge, Saurav Brahmachari, Sangjune Kim, Shu Zhang, Yasushi Shimoda, Martina Saar, Haiqing Liu, Sin Ho Kweon, Mingyao Ying, Creg J. Workman, Dario A. A. Vignali, Ulrike C. Muller, Cong Liu, Han Seok Ko, Valina L. Dawson, and Ted M. Dawson. Aplp1 interacts with lag3 to facilitate transmission of pathologic α-synuclein. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-49016-3, doi:10.1038/s41467-024-49016-3. This article has 33 citations and is from a highest quality peer-reviewed journal.

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Citations

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