Affinage

DPP9

Dipeptidyl peptidase 9 · UniProt Q86TI2

Length
863 aa
Mass
98.3 kDa
Annotated
2026-06-09
48 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DPP9 is an intracellular serine dipeptidyl peptidase of the DPP IV gene family that removes N-terminal Xaa-Pro dipeptides from cytosolic proteins and peptides, coupling N-terminal processing to protein stability and immune regulation (PMID:12459266, PMID:19667070). As a rate-limiting cytoplasmic prolyl-peptidase, it degrades proline-containing antigenic peptides such as RU1(34-42), so that its loss enhances antigen presentation (PMID:19667070). By generating neo-N-termini that feed substrates into the N-degron/proteasomal pathway, DPP9 controls turnover of the tyrosine kinase Syk—recruited via Filamin A and primed for Cbl-mediated ubiquitination—and of adenylate kinase AK2, modulating B-cell receptor signaling and preventing cytosolic accumulation of active AK2 (PMID:27614019, PMID:32815200). The most extensively defined role of DPP9 is as an endogenous brake on the NLRP1 and CARD8 inflammasomes: it forms inhibitory ternary complexes (DPP9:full-length sensor:sensor C-terminal fragment) in which the N-terminus of the sensor CT inserts into the DPP9 active site, with both scaffolding and catalytic activity enforcing autoinhibition; small-molecule DPP8/9 inhibitors or viral antagonists disrupt these complexes to trigger pro-caspase-1-dependent, gasdermin-D-mediated pyroptosis (PMID:27820798, PMID:30291141, PMID:31525884, PMID:33731932, PMID:33731929, PMID:40608794). DPP9 enzymatic activity is allosterically stimulated by SUMO1 binding to an extended arm flanking the substrate entry site (PMID:23152501). Beyond its protease functions, DPP9 acts non-catalytically: it competes with NRF2 for KEAP1 binding to drive an antioxidant response, and it scaffolds the BRISC and CYLD-SPATA2 ubiquitin-signaling complexes (PMID:37713596, PMID:39615677, PMID:41826729, PMID:41636814). A de novo DPP9 mutation (p.Arg252Pro) that destabilizes the protein and abolishes inflammasome restraint causes severe infancy-onset autoinflammation with HLH-like features (PMID:37544411).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2002 Medium

    Establishing that DPP9 is a cytosolic member of the DPP IV serine protease family defined its catalytic machinery and subcellular compartment, framing it as an intracellular peptidase rather than a cell-surface enzyme.

    Evidence In silico identification, in vitro translation, SDS-PAGE, and subcellular fractionation

    PMID:12459266

    Open questions at the time
    • No natural substrate identified at this stage
    • Physiological function unaddressed
  2. 2009 High

    Identifying RU1(34-42) as the first natural substrate showed DPP9 is rate-limiting for cytoplasmic proline-peptide degradation and links its activity to antigen presentation.

    Evidence In vitro peptidase assay with cell extracts and siRNA knockdown with antigen presentation readout

    PMID:19667070

    Open questions at the time
    • Broader substrate repertoire unknown
    • No structural basis for substrate selectivity
  3. 2012 High

    Discovery of SUMO1 binding to an extended arm flanking the substrate entry site revealed an allosteric mechanism that stimulates DPP9 catalytic activity.

    Evidence Pulldown/co-IP, mutagenesis of the binding arm, enzymatic activity assays, and SUMO1 silencing

    PMID:23152501

    Open questions at the time
    • Physiological contexts where SUMO1-dependent regulation matters not defined
    • SUMO2 selectivity basis only partially explained
  4. 2016 High

    Defining Syk as an N-end rule substrate processed by DPP9 (recruited via Filamin A and primed for Cbl ubiquitination) connected DPP9 N-terminal processing to protein turnover and B-cell signaling.

    Evidence Co-IP of DPP9-Filamin A-Syk complex, N-terminal sequencing, pulse-chase/mutagenesis, ubiquitination assays, and siRNA knockdown

    PMID:27614019

    Open questions at the time
    • Generality of the Filamin A-mediated recruitment to other substrates unknown
  5. 2016 High

    Showing that DPP8/9 inhibition triggers ASC-independent pro-caspase-1 activation and gasdermin-D-mediated pyroptosis placed DPP9 as a suppressor of an inflammatory death pathway.

