Affinage

DUSP14

Dual specificity protein phosphatase 14 · UniProt O95147

Length
198 aa
Mass
22.3 kDa
Annotated
2026-06-09
36 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DUSP14 (MKP6/MKP-L) is a dual-specificity MAP kinase phosphatase that acts as a negative-feedback regulator of inflammatory, immune, and stress-activated signaling (PMID:11123293, PMID:23229544). Its catalytic core directly dephosphorylates MAP kinases, hydrolyzing phosphorylated substrates in vitro and dephosphorylating JNK; this activity is competitively blocked by the active-site inhibitor PTP inhibitor IV (PMID:19646420, PMID:19787133). The dominant mechanistic theme is suppression of the TAB1-TAK1 signaling node: DUSP14 directly binds TAK1 and dephosphorylates it at the activation-loop residue Thr-187, and binds TAB1 to dephosphorylate it at Ser-438, inactivating the TAB1-TAK1 complex and dampening downstream JNK, p38, and NF-κB activation (PMID:23229544, PMID:24403530, PMID:29077210). Through this TAK1-directed activity DUSP14 restrains T cell costimulatory and TCR signaling — DUSP14-deficient mice show enhanced T cell responses and EAE susceptibility — and protects multiple tissues from inflammatory and ischemic injury including liver, heart, cartilage, and airway (PMID:24403530, PMID:28887166, PMID:29077210, PMID:40449853). DUSP14 phosphatase activity is switched on by a sequential post-translational cascade in which PRMT5-mediated arginine methylation (R17/R38/R45) licenses TRAF2-mediated Lys63-linked ubiquitination at Lys-103 (PMID:26521044, PMID:29920217). Beyond MAPK control, DUSP14 dephosphorylates MLKL to suppress cardiomyocyte necroptosis and acts through a PTPN12-PPARα-SCD axis to govern ferroptosis in triple-negative breast cancer (PMID:40357546, PMID:41032417).

Mechanistic history

Synthesis pass · year-by-year structured walk · 7 steps
  1. 2001 Medium

    Established DUSP14's physiological context by identifying it as a CD28-tail-binding protein that provides negative feedback on costimulatory signaling, framing it as a brake on MAP kinase-driven T cell activation.

    Evidence Yeast-hybrid cloning plus dominant-negative and CD28-tail-mutant rescue in primary human T cells with IL-2 readout

    PMID:11123293

    Open questions at the time
    • Direct phosphatase substrate not defined at this stage
    • CD28-DUSP14 binding interface not mapped
  2. 2007 Medium

    Demonstrated intrinsic enzymatic activity and broader roles, showing recombinant DUSP14 is an active phosphatase and a negative regulator of MAPK/ERK-driven proliferation and immune suppression.

    Evidence Recombinant phosphatase assay on p-nitrophenyl phosphate, MHC-II cell-binding and DTH assays, and beta-cell siRNA/dominant-negative proliferation assays

    PMID:17263825 PMID:18025410

    Open questions at the time
    • Physiological MAPK substrate not directly identified
    • Secreted-protein and intracellular-phosphatase roles not reconciled
  3. 2009 High

    Provided direct biochemical proof of catalytic mechanism, defining DUSP14 as an active-site phosphatase that dephosphorylates JNK and is inhibited competitively by PTP inhibitor IV.

    Evidence In vitro phosphatase assays, kinetic competitive-inhibition analysis, and a synthetic ESIPT fluorescent substrate

    PMID:19646420 PMID:19787133

    Open questions at the time
    • In-cell substrate specificity not addressed
    • No structural model of the catalytic site
  4. 2014 High

    Identified the core signaling node by showing DUSP14 directly binds TAB1 and TAK1 and dephosphorylates them at defined residues (TAK1 Thr-187, TAB1 Ser-438) to shut down NF-κB/JNK signaling, with loss-of-function confirmed in KO mice.

