| 1993 |
PPP1CA (PP1α) was identified as a binding partner of the retinoblastoma protein (pRB) using yeast two-hybrid screening and in vitro binding assays. PP1α isoforms preferentially bind the hypophosphorylated form of pRB, and this association occurs from mitosis to early G1, suggesting PP1α regulates pRB function through the cell cycle. |
Yeast two-hybrid, in vitro binding assay, cell cycle synchrony experiments |
Genes & development |
High |
8384581
|
| 1984 |
DARPP-32 (a dopamine-regulated neuronal phosphoprotein) is a potent inhibitor of PP1 (protein phosphatase-1, including PP1α) at nanomolar concentrations, and this inhibition is active only in the phosphorylated form of DARPP-32, establishing PP1 as a key effector downstream of dopamine signaling. |
Biochemical inhibition assay with purified proteins |
Nature |
High |
6087160
|
| 1999 |
PPP1CA (PP1α) is phosphorylated at Thr-320 during M-phase and again in late G1 through early S-phase by Cdk2 (but not Cdk4) in a pRB-dependent manner. This inhibitory phosphorylation is required to prevent untimely pRB reactivation during the G1/S transition; PP1α phosphorylated at Thr-320 co-precipitates with pRB during G1/S. |
In vivo phosphorylation with isoform-specific antibodies, in vitro Cdk2 kinase assay, co-immunoprecipitation, cell cycle synchronization |
The Journal of biological chemistry |
High |
10506210
|
| 2000 |
PP1 (including PPP1CA) is a component of the macromolecular RyR2 signaling complex on the sarcoplasmic reticulum, demonstrated by co-sedimentation and co-immunoprecipitation. PKA phosphorylation of RyR2 regulates channel open probability, and in failing human hearts RyR2 is PKA hyperphosphorylated with defective channel function. |
Co-sedimentation, co-immunoprecipitation, single-channel recordings |
Cell |
High |
10830164
|
| 2002 |
PP1 (PPP1CA) is required for β-adrenergic regulation of the KCNQ1-KCNE1 (IKS) potassium channel. PP1 is targeted to hKCNQ1 through the anchoring protein yotiao via a leucine zipper motif. Disruption of this interaction by an LQTS mutation (hKCNQ1-G589D) impairs channel regulation. |
Co-immunoprecipitation, mutagenesis, electrophysiology |
Science |
High |
11799244
|
| 2002 |
PP1 (PPP1CA catalytic subunit) is recruited to substrates through over fifty regulatory/targeting subunits that interact with a conserved RVxF motif-binding hydrophobic groove on the PP1c surface. This targeting mechanism directs PP1c to specific subcellular locations and modulates its activity/specificity. |
Biochemical interaction mapping, structural analysis of PP1c complexes, mutational analysis |
Journal of cell science |
High |
11839776
|
| 2003 |
PP1 (including PPP1CA) resides in a mitochondrial macromolecular complex with BAD, PKA, WAVE-1, and glucokinase in liver. BAD is required to assemble this complex; its phosphorylation status regulates glucokinase activity and integrates glycolysis with apoptosis. |
Proteomic analysis, co-immunoprecipitation, genetics (Bad-deficient hepatocytes), functional metabolic assays |
Nature |
High |
12931191
|
| 2005 |
PP1 (including PPP1CA) dephosphorylates tau at multiple sites (Ser199, Ser202, Thr205, Thr212, Ser214, Ser235, Ser262, Ser396, Ser404, Ser409) in vitro, contributing approximately 11% of total tau phosphatase activity in human brain, with Km values of 8-12 μM. |
In vitro phosphatase assay with purified proteins and phosphorylation site-specific antibodies, Km determination |
The European journal of neuroscience |
High |
16262633
|
| 2008 |