    Evidence Val-boroPro inhibition, caspase-1 KO mice, caspase-1 activity assays, and gasdermin D cleavage assays

    PMID:27820798

    Open questions at the time
    • The upstream sensor restrained by DPP9 was not yet identified at this stage
  6. 2018 High

    Identifying NLRP1 and CARD8 as DPP9-bound inflammasome sensors, and dissecting whether catalytic or scaffolding activity restrains each, established DPP9 as a direct endogenous inflammasome brake.

    Evidence Proteomics, co-IP, CRISPR deletion, catalytic-mutant rescue, reconstituted inflammasome and pyroptosis assays, and patient mutation analysis

    PMID:29967349 PMID:30291141 PMID:31525884

    Open questions at the time
    • Structural basis of the inhibitory complex not yet resolved
    • Differential requirement of binding vs. catalysis for NLRP1 vs. CARD8 mechanistically distinct
  7. 2017 High

    A catalytically inactive S729A knock-in mouse demonstrated that DPP9 enzymatic activity is required in vivo for survival of migratory tongue muscle progenitors, giving the protease an essential developmental role.

    Evidence Catalytic knock-in mouse, histology, apoptosis quantification, and phenotypic rescue by manual feeding

    PMID:28887018

    Open questions at the time
    • The relevant in vivo substrate driving progenitor apoptosis is not identified
  8. 2020 High

    Identifying AK2 as a substrate whose N-terminal processing triggers proteasomal degradation, plus >100 candidate mitochondrial-derived substrates, broadened DPP9's role in cytosolic proteostasis.

    Evidence Biochemical fractionation, DPP8/9 and proteasome inhibition, AK2 validation, and MS-based proteomics

    PMID:32815200

    Open questions at the time
    • Functional consequences for most candidate substrates untested
    • Physiological role of clearing cytosolic AK2 not fully defined
  9. 2021 High

    Cryo-EM structures of the NLRP1-DPP9 ternary complex resolved how DPP9 binds full-length NLRP1 and inserts the CT N-terminus into its active site, explaining how Val-boroPro disrupts autoinhibition to activate the inflammasome.

    Evidence Cryo-EM/crystal structures, biochemical reconstitution, structure-guided mutagenesis, and functional inflammasome assays (human and rat)

    PMID:33731929 PMID:33731932

    Open questions at the time
    • Structural detail of the DPP9-CARD8 complex less defined
    • How sensor CT degradation kinetics couple to oligomerization quantitatively
  10. 2018 Medium

    Linking DPP9 to CaMKII-phospholamban and PKC signaling in cardiomyocytes extended its functional reach to cardiac signaling, distinguishing it from DPP8.

    Evidence DPP9-specific siRNA, pharmacological inhibition, phosphorylation and PKC activity assays, Ca2+ transient and action potential recordings

    PMID:30487758

    Open questions at the time
    • Direct molecular substrate/partner mediating cardiac effects not identified
    • Single-lab finding
  11. 2023 Medium

    Demonstrating that DPP9 competes with NRF2 for KEAP1 binding via an ESGE motif in an enzyme-independent manner revealed a non-catalytic role in redox sensing and ferroptosis/drug resistance.

    Evidence Affinity purification, competition co-IP, ESGE motif mutagenesis, NRF2 stability and ROS assays, ferroptosis and sorafenib-resistance assays in ccRCC

    PMID:37713596

    Open questions at the time
    • In vivo relevance of the DPP9-KEAP1-NRF2 axis untested
    • Single lab
  12. 2024 Medium

    Showing KEAP1 traps DPP9 in an inactive non-dimeric conformation, which in turn blocks KEAP1 from degrading NRF2, defined a reciprocal endogenous inhibition mechanism coupling DPP9 to redox state.

    Evidence Co-IP, biochemical characterization of DPP9 conformational states, and NRF2 stability/competition assays

    PMID:39615677

    Open questions at the time
    • Physiological trigger driving the conformational switch not identified
    • Single lab
  13. 2023 Low

    Reporting BRCA2 as a DPP9 substrate whose N-terminal processing accelerates proteasomal turnover positioned DPP9 upstream of the N-degron pathway for a tumor suppressor.