    Evidence Co-IP, in vitro dephosphorylation, catalytic-dead and binding mutants, TAB1 knockdown epistasis, and DUSP14-KO mice with EAE phenotype

    PMID:23229544 PMID:24403530

    Open questions at the time
    • Relative contribution of TAK1 vs TAB1 dephosphorylation unresolved
    • Whether DUSP14 binds TAK1 directly or via TAB1 later disputed
  5. 2018 High

    Defined how DUSP14 is activated, establishing a sequential PTM cascade in which PRMT5 arginine methylation (R17/38/45) is required for TRAF2-mediated K63 ubiquitination at K103, which in turn enables phosphatase activity during TCR signaling.

    Evidence MS site mapping, PRMT5 in vitro methylation, K103 and triple-methylation mutants, TRAF2/PRMT5 shRNA epistasis, proximity ligation, and phosphatase assays

    PMID:26521044 PMID:29920217

    Open questions at the time
    • Structural basis for how methylation/ubiquitination activates catalysis unknown
    • Whether the cascade operates outside TCR signaling untested
  6. 2018 High

    Extended the TAK1-axis to tissue protection, showing hepatocyte DUSP14-TAK1 binding suppresses JNK/p38/NF-κB to guard against ischemia-reperfusion injury and NAFLD steatosis, requiring both binding and catalytic activity.

    Evidence Hepatocyte-specific KO and transgenic mice, Co-IP/pulldown, binding-domain and phosphatase-dead mutants, and TAK1 inhibitor epistasis

    PMID:28887166 PMID:29077210

    Open questions at the time
    • Upstream signals controlling hepatic DUSP14 activity not defined
    • Contribution of ROS reduction vs direct dephosphorylation not separated
  7. 2025 High

    Broadened the substrate repertoire beyond MAPK signaling, showing DUSP14 dephosphorylates MLKL to block necroptosis and acts via PTPN12-PPARα-SCD to control ferroptosis, expanding its role into regulated cell death.

    Evidence DUSP14 KO/overexpression mice with p-MLKL readout and small-molecule activator, plus DUSP14 knockdown with PTPN12/PPARα/SCD and lipid-peroxidation readouts in TNBC xenografts

    PMID:40357546 PMID:41032417

    Open questions at the time
    • Direct dephosphorylation of MLKL/PTPN12 vs indirect effects not fully resolved
    • Phospho-residues targeted on these substrates not mapped

Open questions

Synthesis pass · forward-looking unresolved questions
  • How DUSP14 substrate selection is partitioned across its many substrates (TAK1, TAB1, JNK, MLKL, PTPN12) in different tissues, and the structural basis for its PTM-dependent activation, remain open.
  • No structure of DUSP14 in complex with any substrate
  • Tissue-specific determinants of substrate preference unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 5 GO:0016787 hydrolase activity 3 GO:0098772 molecular function regulator activity 3
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 2 R-HSA-5357801 Programmed Cell Death 2
Partners
CD28MLKLPRMT5PTPN12TAB1TAK1TRAF2