PPP1CA (PP1α) acts cooperatively with PP2B downstream of Ca2+ signaling to release P-TEFb from the 7SK snRNP complex. PP1α dephosphorylates phospho-Thr186 in the Cdk9 T-loop, releasing P-TEFb to activate RNA Pol II transcription elongation. PP2B acts first to induce a conformational change in 7SK snRNP that facilitates PP1α access. |
Co-immunoprecipitation, in vitro phosphatase assay, siRNA knockdown, analysis of UV/HMBA-induced P-TEFb release |
Genes & development |
High |
18483222
|
| 2008 |
PPP1CA contributes to oncogenic Ras-induced senescence by promoting pRb dephosphorylation downstream of ceramide accumulation. Loss of PPP1CA function (via antisense RNA or shRNA) bypasses ras/p53-induced growth arrest; PPP1CA shRNA impairs p53-dependent p21 induction after DNA damage and blocks pRb dephosphorylation. |
Retroviral genetic screen, shRNA knockdown, cell cycle analysis, ceramide treatment |
Carcinogenesis |
Medium |
18204081
|
| 2008 |
Drosophila Uri (a conserved molecular chaperone) binds PP1α with much higher affinity than PP1β, and this PP1α-selective binding is conserved in humans. Uri is the first PP1α-specific binding protein identified in Drosophila; uri mutants show transcriptional defects, reduced cell viability in the germline, and accumulation of DNA damage. |
Binding affinity assays, loss-of-function genetics in Drosophila, immunostaining |
BMC molecular biology |
Medium |
18412953
|
| 2008 |
Hippocampal knockdown of PP1 (PPP1CA) by siRNA injection in mice was sufficient to enhance contextual and temporal long-term memory formation, demonstrating that PP1 acts as a negative regulator of memory consolidation in vivo. |
In vivo siRNA injection into hippocampus, contextual fear conditioning behavioral assay |
Genes, brain, and behavior |
Medium |
19191880
|
| 2010 |
PINCH1 directly binds PP1α (PPP1CA) and inhibits its phosphatase activity, resulting in increased Akt1 phosphorylation and enhanced radioresistance. PINCH1-mediated inhibition of PP1α perpetuates Akt1 activity in tumor cells adhered to ECM. |
Co-immunoprecipitation, in vitro phosphatase activity assay, siRNA knockdown, in vitro and in vivo irradiation experiments |
The Journal of clinical investigation |
High |
20530873
|
| 2011 |
PP1A (PPP1CA) directly interacts with and dephosphorylates YAP2 at Ser127 in vitro and in vivo, promoting YAP2 nuclear accumulation and transcriptional activation. Inhibition of PP1 by okadaic acid increases YAP2 phosphorylation and cytoplasmic retention. PP1A-mediated YAP2 dephosphorylation enhances cell survival in ovarian cancer cells. |
Co-immunoprecipitation, in vitro dephosphorylation assay, okadaic acid inhibition, subcellular fractionation, transcriptional reporter assay |
PloS one |
High |
21909427
|
| 2011 |
Taperin (C9orf75), encoded by a nonsyndromic deafness gene, preferentially docks PP1α (over PP1β/γ) through a classic RVxF motif and suppresses PP1α general phosphatase activity. Taperin-PP1α complexes are found in both nucleus and cytoplasm. SILAC mass spectrometry revealed taperin associates with DNA damage response proteins Ku70, Ku80, PARP, and topoisomerases, and taperin is actively recruited to sites of DNA damage. |
Biochemical purification, co-immunoprecipitation, SILAC mass spectrometry, phosphatase activity assay, mutagenesis of RVxF motif, live-cell imaging of DNA damage recruitment |
Biology open |
High |
23213405
|
| 2013 |
PP1α (PPP1CA), PP1β, and Wip1 phosphatases regulate histone H4 Ser47 phosphorylation (H4S47ph) levels and thereby control deposition of histone variant H3.3. PP1α and PP1β bind H3-H4 in vitro and in vivo and also interact with the H4S47 kinase Pak2, suggesting they regulate both Pak2 activity and direct H4S47 dephosphorylation. Depletion of PP1α increases H3.3 occupancy and deposition. |
