| Dipeptidyl-peptidase 9 regulates the dynamics of tumorigenesis and metastasis in breast cancer. | Dipeptidyl-peptidase 9 regulates the dynamics of tumorigenesis and metastasis in breast cancer.
Heß L, Aliar K, Grünwald BT, Griffin R, Lozan A, Knöller M, Khokha R, Brummer T, Reinheckel T. | 05/29/2024 |
| DPP8/9 inhibition attenuates the TGF-beta1-induced excessive deposition of extracellular matrix (ECM) in human mesangial cells via Smad and Akt signaling pathways. | DPP8/9 inhibition attenuates the TGF-β1-induced excessive deposition of extracellular matrix (ECM) in human mesangial cells via Smad and Akt signaling pathways.
Li K, Zhang Y, Zhao W, Wang R, Li Y, Wei L, Wang L, Chen X, Chen Z, Liu P, Nie N, Tian X, Fu R. | 05/9/2024 |
| DPP9 Stabilizes NRF2 to Suppress Ferroptosis and Induce Sorafenib Resistance in Clear Cell Renal Cell Carcinoma. | DPP9 Stabilizes NRF2 to Suppress Ferroptosis and Induce Sorafenib Resistance in Clear Cell Renal Cell Carcinoma.
Chang K, Chen Y, Zhang X, Zhang W, Xu N, Zeng B, Wang Y, Feng T, Dai B, Xu F, Ye D, Wang C. | 12/5/2023 |
| Hemophagocytic lymphohistiocytosis-like hyperinflammation due to a de novo mutation in DPP9. | Hemophagocytic lymphohistiocytosis-like hyperinflammation due to a de novo mutation in DPP9.
Wolf C, Fischer H, Kühl JS, Koss S, Jamra RA, Starke S, Schultz J, Ehl S, Neumann K, Schuetz C, Huber R, Hornung V, Lee-Kirsch MA., Free PMC Article | 11/13/2023 |
| Inflammasome sensor NLRP1 disease variant M1184V promotes autoproteolysis and DPP9 complex formation by stabilizing the FIIND domain. | Inflammasome sensor NLRP1 disease variant M1184V promotes autoproteolysis and DPP9 complex formation by stabilizing the FIIND domain.
Moecking J, Laohamonthonkul P, Meşe K, Hagelueken G, Steiner A, Harapas CR, Sandow JJ, Graves JD, Masters SL, Geyer M., Free PMC Article | 01/11/2023 |
| CCR2 and DPP9 expression in the peripheral blood of COVID-19 patients: Influences of the disease severity and gender. | CCR2 and DPP9 expression in the peripheral blood of COVID-19 patients: Influences of the disease severity and gender.
Sharif-Zak M, Abbasi-Jorjandi M, Asadikaram G, Ghoreshi ZA, Rezazadeh-Jabalbarzi M, Afsharipur A, Rashidinejad H, Khajepour F, Jafarzadeh A, Arefinia N, Kheyrkhah A, Abolhassani M., Free PMC Article | 03/19/2022 |
| Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells. | Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells.
Zhang Y, Li K, Li Y, Zhao W, Wang L, Chen Z, Ma X, Yao T, Wang J, Dong W, Li X, Tian X, Fu R. | 02/12/2022 |
| DPP9 sequesters the C terminus of NLRP1 to repress inflammasome activation. | DPP9 sequesters the C terminus of NLRP1 to repress inflammasome activation.
Hollingsworth LR, Sharif H, Griswold AR, Fontana P, Mintseris J, Dagbay KB, Paulo JA, Gygi SP, Bachovchin DA, Wu H., Free PMC Article | 01/15/2022 |
| Structural and biochemical mechanisms of NLRP1 inhibition by DPP9. | Structural and biochemical mechanisms of NLRP1 inhibition by DPP9.
Huang M, Zhang X, Toh GA, Gong Q, Wang J, Han Z, Wu B, Zhong F, Chai J., Free PMC Article | 01/15/2022 |
| Dipeptidyl peptidase 9 sets a threshold for CARD8 inflammasome formation by sequestering its active C-terminal fragment. | Dipeptidyl peptidase 9 sets a threshold for CARD8 inflammasome formation by sequestering its active C-terminal fragment.
Sharif H, Hollingsworth LR, Griswold AR, Hsiao JC, Wang Q, Bachovchin DA, Wu H., Free PMC Article | 09/18/2021 |
| DPP9 restrains NLRP1 activation. | DPP9 restrains NLRP1 activation.
Bauernfried S, Hornung V. | 06/26/2021 |
| Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import. | Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import.
Finger Y, Habich M, Gerlich S, Urbanczyk S, van de Logt E, Koch J, Schu L, Lapacz KJ, Ali M, Petrungaro C, Salscheider SL, Pichlo C, Baumann U, Mielenz D, Dengjel J, Brachvogel B, Hofmann K, Riemer J., Free PMC Article | 04/13/2021 |
| Dipeptidyl Peptidase 9 Increases Chemoresistance and is an Indicator of Poor Prognosis in Colorectal Cancer. | Dipeptidyl Peptidase 9 Increases Chemoresistance and is an Indicator of Poor Prognosis in Colorectal Cancer.