    Evidence Enzymatic assays and substrate identification described in a methods review chapter

    PMID:37230592

    Open questions at the time
    • Reported in a methods review rather than detailed in an original research study
    • Cellular and physiological consequences not independently characterized
  14. 2026 Medium

    Proximity-labeling interactome mapping identified DPP9 as a non-catalytic scaffold disrupting BRISC and CYLD-SPATA2 ubiquitin-signaling complexes, linking it to IFNAR1 stability, PD-L1 transcription, and antitumor immunity.

    Evidence TurboID proximity labeling, NanoBRET in living cells, IFNAR1 ubiquitination, PD-L1, and T cell cytotoxicity assays with DPP9 inhibition

    PMID:41636814 PMID:41826729

    Open questions at the time
    • Structural basis of BRISC/CYLD-SPATA2 disruption unknown
    • Single-lab findings awaiting independent replication
  15. 2023 Medium

    A destabilizing de novo DPP9 mutation causing constitutive NLRP1/CARD8 activation and severe autoinflammation established DPP9 loss-of-function as a Mendelian autoinflammatory disease mechanism.

    Evidence Patient genetics, transfection in HEK293T and patient iPSCs, inflammasome activity assays, and protein stability assessment

    PMID:37544411

    Open questions at the time
    • Genotype-phenotype spectrum across patients not defined
    • Single index case