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 MKP6 (DUSP14) was identified as a CD28 cytoplasmic tail-interacting protein via yeast-hybrid technology, and functions as a negative-feedback regulator of CD28 costimulatory signaling by inactivating MAP kinases; dominant-negative MKP6 enhanced IL-2 secretion specifically in response to CD28 costimulation, and a CD28 cytoplasmic tail mutant unable to bind MKP6 costimulated larger quantities of IL-2. Yeast-hybrid cloning, retroviral dominant-negative transfer into primary human T cells, IL-2 secretion assay, MAP kinase activation measurement Journal of immunology Medium 11123293
2009 DUSP14 phosphatase activity is selectively inhibited by PTP inhibitor IV (bis(4-trifluoromethyl-sulfonamidophenyl)-1,4-diisopropylbenzene) in a competitive manner, indicating that PTP inhibitor IV binds to the catalytic site of DUSP14; DUSP14 was shown to directly dephosphorylate JNK in vitro. In vitro phosphatase activity screen, kinetic competitive inhibition assay, in vitro DUSP14-mediated JNK dephosphorylation assay Biochemical and biophysical research communications High 19646420
2009 A fluorescent ESIPT probe was designed by phosphorylation of the HBT chromophore and shown to be selectively hydrolyzed by DUSP14 (MKP-6) phosphatase activity, demonstrating the enzymatic activity of DUSP14 toward a phosphorylated substrate. In vitro fluorescent probe enzymatic hydrolysis assay (ESIPT-based) Chemical communications Medium 19787133
2012 DUSP14 negatively regulates TNF- and IL-1-induced NF-κB activation by directly interacting with TAK1 and dephosphorylating TAK1 at Thr-187 (a residue in the activation loop critical for TAK1 activation); overexpression of phosphatase-dead DUSP14 mutant failed to inhibit NF-κB activation, confirming catalytic activity is required. Co-immunoprecipitation, overexpression and knockdown (siRNA), Western blot for TAK1 phosphorylation, NF-κB reporter assay, phosphatase-deficient mutant analysis The Journal of biological chemistry High 23229544
2014 DUSP14 negatively regulates TCR signaling by directly interacting with TAB1 (TAK1-binding protein 1) and dephosphorylating TAB1 at Ser438, leading to inactivation of the TAB1-TAK1 complex and reduced downstream JNK and IKK activation; DUSP14-deficient mice showed enhanced T cell proliferation, cytokine production, and susceptibility to EAE. DUSP14-knockout mouse generation, co-immunoprecipitation, in vitro dephosphorylation assay, TAB1 shRNA knockdown epistasis, EAE disease model Journal of immunology High 24403530
2015 DUSP14 is modified by TRAF2-mediated Lys63-linked ubiquitination at lysine 103, and this ubiquitination is required for DUSP14 phosphatase activity during TCR signaling; TRAF2 shRNA knockdown reduced DUSP14 ubiquitination and phosphatase activity. Mass spectrometry identification of ubiquitination site, mutational analysis (K103 mutation), co-immunoprecipitation of TRAF2-DUSP14, TRAF2 shRNA knockdown, phosphatase activity assay Cellular signalling High 26521044
2017 DUSP14 physically interacts with TAK1 and suppresses NF-κB and MAPK (JNK) signaling in hepatocytes; hepatocyte-specific DUSP14 knockout exacerbated hepatic ischemia-reperfusion injury while DUSP14 transgenic mice were protected; mutant DUSP14 unable to bind TAK1 failed to protect against hepatic I/R injury; TAK1 inhibition abolished DUSP14 function in vivo, placing DUSP14 upstream of TAK1 in this pathway. Hepatocyte-specific KO and TG mouse models, co-immunoprecipitation, pull-down assays, Western blot, TAK1 inhibitor epistasis, TAK1-binding mutant DUSP14 Journal of hepatology High 28887166