Saso K, Miyoshi N, Fujino S, Sasaki M, Yasui M, Ohue M, Ogino T, Takahashi H, Uemura M, Matsuda C, Mizushima T, Doki Y, Eguchi H. | 04/3/2021 |
| Decrease of the pro-inflammatory M1-like response by inhibition of dipeptidyl peptidases 8/9 in THP-1 macrophages - quantitative proteomics of the proteome and secretome. | Decrease of the pro-inflammatory M1-like response by inhibition of dipeptidyl peptidases 8/9 in THP-1 macrophages - quantitative proteomics of the proteome and secretome.
Suski M, Wiśniewska A, Kuś K, Kiepura A, Stachowicz A, Stachyra K, Czepiel K, Madej J, Olszanecki R. | 12/5/2020 |
| DPP9 is an interacting partner of human NLRP1 and a related, human-specific inflammasome regulator, CARD8, and binds the autoproteolytic FIIND domain of both proteins. | Human DPP9 represses NLRP1 inflammasome and protects against autoinflammatory diseases via both peptidase activity and FIIND domain binding.
Zhong FL, Robinson K, Teo DET, Tan KY, Lim C, Harapas CR, Yu CH, Xie WH, Sobota RM, Au VB, Hopkins R, D'Osualdo A, Reed JC, Connolly JE, Masters SL, Reversade B., Free PMC Article | 04/20/2019 |
| we found a DPP9-PPP6R3 fusion transcript in one tumor showing a matching genomic 11;19-translocation. Another tumor had a rearrangement of DPP9 with PLIN3. Both rearrangements were associated with diminished expression of the 3' end of DPP9 corresponding to the breakpoints identified by RNA-seq. | Involvement of DPP9 in gene fusions in serous ovarian carcinoma.
Smebye ML, Agostini A, Johannessen B, Thorsen J, Davidson B, Tropé CG, Heim S, Skotheim RI, Micci F., Free PMC Article | 05/19/2018 |
| The data of this study have shown that fibroblasts and keratinocytes of normal skin endogenously express DPP9 both at transcriptional and protein level. It is localized intracellularly, mostly in cytoplasm, whereby the sub-localization within Golgi is very scarce. | Dipeptidyl peptidase 9 (DPP9) in human skin cells.
Gabrilovac J, Čupić B, Zapletal E, Kraus O, Jakić-Razumović J. | 12/9/2017 |
| DPP9 has a role in promoting tumorgenicity, metastasis and the prediction of poor prognosis in non-small cell lung cancer | Contribution of upregulated dipeptidyl peptidase 9 (DPP9) in promoting tumoregenicity, metastasis and the prediction of poor prognosis in non-small cell lung cancer (NSCLC).
Tang Z, Li J, Shen Q, Feng J, Liu H, Wang W, Xu L, Shi G, Ye X, Ge M, Zhou X, Ni S., Free PMC Article | 05/7/2017 |
| The DPP9 expressing cell model system is a very useful and promising system for investigating the selectivity and associated toxicity of DPP4 inhibitors on DPP9. | Establishment of a dipeptidyl peptidases (DPP) 8/9 expressing cell model for evaluating the selectivity of DPP4 inhibitors.
Huan Y, Jiang Q, Liu JL, Shen ZF. | 04/23/2016 |
| There was a concomitant decrease in the phosphorylation of focal adhesion kinase and paxillin, indicating that DPP9 knockdown or enzyme inhibition suppressed the associated adhesion signaling pathway, causing impaired cell movement. | Dipeptidyl peptidase 9 subcellular localization and a role in cell adhesion involving focal adhesion kinase and paxillin.
Zhang H, Chen Y, Wadham C, McCaughan GW, Keane FM, Gorrell MD. | 04/25/2015 |
| Whereas DPP9-short is present in the cytosol, DPP9-long localizes preferentially to the nucleus. | The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus.
Justa-Schuch D, Möller U, Geiss-Friedlander R., Free PMC Article | 11/8/2014 |
| The SUMO1-E67 interacting loop peptide is an allosteric inhibitor of the dipeptidyl peptidases 8 and 9. | The SUMO1-E67 interacting loop peptide is an allosteric inhibitor of the dipeptidyl peptidases 8 and 9.
Pilla E, Kilisch M, Lenz C, Urlaub H, Geiss-Friedlander R., Free PMC Article | 01/25/2014 |
| Suggest roles for DPP8 and DPP9 in lymphocyte activation and apoptosis and in hepatocytes during liver disease pathogenesis. | Regulation of dipeptidyl peptidase 8 and 9 expression in activated lymphocytes and injured liver.
Chowdhury S, Chen Y, Yao TW, Ajami K, Wang XM, Popov Y, Schuppan D, Bertolino P, McCaughan GW, Yu DM, Gorrell MD., Free PMC Article | 01/4/2014 |
| DPP9 was found in macrophages of carotid atherosclerotic plaque and may play a role in disease progression. | Dipeptidyl peptidases in atherosclerosis: expression and role in macrophage differentiation, activation and apoptosis.
Matheeussen V, Waumans Y, Martinet W, Van Goethem S, Van der Veken P, Scharpé S, Augustyns K, De Meyer GR, De Meester I. | 08/31/2013 |
| analysis of dipeptidyl peptidases 8 and 9 reveals that they may have compensatory roles | Identifying natural substrates for dipeptidyl peptidases 8 and 9 using terminal amine isotopic labeling of substrates (TAILS) reveals in vivo roles in cellular homeostasis and energy metabolism.
Wilson CH, Indarto D, Doucet A, Pogson LD, Pitman MR, McNicholas K, Menz RI, Overall CM, Abbott CA., Free PMC Article | 08/10/2013 |