Open questions

Synthesis pass · forward-looking unresolved questions
  • The full physiological substrate repertoire of DPP9, the mechanisms switching it between catalytic and non-catalytic scaffolding roles, and how its redox-sensing, ubiquitin-signaling, and inflammasome functions are coordinated in vivo remain open.
  • Most candidate substrates lack functional validation
  • Conformational/redox triggers governing DPP9 activity state unresolved
  • Integration of DPP9's diverse functions at the organismal level unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 3 GO:0016787 hydrolase activity 2
Localization
GO:0005829 cytosol 3
Pathway
R-HSA-168256 Immune System 5 R-HSA-392499 Metabolism of proteins 3 R-HSA-5357801 Programmed Cell Death 3 R-HSA-8953897 Cellular responses to stimuli 2
Partners
ABRAXAS2BRCC3CARD8FLNAKEAP1NLRP1SUMO1SYK
Complex memberships
BRISCCARD8-DPP9 complexCYLD-SPATA2NLRP1-DPP9 inflammasome ternary complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 DPP9 is a cytosolic serine protease belonging to the DPP IV gene family, containing a catalytic triad (Ser, Asp, His) and the GWSYG serine protease motif identical to DPP IV. It lacks transmembrane domains and a signal sequence, consistent with its cytosolic localization, and migrates at ~98 kDa on SDS-PAGE. In silico identification, in vitro translation, SDS-PAGE, subcellular fractionation Gene Medium 12459266
2009 DPP9 is rate-limiting for degradation of proline-containing peptides in the cytoplasm. Its first identified natural substrate is the RU1(34-42) antigenic peptide (VPYGSFKHV); DPP9 degrades this peptide in vitro, and DPP9 knockdown in intact cells increases antigen presentation of RU1(34-42). In vitro peptidase assay with cell extracts; siRNA knockdown with antigen presentation readout The Journal of biological chemistry High 19667070
2012 DPP9 binds SUMO1 (but not SUMO2) via a novel SUMO-interacting motif in an extended arm structure flanking the substrate entry site, independent of the canonical SIM. SUMO1 binding stimulates DPP9 enzymatic activity; mutations in the SUMO1-binding arm reduce DPP9 activity, and silencing SUMO1 decreases cytosolic prolyl-peptidase activity. Pulldown/co-IP, mutagenesis, enzymatic activity assays, siRNA knockdown The Journal of biological chemistry High 23152501
2016 DPP8 and DPP9 inhibition (by Val-boroPro/Talabostat) triggers pyroptosis in monocytes and macrophages by activating pro-caspase-1 independent of the inflammasome adaptor ASC. Activated pro-caspase-1 cleaves gasdermin D to induce pyroptosis but does not efficiently process itself or IL-1β. Caspase-1 knockout mice do not show immune stimulation after Val-boroPro treatment. Small-molecule inhibition, genetic knockout (caspase-1 KO mice), caspase-1 activity assays, gasdermin D cleavage assay Nature chemical biology High 27820798
2016 DPP9 interacts with Filamin A, which recruits DPP9 to the tyrosine kinase Syk. DPP9 cleaves Syk to expose a neo-N-terminus with serine at position 1 (N-end rule substrate), which strongly influences Syk stability. DPP9 processing is a prerequisite for Syk ubiquitination by the E3 ligase Cbl, and DPP9 inhibition stabilizes Syk and modulates B-cell signaling. Co-IP (DPP9-Filamin A-Syk complex), N-terminal sequencing, pulse-chase/mutagenesis, siRNA knockdown, ubiquitination assays eLife High 27614019
2018 CARD8 mediates DPP8/9 inhibitor-induced pro-caspase-1-dependent pyroptosis in human myeloid cells. DPP8/9 inhibitors induce pyroptosis in the majority of human AML cell lines and primary AML samples but not in cells from many other lineages. Genetic knockdown/knockout, reconstituted inflammasome assays, primary patient samples, mouse xenograft models Nature medicine High 29967349
2018 DPP9 directly interacts with human NLRP1 and CARD8 via their FIIND (Function-to-Find) autoproteolytic domains and acts as an endogenous inhibitor of the NLRP1 inflammasome. Both DPP9's scaffolding/binding function and its catalytic activity act synergistically to maintain NLRP1 in its inactive state. A patient-derived germline missense mutation in NLRP1's FIIND domain abrogates DPP9 binding and causes inflammasome hyperactivation. Proteomics screen, co-IP, CRISPR/Cas9 deletion, small-molecule inhibitors, ASC speck formation assay, IL-1β secretion, pyroptosis assays, patient mutation functional analysis The Journal of biological chemistry High 30291141