Co-immunoprecipitation, in vitro binding assay, ChIP, siRNA depletion, mass spectrometry |
Nucleic acids research |
High |
23828041
|
| 2013 |
In the ERK/PP1α/PLB/SERCA2a pathway, luteolin activates ERK1/2 which upregulates PP1α expression, leading to phospholamban (PLB) upregulation and relief of SERCA2a inhibition, improving cardiomyocyte contractile function after ischemia/reperfusion injury. |
Isolated heart and cardiomyocyte functional assay, western blotting for phosphorylation status, pharmacological inhibitors (PD98059, SP600125), rat I/R model |
PloS one |
Medium |
24386130
|
| 2014 |
PP1A (PPP1CA) mediates canonical Wnt3a-induced TAZ dephosphorylation during osteogenic differentiation. Wnt3a signaling (through GSK3β inhibition) facilitates TAZ dephosphorylation by PP1A, which stabilizes TAZ, prevents 14-3-3 binding, and induces nuclear localization. Depletion of PP1A blocks Wnt3a-induced TAZ stabilization and osteoblast differentiation. |
siRNA depletion, western blotting for phospho-TAZ, subcellular fractionation, co-immunoprecipitation, differentiation assays |
Cell death and differentiation |
High |
24510127
|
| 2014 |
14-3-3ζ binds PPP1CA (PP1α) within residues 159-279 (independent of PP1α phosphorylation status) and retains PP1α in the cytosol, thereby regulating its nuclear trafficking. Expression of dominant-negative 14-3-3ζ (K49E) causes PP1α nuclear accumulation. 14-3-3ζ binding does not affect PP1α catalytic activity. |
Co-immunoprecipitation, GST pulldown, deletion mutant mapping, subcellular fractionation, dominant-negative expression |
Archives of biochemistry and biophysics |
Medium |
24956593
|
| 2005 |
PP1 inhibitor-3 (Inh3) co-localizes with PPP1CA (PP1α) specifically at centrosomes (not nucleoli) in interphase HEK293 cells, and co-immunoprecipitates with PP1α but not PP1β in vitro. Nucleolar localization of Inh3 is with PP1γ1. This demonstrates isoform-specific subcellular targeting of Inh3 to different PP1 complexes. |
Immunofluorescence co-localization, co-immunoprecipitation, site-directed mutagenesis of localization signals, laser scanning cytometry |
Archives of biochemistry and biophysics |
Medium |
16256067
|
| 2006 |
PP1α (PPP1CA) is identified as a regulator of caspase-9 activation. In IL-2-proliferating T cells, phosphorylated PP1α associates with phosphorylated caspase-9 (at Thr125). IL-2 deprivation induces PP1α dephosphorylation and activation, which then dephosphorylates caspase-9 Thr125 causing caspase-9 (and caspase-3) activation. PP1α associates with caspase-9 in vitro and in vivo; two novel PP1α-binding sites on caspase-9 were identified. |
Co-immunoprecipitation in vivo and in vitro, cell-free caspase activation assay, siRNA/phosphatase inhibitor experiments, identification of novel binding motifs |
Journal of immunology |
High |
16888006
|
| 2013 |
FOXP3 transcriptional activity in regulatory T cells is regulated by dephosphorylation at Ser418 by protein phosphatase 1 (PP1, including PPP1CA). TNF-α in rheumatoid arthritis synovium induces PP1 expression and activity, leading to FOXP3 Ser418 dephosphorylation and impaired Treg cell function. |
Western blotting with phospho-specific antibodies, PP1 activity assay, siRNA knockdown, functional Treg suppression assay, patient samples |
Nature medicine |
High |
23396208
|
| 2015 |
HSV-1 γ34.5 protein targets host PP1α (PPP1CA) to reverse translational arrest; this PP1α-targeting is required for HSV-1 to cause disseminated disease in neonatal mice. The PP1α-binding mutant of HSV-1 replicated in visceral organs early but failed to cause full disease. PP1α targeting by γ34.5 mediates eIF2α dephosphorylation to overcome the integrated stress response. |