2018 PRMT5 methylates DUSP14 at arginine residues 17, 38, and 45; this arginine methylation is required for subsequent TRAF2-mediated Lys63-linked ubiquitination and phosphatase activity of DUSP14 during TCR signaling, establishing a sequential PTM cascade (methylation→ubiquitination→activation). DUSP14 directly interacts with TAB1 but not TAK1. Proximity ligation assay, co-immunoprecipitation, in vitro methylation assay (PRMT5), triple-methylation mutant analysis, PRMT5 shRNA knockdown, phosphatase activity assay FASEB journal High 29920217
2018 DUSP14 directly binds to and dephosphorylates TAK1 in hepatocytes, reducing activation of TAK1 downstream signaling including JNK1, p38, and NF-κB; both the binding domain and phosphatase activity of DUSP14 are required for protection against hepatic steatosis in NAFLD models; disruption of the DUSP14-TAK1 interaction abolished DUSP14's mitigative effects. Hepatocyte-specific overexpression (HTG) and KO (HKO) mouse models, co-immunoprecipitation, binding-domain and phosphatase-dead mutants, high-fat diet NAFLD model, TAK1 inhibitor rescue Hepatology High 29077210
2007 DUSP14 knockdown or expression of dominant-negative DUSP14 in beta-cells increased beta-cell line proliferation and enhanced GLP-1-induced proliferation of primary beta-cells, identifying DUSP14 as a negative regulator of the MAPK/ERK1/2 pathway that limits GLP-1-induced beta-cell proliferation. siRNA knockdown, dominant-negative expression, [3H]thymidine and BrdU incorporation proliferation assays in beta-cell lines and primary mouse islets Diabetes Medium 18025410
2007 DUSP14 (as NSF) was identified by MALDI-TOF mass spectrometry as a ~22.5 kDa protein secreted by macrophage-like suppressor cells that exists as a dimer under non-reducing conditions; recombinant DUSP14 exhibited phosphatase activity toward p-nitrophenyl phosphate and suppressed delayed-type hypersensitivity by binding specifically to MHC class II (Ia)-positive dendritic cells. MALDI-TOF mass spectrometry protein identification, recombinant DUSP14 in vitro phosphatase assay, binding assay to MHC class II+ cells, anti-DUSP14 monoclonal antibody neutralization, DTH/CHS functional assays The British journal of dermatology Medium 17263825
2018 DUSP14 knockout in mice increased NF-κB and MAPK (p38, ERK1/2, JNK) activation following cardiac ischemia-reperfusion injury; ROS scavenger N-acetylcysteine abolished the DUSP14-knockdown-augmented NF-κB and MAPK activation in cardiomyocytes, indicating DUSP14 suppresses these pathways via reducing ROS generation. DUSP14 knockout mouse, DUSP14 siRNA knockdown in primary cardiomyocytes, Western blot for MAPK/NF-κB, ROS measurement, N-acetylcysteine rescue experiment Biochemical and biophysical research communications Medium 29660332
2018 DUSP14 axon growth inhibition in retinal ganglion cells operates downstream of KLF9 transcription factor; decreasing Dusp14 expression (siRNA/shRNA) or pharmacological inhibition (PTP inhibitor IV) increased axon growth in vitro and promoted RGC survival and optic nerve regeneration in vivo, linking the KLF9-Dusp14 axis to suppression of MAPK-dependent neurotrophic signaling. KLF9 overexpression + microarray to identify downstream targets, siRNA/shRNA knockdown of Dusp14, PTP inhibitor IV pharmacological inhibition, in vitro neurite length assay, in vivo optic nerve crush model in rats and mice Investigative ophthalmology & visual science Medium 29860460