2017 DPP9 enzyme activity is required for survival of migratory tongue muscle progenitors in vivo. Catalytically inactive DPP9 knock-in mice (S729A) die within 12–18 h of birth due to microglossia caused by increased apoptosis of occipital somite-derived migratory muscle progenitors forming distal tongue intrinsic muscles. Catalytic knock-in mouse (S729A), histology, apoptosis quantification, phenotypic rescue by manual feeding Developmental biology High 28887018
2018 DPP9's enzymatic catalytic activity, but not its binding to CARD8, restrains the CARD8 inflammasome. Wild-type but not catalytically inactive DPP9 rescues CARD8-mediated cell death in DPP9 knockout cells. The DPP9-CARD8 interaction (unlike the DPP9-NLRP1 interaction) is not disrupted by DPP9 inhibitors or CARD8 mutations blocking autoproteolysis. Activity-based probes, reconstituted inflammasome assays, mass spectrometry-based proteomics, DPP9 knockout cell lines, catalytic mutant rescue ACS chemical biology High 31525884
2020 DPP8/9 mediate N-terminal processing of adenylate kinase 2 (AK2) in the cytoplasm. DPP9-mediated processing of AK2 induces its rapid proteasomal degradation and prevents cytosolic accumulation of enzymatically active AK2. Over 100 mitochondrial proteins with putative DPP8/9 recognition sites were identified, and DPP8/9 influence cellular levels of a subset of these. Biochemical fractionation, DPP8/9 inhibition, proteasome inhibition, AK2 substrate validation, MS-based proteomics The EMBO journal High 32815200
2021 Cryo-EM structures of human NLRP1-DPP9 complex (alone and with Val-boroPro) reveal a ternary complex comprising DPP9, full-length NLRP1, and the NLRP1 C-terminal fragment (CT). The N-terminus of NLRP1 CT inserts into the DPP9 active site; Val-boroPro disrupts this interaction. Binding of NLRP1 CT to DPP9 requires full-length NLRP1. VbP weakens the NLRP1-DPP9 interaction and accelerates degradation of the N-terminal fragment to induce inflammasome activation. Cryo-EM structure determination, biochemical binding assays, functional inflammasome assays, ectopic expression rescue experiments Nature High 33731932
2021 Structural and biochemical analysis of rat NLRP1-DPP9 shows a 2:1 complex with one autoinhibited full-length NLRP1 and one active UPA-CARD fragment. The ZU5 domain is required for both NLRP1 autoinhibition and 2:1 complex assembly. Complex formation prevents UPA-mediated higher-order oligomerization and strengthens ZU5-mediated autoinhibition. Both NLRP1 binding and DPP9 enzymatic activity are required to suppress NLRP1 in human cells. Cryo-EM/crystal structure, biochemical reconstitution, structure-guided mutagenesis, functional inflammasome assays in human cells Nature High 33731929
2018 Saxagliptin (but not sitagliptin) inhibits DPP9 in cardiomyocytes and impairs CaMKII phosphorylation of phospholamban and PKC activity. DPP9 knockdown (but not DPP8 knockdown) and pharmacological DPP8/9 inhibition recapitulate these effects, implicating DPP9 specifically in CaMKII-PLB and PKC signaling in cardiomyocytes. siRNA knockdown of DPP9 vs DPP8, pharmacological inhibition (TC-E-5007, saxagliptin, sitagliptin), CaMKII/PLB phosphorylation assays, PKC activity assays, Ca2+ transient measurements, action potential duration recording in cardiomyocytes Frontiers in physiology Medium 30487758
2023 DPP9 binds KEAP1 via a conserved ESGE motif and disrupts KEAP1-NRF2 binding by competing with NRF2 for KEAP1 binding in an enzyme-independent (non-catalytic) manner. DPP9 overexpression stabilizes NRF2, drives NRF2-dependent transcription, decreases cellular ROS, suppresses ferroptosis, and induces sorafenib resistance in ccRCC cells, largely dependent on the NRF2 target SLC7A11. Protein affinity purification, co-IP competition assays, ESGE motif mutagenesis (enzyme-independent binding), NRF2 stability assays, ROS measurement, ferroptosis assays, drug resistance assays Cancer research Medium 37713596