Murine neonatal infection model, PP1α-binding mutant virus, type I IFN-deficient mice, pharmacological inhibition of eIF2α dephosphorylation in brain slice culture |
PNAS |
High |
26621722
|
| 2016 |
PP1α (PPP1CA) was identified as a negative regulator of TRPV1 channel activity through an HSV-based cDNA library screen. Vectors expressing PP1α reduced thermal sensitivity in rat footpads following virus injection, demonstrating that PP1α-mediated negative regulation of TRPV1 is functional in vivo with specificity for thermal pain. |
HSV-based library screen for TRPV1 inhibitors, in vitro capsaicin-based selection, in vivo thermal pain behavioral assay |
Molecular therapy. Methods & clinical development |
Medium |
27382601
|
| 2017 |
PP1α (PPP1CA) acts as a B-Raf activating phosphatase in a S6K/PP1α/B-Raf signaling pathway leading to MAPK activation. PML tumor suppressor sequesters PP1α into PML nuclear bodies, repressing S6K-dependent PP1α phosphorylation, 14-3-3 binding, and cytoplasmic accumulation. PPP1CA gene amplification is enriched in metastatic prostate cancer, and loss of PML derepresses this pathway. |
Co-immunoprecipitation, phosphorylation assays, subcellular fractionation, MAPK activity assays, genomic analysis of human cancer, mouse xenograft models |
Nature communications |
High |
29335436
|
| 2017 |
Oxidative stress (arsenite) promotes SIRT1 recruitment to the GADD34/PP1α complex to form a cytoplasmic GADD34/PP1α/eIF2α/SIRT1 complex. The GADD34/PP1α complex dephosphorylates both eIF2α (pSer51) and SIRT1 (pSer47); SIRT1 dephosphorylation activates its deacetylase activity. GADD34 mutants unable to bind PP1α fail to restore eIF2α or SIRT1 dephosphorylation. |
Mass spectrometry, co-immunoprecipitation, in vitro phosphatase assay, GADD34 knockout MEFs, rescue experiments with PP1α-binding mutant |
Cell death and differentiation |
High |
28984870
|
| 2018 |
The reduced activity of PP-1α under redox/oxidative stress is caused by transient disulfide bond formation (involving Cys39 and Cys127 in a dimerization event) mediated by glutathione (GSH). This shelters PP-1α against irreversible over-oxidation. The disulfide forms preferentially in the absence of substrate and the electron transport proceeds from the PP-1α catalytic core to the surface. |
Cross-over-read mass spectrometry for disulfide identification, biochemical activity assays under redox conditions, GSH treatment |
Scientific reports |
Medium |
30531830
|
| 2019 |
USP11 deubiquitinase stabilizes PPP1CA by deubiquitinating it and protecting it from proteasome-mediated degradation. The USP11/PPP1CA complex promotes colorectal cancer progression by activating the ERK/MAPK signaling pathway. |
LC-MS/MS protein interaction identification, co-immunoprecipitation, ubiquitination assays, in vitro and in vivo tumor assays |
EBioMedicine |
High |
31521612
|
| 2019 |
PP1A (PPP1CA) interacts with and dephosphorylates the transcriptional cofactor NACA at Thr-89, Ser-151, and Thr-174. NACA dephosphorylation increases its nuclear localization and, together with PP1A, cooperatively potentiates cJUN transcriptional activity of AP-1 target genes. This is required for osteoblast differentiation and matrix mineralization. |
Affinity purification mass spectrometry, co-immunoprecipitation with regulatory subunits (PPP1R9B, PPP1R12A, PPP1R18), MS-based phosphorylation mapping, Ala/Asp NACA mutants, transcriptional reporter assays, MC3T3-E1 osteoblast differentiation |