2024 JUNI lncRNA physically interacts with DUSP14 protein and counteracts its phosphatase activity, thereby facilitating JNK phosphorylation and c-Jun induction under UV/genotoxic stress; depletion of JUNI reduced JNK phosphorylation and cell survival, and this effect was mediated through JUNI's antagonism of DUSP14. Protein-RNA interaction screen (57 JUNI-interacting proteins identified), JNK phosphorylation Western blot, JUNI depletion functional rescue, UV/genotoxic drug treatment Oncogene Medium 38565943
2025 DUSP14 dephosphorylates MLKL (mixed lineage kinase domain-like protein), thereby inhibiting necroptosis in cardiomyocytes; cardiomyocyte-specific DUSP14 overexpression reduced MLKL phosphorylation and necroptosis in hypothyroid mice, while DUSP14 knockout exacerbated necroptosis and cardiac dysfunction; a small-molecule activator (P077-0472) of DUSP14 inhibited cardiomyocyte necroptosis. DUSP14 KO mouse and AAV-mediated cardiomyocyte-specific overexpression, MLKL phosphorylation Western blot, Evans blue staining, LDH measurement, molecular docking for small-molecule activator, in vitro pharmacological activation assay Circulation High 40357546
2025 DUSP14 knockdown increased phosphorylation of PTPN12, thereby inhibiting PPARα transcriptional activity and downregulating SCD expression; this led to lipid peroxidation and ferroptotic cell death in triple-negative breast cancer cells; targeting the DUSP14-PTPN12-PPARα/SCD axis with a small-molecule drug restricted TNBC malignant phenotype. DUSP14 knockdown (in vitro and xenograft), PTPN12 phosphorylation Western blot, PPARα transcriptional activity assay, SCD expression measurement, lipid peroxidation assay, xenograft tumor model, small-molecule drug treatment Cell reports Medium 41032417
2025 DUSP14 interacts with TAK1 in bronchial epithelial cells (confirmed by co-immunoprecipitation) and DUSP14 overexpression restrains TAK1 and downstream NF-κB pathway activation, alleviating airway inflammation and mucus hypersecretion in an OVA asthma model. Co-immunoprecipitation of DUSP14-TAK1, DUSP14 overexpression in vitro (BEAS-2B cells) and OVA mouse model, Western blot for NF-κB/TAK1, inflammatory cytokine measurement Immunology letters Medium 40449853
2019 DUSP14 overexpression inhibited osteoclast differentiation induced by M-CSF and RANKL in bone marrow-derived cells and activated AMPKα; AMPKα blockade abolished the anti-osteoclast effect of DUSP14, placing DUSP14 upstream of AMPKα in suppression of osteoclastogenesis; DUSP14 transgenic mice were protected from magnesium silicate-induced inflammatory osteoporosis. DUSP14 overexpression in bone marrow-derived cells, M-CSF/RANKL osteoclast differentiation assay, AMPKα inhibitor epistasis, DUSP14 TG mouse model Biochemical and biophysical research communications Medium 31526569
2021 DUSP14 elevation in chondrocytes increased AMPK phosphorylation and inhibited NF-κB signaling (increased IκB, decreased p-p65); AMPK blockade abolished the protective effect of DUSP14 overexpression against IL-1β-induced inflammatory injury, establishing DUSP14 as acting upstream of AMPK-IκB to restrain NF-κB. DUSP14 overexpression in IL-1β-stimulated chondrocytes, AMPK inhibitor epistasis, Western blot for AMPK/NF-κB pathway, ACLT-induced OA rat model with DUSP14 injection, histological evaluation Bioengineered Medium 34605731
2026 DUSP14 protein level in colon cancer cells is inversely correlated with total TAK1 protein, and DUSP14 was functionally validated as a pharmacological target using cell lines and patient-derived organoids. RNA-sequencing, Western blot correlation of DUSP14 and TAK1 levels, in vitro cell line and patient-derived organoid drug targeting assays International journal of cancer Low 41922912