2022 The NLRP1 variant M1184V stabilizes the FIIND domain in a monomeric conformation, promotes DPP9 binding (confirmed by surface plasmon resonance and co-IP), and enhances formation of the autoinhibited NLRP1-DPP9 complex, leading to reduced inflammasome activation. Size-exclusion chromatography, molecular dynamics simulation, surface plasmon resonance, immunoprecipitation, inflammasome activity assays The Journal of biological chemistry Medium 36309085
2023 In addition to Syk and AK2, BRCA2 (tumor suppressor) was identified as a DPP9 substrate; N-terminal processing of BRCA2 by DPP9 triggers its rapid proteasomal turnover, placing DPP9 as an upstream component of the N-degron pathway. Enzymatic assays, substrate identification (described in review/methods context referencing experimental data) Methods in enzymology Low 37230592
2023 A de novo DPP9 mutation (p.Arg252Pro) destabilizes the DPP9 protein and causes it to fail to restrain the NLRP1 and CARD8 inflammasomes, resulting in constitutive inflammasome activation and severe infancy-onset autoinflammation with HLH-like features. Patient genetic analysis, transfection in HEK293T cells and patient iPSCs, functional inflammasome assays (caspase-1 activation, IL-1β/IL-18 secretion), protein stability assessment The Journal of allergy and clinical immunology Medium 37544411
2020 FAP (Fibroblast Activation Protein) interacts intracellularly with DPP9 (identified by IP-MS), and FAP overexpression leads to reduction in DPP9 expression, promoting EMT in oral squamous cell carcinoma. DPP9 overexpression reverses FAP-induced proliferation, migration, invasion, and EMT, acting in a non-enzymatic manner. IP-mass spectrometry, DPP9 knockdown/overexpression, cell proliferation, migration and invasion assays, EMT marker analysis, in vivo xenograft OncoTargets and therapy Low 32273729
2024 KEAP1 binds DPP9 in an inactive (non-native) conformation and stabilizes this non-dimeric fold. Reciprocally, this inactive form of DPP9 inhibits KEAP1 from binding and degrading NRF2, thereby inducing an antioxidant response. This reveals an endogenous DPP9 inhibition mechanism and links DPP9, like thioredoxin-1, to the intracellular redox potential. Co-IP, biochemical characterization of DPP9 conformational states, NRF2 stability assays, binding competition assays The Journal of biological chemistry Medium 39615677
2025 SFTSV non-structural protein NSs activates the NLRP1 and CARD8 inflammasomes by disrupting the DPP9-mediated inhibitory ternary complex: NSs binds NLRP1 and CARD8 via their FIIND domains (competing with DPP8/9 for binding) and promotes degradation of DPP8 and DPP9, releasing activated C-terminal fragments. Viral infection of primary keratinocytes and macrophages, co-IP (NSs-NLRP1/CARD8 interaction), DPP9 protein level measurement, CARD8 deletion functional assay PLoS pathogens Medium 40608794
2026 DPP9 interacts with the BRISC deubiquitinase complex (BRCC36/BRCC3 and ABRO1/ABRAXAS2) and CYLD-SPATA2 complex. DPP9 disrupts BRISC-SHMT2 complex formation, reducing BRISC-mediated deubiquitination and stabilization of IFNAR1, thereby suppressing JAK/STAT-driven PD-L1 transcription in ccRCC. DPP9 inhibition restores T cell cytotoxicity and enhances checkpoint blockade. TurboID proximity labeling, NanoBRET in living cells, pharmacological DPP9 inhibition (1G244), IFNAR1 ubiquitination assays, PD-L1 expression assays, T cell cytotoxicity assays, co-IP Cell death and differentiation Medium 41826729
2026 DPP9 interactome mapped by TurboID proximity labeling reveals DPP8, the E3 ligase CBL, the deubiquitinase complex CYLD-SPATA2, and BRISC complex components (BRCC36/BRCC3, ABRO1/ABRAXAS2) as DPP9 interactors. NanoBRET assays show DPP9 disrupts BRCC36-ABRO1 binding and CYLD-SPATA2 interaction, revealing non-catalytic scaffolding functions of DPP9 in ubiquitin signaling. TurboID proximity labeling in DPP9-KO HEK293 cells, NanoBRET in living cells, validation co-IPs Cellular and molecular life sciences Medium 41636814