The Journal of biological chemistry |
High |
30948508
|
| 2019 |
Cavin-3 released from caveolae upon UV stress interacts with and inhibits PP1α (PPP1CA), resulting in increased H2AX phosphorylation and promotion of apoptosis. This defines a pro-apoptotic signaling pathway from plasma membrane caveolae to the nucleus via PP1α. |
Biotin affinity proteomics, mass spectrometry, cell-free expression system, protein-protein binding assays, co-immunoprecipitation, functional apoptosis assays |
Nature communications |
High |
31332168
|
| 2019 |
MIIP (migration and invasion inhibitory protein) interacts with PP1α (PPP1CA) via its C-terminal domain and enhances PP1-mediated AKT dephosphorylation, suppressing AKT-mTOR signaling in prostate cancer. Silencing PP1α reverses MIIP's inhibitory effect on AKT phosphorylation and cell growth; MIIPC lacking the PP1α-interaction domain loses its function. |
Western blot, immunofluorescence co-localization, co-immunoprecipitation, domain deletion mutants, PP1α siRNA, xenograft tumor model |
Cell communication and signaling |
Medium |
31092266
|
| 2021 |
The Smad4-MYO18A-PP1A complex dephosphorylates PAK1 at Thr423, which prevents PAK1-mediated phosphorylation of β-catenin at Ser675 and its nuclear translocation. MYO18A serves as the PP1-interacting protein for substrate recognition, binding PP1A via an RVFFR motif and Smad4 via its CC domain. |
LC-MS/MS, co-immunoprecipitation, biochemical dephosphorylation assays, RVFFR motif mutagenesis, in vitro and in vivo functional assays |
Cell death and differentiation |
High |
34799729
|
| 2021 |
SRPK1/2 and PP1α exert opposing functions on SRSF1 phosphorylation and nuclear translocation, which governs MKNK2 alternative splicing in colon adenocarcinoma. Decreased PP1α activity leads to enhanced SRSF1 phosphorylation and nuclear localization, promoting MKNK2b isoform expression. |
Western blotting, PCR-based splicing assays, kinase/phosphatase inhibitor treatment, siRNA knockdown, xenograft models |
Journal of experimental & clinical cancer research |
Medium |
33602301
|
| 2021 |
SNORD12B snoRNA interacts with PP-1α (PPP1CA) and disrupts the interaction between 14-3-3ζ and PP-1α, abolishing 14-3-3ζ-mediated cytoplasmic retention of PP-1α and causing its translocation to the nucleus. Nuclear sequestration of PP-1α reduces AKT dephosphorylation in the cytosol and activates AKT-mTOR-4EBP1 signaling to promote esophageal squamous cell carcinoma progression. |
Co-immunoprecipitation, subcellular fractionation, RNA immunoprecipitation, western blotting for phospho-AKT, in vitro and in vivo tumor models |
Oncogene |
Medium |
33941854
|
| 2021 |
LACTB directly binds PP1A (PPP1CA) and attenuates the PP1A-YAP interaction, resulting in decreased YAP dephosphorylation, increased phospho-YAP (Ser127), and prevention of YAP nuclear translocation, suppressing melanoma progression in a LATS1-independent manner. |
Co-immunoprecipitation, western blotting for phospho-YAP, subcellular fractionation, overexpression/knockdown functional assays, in vivo xenograft |
Cancer letters |
Medium |
33675985
|
| 2023 |
CARM1 methyltransferase methylates PPP1CA at arginine 23 (R23), which affects PPP1CA-mediated dephosphorylation of AKT at Thr450 and AMPK at Thr172, leading to increased glycolytic flux (via phosphofructokinase-1 and PFKFB3 activation), promoting osteogenic differentiation and inhibiting osteoclastic differentiation. |
In vitro methylation assay identifying R23 methylation site, CRISPR/Cas9 knockout, lentiviral overexpression, transcriptomics, metabolomics, western blotting, in vivo osteoporosis model |
Clinical and translational medicine |