Source papers

Stage 0 corpus · 36 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6. Journal of immunology (Baltimore, Md. : 1950) 88 11123293
2012 Unrestrained p38 MAPK activation in Dusp1/4 double-null mice induces cardiomyopathy. Circulation research 87 22993413
2009 A highly selective fluorescent ESIPT probe for the dual specificity phosphatase MKP-6. Chemical communications (Cambridge, England) 86 19787133
2007 Increasing GLP-1-induced beta-cell proliferation by silencing the negative regulators of signaling cAMP response element modulator-alpha and DUSP14. Diabetes 80 18025410
2018 Evaluation of exosomal miR-9 and miR-155 targeting PTEN and DUSP14 in highly metastatic breast cancer and their effect on low metastatic cells. Journal of cellular biochemistry 68 30335891
2017 Dusp14 protects against hepatic ischaemia-reperfusion injury via Tak1 suppression. Journal of hepatology 65 28887166
2014 Dual-specificity phosphatase 14 (DUSP14/MKP6) negatively regulates TCR signaling by inhibiting TAB1 activation. Journal of immunology (Baltimore, Md. : 1950) 59 24403530
2018 Hepatocyte DUSP14 maintains metabolic homeostasis and suppresses inflammation in the liver. Hepatology (Baltimore, Md.) 50 29077210
2012 The dual-specificity phosphatase DUSP14 negatively regulates tumor necrosis factor- and interleukin-1-induced nuclear factor-κB activation by dephosphorylating the protein kinase TAK1. The Journal of biological chemistry 49 23229544
2018 The Krüppel-Like Factor Gene Target Dusp14 Regulates Axon Growth and Regeneration. Investigative ophthalmology & visual science 45 29860460
2020 MiR-155-5p accelerates cerebral ischemia-reperfusion injury via targeting DUSP14 by regulating NF-κB and MAPKs signaling pathways. European review for medical and pharmacological sciences 39 32096190
2019 Iron overload threatens the growth of osteoblast cells via inhibiting the PI3K/AKT/FOXO3a/DUSP14 signaling pathway. Journal of cellular physiology 39 30693516
2020 Neuroprotective effect of DUSP14 overexpression against isoflurane-induced inflammatory response, pyroptosis and cognitive impairment in aged rats through inhibiting the NLRP3 inflammasome. European review for medical and pharmacological sciences 32 32633405
2018 DUSP14 knockout accelerates cardiac ischemia reperfusion (IR) injury through activating NF-κB and MAPKs signaling pathways modulated by ROS generation. Biochemical and biophysical research communications 30 29660332
2019 DUSP14 rescues cerebral ischemia/reperfusion (IR) injury by reducing inflammation and apoptosis via the activation of Nrf-2. Biochemical and biophysical research communications 28 30638656
2015 TRAF2-mediated Lys63-linked ubiquitination of DUSP14/MKP6 is essential for its phosphatase activity. Cellular signalling 27 26521044
2022 miR-155-5p accelerates cerebral ischemia-reperfusion inflammation injury and cell pyroptosis via DUSP14/ TXNIP/NLRP3 pathway. Acta biochimica Polonica 25 36441582
2018 Induction of DUSP14 ubiquitination by PRMT5-mediated arginine methylation. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 23 29920217
2016 Influence of the polymorphism of the DUSP14 gene on the expression of immune-related genes and development of pulmonary tuberculosis. Genes and immunity 14 26938665
2021 Eriocitrin attenuates ischemia reperfusion-induced oxidative stress and inflammation in rats with acute kidney injury by regulating the dual-specificity phosphatase 14 (DUSP14)-mediated Nrf2 and nuclear factor-κB (NF-κB) pathways. Annals of translational medicine 13 33708977
2009 PTP inhibitor IV protects JNK kinase activity by inhibiting dual-specificity phosphatase 14 (DUSP14). Biochemical and biophysical research communications 13 19646420
2024 Silencing miR-155-5p alleviates hippocampal damage in kainic acid-induced epileptic rats via the Dusp14/MAPK pathway. Brain research bulletin 10 39209069
2007 Novel function of DUSP14/MKP6 (dual specific phosphatase 14) as a nonspecific regulatory molecule for delayed-type hypersensitivity. The British journal of dermatology 10 17263825
2021 Enhancement of DUSP14 (dual specificity phosphatase 14) limits osteoarthritis progression by alleviating chondrocyte injury, inflammation and metabolic homeostasis. Bioengineered 8 34605731
2024 Inhibiting TRIM8 alleviates adipocyte inflammation and insulin resistance by regulating the DUSP14/MAPKs pathway. Adipocyte 7 39039652
2025 Exosomal Delivery of miR-155 Inhibitor can Suppress Migration, Invasion, and Angiogenesis Via PTEN and DUSP14 in Triple-negative Breast Cancer. Current medicinal chemistry 5 39484777
2022 Sevoflurane Post-treatment Mitigates Oxygen-glucose Deprivationinduced Pyroptosis of Hippocampal Neurons by Regulating the Mafb/DUSP14 Axis. Current neurovascular research 5 35927915
2024 The lincRNA JUNI regulates the stress-dependent induction of c-Jun, cellular migration and survival through the modulation of the DUSP14-JNK axis. Oncogene 4 38565943
2024 miR-199a-5p targets DUSP14 to regulate cell proliferation, invasion and stemness in non-small cell lung cancer. Heliyon 4 38644862
2023 Eriocitrin Alleviates Inflammation and Oxidative Stress in Subarachnoid Hemorrhage by Regulating DUSP14. Discovery medicine 4 38058079
2019 Activation of Dusp14 protects against osteoclast generation and bone loss by regulating AMPKα-dependent manner. Biochemical and biophysical research communications 4 31526569
2025 Dusp14-Mediated Dephosphorylation of MLKL Protects Against Cardiomyocyte Necroptosis in Hypothyroidism-Induced Heart Failure. Circulation 2 40357546
2025 DUSP14 attenuates airway inflammation and mucus hypersecretion in allergic asthma by regulating TAK1 activity. Immunology letters 2 40449853
2025 DUSP14 suppresses ferroptosis and promotes tumor progression of triple-negative breast cancer. Cell reports 2 41032417
2024 A Negative Regulatory Feedback Loop within the JAK-STAT Pathway Mediated by the Protein Tyrosine Phosphatase DUSP14 in Shrimp. Journal of immunology (Baltimore, Md. : 1950) 1 38767414
2026 Globo-H diagnostic stratification and identification of DUSP14 as a candidate target in colorectal cancer. International journal of cancer 0 41922912

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