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2018 DPP8/DPP9 inhibitor-induced pyroptosis for treatment of acute myeloid leukemia. Nature medicine 304 29967349
2016 DPP8 and DPP9 inhibition induces pro-caspase-1-dependent monocyte and macrophage pyroptosis. Nature chemical biology 243 27820798
2018 Human DPP9 represses NLRP1 inflammasome and protects against autoinflammatory diseases via both peptidase activity and FIIND domain binding. The Journal of biological chemistry 189 30291141
2021 DPP9 sequesters the C terminus of NLRP1 to repress inflammasome activation. Nature 169 33731932
2021 Structural and biochemical mechanisms of NLRP1 inhibition by DPP9. Nature 127 33731929
2002 Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV. Gene 119 12459266
2009 The cytoplasmic peptidase DPP9 is rate-limiting for degradation of proline-containing peptides. The Journal of biological chemistry 92 19667070
2023 DPP9 Stabilizes NRF2 to Suppress Ferroptosis and Induce Sorafenib Resistance in Clear Cell Renal Cell Carcinoma. Cancer research 89 37713596
2012 A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulation. The Journal of biological chemistry 56 23152501
2019 DPP9's Enzymatic Activity and Not Its Binding to CARD8 Inhibits Inflammasome Activation. ACS chemical biology 54 31525884
2011 Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal? Journal of medicinal chemistry 50 21711053
2020 Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import. The EMBO journal 49 32815200
2016 DPP9 is a novel component of the N-end rule pathway targeting the tyrosine kinase Syk. eLife 47 27614019
2020 Fibroblast Activation Protein (FAP) Overexpression Induces Epithelial-Mesenchymal Transition (EMT) in Oral Squamous Cell Carcinoma by Down-Regulating Dipeptidyl Peptidase 9 (DPP9). OncoTargets and therapy 30 32273729
2022 CCR2 and DPP9 expression in the peripheral blood of COVID-19 patients: Influences of the disease severity and gender. Immunobiology 28 35131543
2022 A Phenotypic Screen Identifies Potent DPP9 Inhibitors Capable of Killing HIV-1 Infected Cells. ACS chemical biology 25 36044633
2017 Involvement of DPP9 in gene fusions in serous ovarian carcinoma. BMC cancer 23 28893231
2024 DPP9 regulates NQO1 and ROS to promote resistance to chemotherapy in liver cancer cells. Redox biology 20 39094401
2018 Saxagliptin but Not Sitagliptin Inhibits CaMKII and PKC via DPP9 Inhibition in Cardiomyocytes. Frontiers in physiology 19 30487758
2017 DPP9 enzyme activity controls survival of mouse migratory tongue muscle progenitors and its absence leads to neonatal lethality due to suckling defect. Developmental biology 19 28887018
2023 Highly Selective Inhibitors of Dipeptidyl Peptidase 9 (DPP9) Derived from the Clinically Used DPP4-Inhibitor Vildagliptin. Journal of medicinal chemistry 16 37721854
2013 DPP8 and DPP9 expression in cynomolgus monkey and Sprague Dawley rat tissues. Regulatory peptides 16 23850796
2021 Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells. Pharmacological research 15 33932609
2016 Dipeptidyl peptidase 9 (DPP9) in human skin cells. Immunobiology 15 27682012
2018 Expression and clinical role of the dipeptidyl peptidases DPP8 and DPP9 in ovarian carcinoma. Virchows Archiv : an international journal of pathology 14 30467600
2009 Dipeptidyl peptidase 9 (DPP9) from bovine testes: identification and characterization as the short form by mass spectrometry. Biochimica et biophysica acta 14 20026260
2023 Hemophagocytic lymphohistiocytosis-like hyperinflammation due to a de novo mutation in DPP9. The Journal of allergy and clinical immunology 10 37544411
2014 Establishment of a selective evaluation method for DPP4 inhibitors based on recombinant human DPP8 and DPP9 proteins. Acta pharmaceutica Sinica. B 10 26579375
2008 Association study between adolescent idiopathic scoliosis and the DPP9 gene which is located in the candidate region identified by linkage analysis. Postgraduate medical journal 8 18940951
2024 Pinocembrin activation of DPP9 inhibits NLRP1 inflammasome activation to alleviate cerebral ischemia/reperfusion-induced lung and intestinal injury. Immunologic research 7 39676095
2022 Inflammasome sensor NLRP1 disease variant M1184V promotes autoproteolysis and DPP9 complex formation by stabilizing the FIIND domain. The Journal of biological chemistry 7 36309085
2025 The non-structural protein of SFTSV activates NLRP1 and CARD8 inflammasome through disrupting the DPP9-mediated ternary complex. PLoS pathogens 4 40608794
2024 The serine protease DPP9 and the redox sensor KEAP1 form a mutually inhibitory complex. The Journal of biological chemistry 4 39615677
2022 DPP9 as a Potential Novel Mediator in Gastrointestinal Virus Infection. Antioxidants (Basel, Switzerland) 4 36358551
2018 DPP9 enzymatic activity in hematopoietic cells is dispensable for mouse hematopoiesis. Immunology letters 4 29709545
2025 Dipeptidyl peptidase 9 (DPP9) depletion from hepatocytes in experimental primary liver cancer. Biochimica et biophysica acta. Molecular basis of disease 3 40187163
2024 Study on the correlation between DPP9 rs2109069 and IFNAR2 rs2236757 polymorphisms with COVID-19 mortality. Nucleosides, nucleotides & nucleic acids 3 38660988
2023 The amino-dipeptidyl peptidases DPP8 and DPP9: Purification and enzymatic assays. Methods in enzymology 3 37230592
2019 Immune regeneration in irradiated mice is not impaired by the absence of DPP9 enzymatic activity. Scientific reports 3 31086209
2025 DPP8 and DPP9 promote tubular epithelial cell ferroptosis in acute kidney injury. European journal of medical research 2 40665400
2024 Single nucleotide variants in the CCL2, OAS1 and DPP9 genes and their association with the severity of COVID-19 in an Ecuadorian population. Frontiers in cellular and infection microbiology 2 38694517
2024 In Silico analysis unveils rs2109069 of DPP9 as a potential catalyst for COVID-19 severity and risk of inflammatory symptoms. Experimental and molecular pathology 2 39615159
2017 Expression, subcellular localisation, and possible roles of dipeptidyl peptidase 9 (DPP9) in murine macrophages. Cell biochemistry and function 2 28256001
2024 Cosolvent Molecular Dynamics Applied to DPP4, DPP8 and DPP9: Reproduction of Important Binding Features and Use in Inhibitor Design. Journal of chemical information and modeling 1 39332821
2024 Molecular Targeted Engagement of DPP9 in Rat Tissue Using CETSA, SP3 Processing, and Absolute Quantitation Mass Spectrometry. ACS chemical biology 1 39642389
2023 DPP9 Comes of Age: Highly Selective Inhibitors Promise New Therapeutic Opportunities. Journal of medicinal chemistry 1 37721863
2026 Proximity labeling reveals non-catalytic interactions between DPP9 and ubiquitin signaling complexes. Cellular and molecular life sciences : CMLS 0 41636814
2026 DPP9 inhibition boosts antitumor immunity by disrupting BRISC-mediated PD-L1 expression in clear cell renal cell carcinoma. Cell death and differentiation 0 41826729

Missed literature

Know a paper Affinage missed for DPP9? Flag it for the maintainers and the community.

No submissions yet.