High |
37649137
|
| 2023 |
SUV39H2 methyltransferase mono-methylates PPP1CA at K141, disrupting its interaction with TFEB (a newly identified PPP1CA substrate) and blocking TFEB dephosphorylation and nuclear translocation, leading to autophagy deficiency and nucleus pulposus cell senescence in intervertebral disc degeneration. PPP1R9B (neurabin II) serves as a regulatory subunit facilitating PPP1CA-TFEB targeting. |
Proteomic analysis, co-immunoprecipitation, in vitro dephosphorylation, K141 methylation-site identification, TFEB nuclear translocation assays, autophagy flux assays, in vivo disc degeneration model |
Cell death and differentiation |
High |
37605006
|
| 2023 |
Dietary potassium upregulates Ppp1Ca (PP1A) expression in the kidney and its negative regulator Ppp1r1a is suppressed. PP1A directly binds to and dephosphorylates the NaCl cotransporter (NCC), and this dephosphorylation is potassium-regulated and occurs in a WNK/SPAK-independent manner. Potassium-dependent suppression of inhibitory subunit 1 (I1) amplifies PP1A activity toward NCC, providing a mechanism for high-K+ diet to lower blood pressure. |
Transcriptomics screen, constitutively active SPAK knockin mice, direct PP1A-NCC co-immunoprecipitation, potassium manipulation experiments, blood pressure measurements |
The Journal of clinical investigation |
High |
37676724
|
| 2024 |
A peptide (PDHK1-241aa) encoded by circPDHK1 interacts with PPP1CA and causes its relocalization to the nucleus, thereby inhibiting AKT dephosphorylation in the cytosol and activating the AKT-mTOR signaling pathway to promote clear cell renal cell carcinoma progression. |
IP-MS, immunofluorescence, western blot, subcellular fractionation, siRNA/lentiviral expression, co-immunoprecipitation, xenograft and metastasis models |
Molecular cancer |
Medium |
38360682
|
| 2024 |
Zika virus NS2B acts as a scaffold mediating interaction between PP1α (PPP1CA) and eIF2α, promoting PP1α-dependent dephosphorylation of eIF2α to inhibit stress granule formation and boost viral replication. The NS2B-PP1α complex is resistant to ubiquitin-induced degradation. NS2BV35A mutant interacting only with eIF2α fails to inhibit stress granule formation. |
Co-immunoprecipitation, phosphorylation assays (phospho-eIF2α western blot), NS2B mutagenesis, stress granule imaging, brain organoid model, viral replication assays |
PLoS pathogens |
High |
38935808
|
| 1997 |
B-cell receptor (BCR) stimulation via surface IgM transiently decreases PP1 activity (predominantly PP1α). PP1α undergoes unique phosphorylation changes after BCR stimulation and PMA treatment; PP1α is a better substrate for PKC than PP1γ isoforms, being phosphorylated by PKC at Ser-325 in its C-terminal region. PP1δ does not contain this phosphorylation site. This suggests PP1α is specifically involved in BCR signal transduction via PKC-mediated phosphorylation. |
Phosphatase activity assay, 2D electrophoresis/western blot, in vitro PKC phosphorylation assay with C-terminal peptides, subcellular distribution analysis |
Journal of biochemistry |
Medium |
9399575
|
| 2025 |
NY-ESO-1 acts as a scaffold to recruit deubiquitinase OTUB1 to PP1α (PPP1CA), forming a ternary complex that prevents PP1α polyubiquitination and promotes its stability. OTUB1 deubiquitinase catalytic activity (not its E2-suppressing function) is required to stabilize PP1α. Accumulated PP1α then activates downstream ERK1/2 to promote anoikis resistance and tumor metastasis. Knockdown of PP1α antagonizes NY-ESO-1-mediated anoikis resistance. |
Co-immunoprecipitation, ubiquitination assays, OTUB1 catalytic mutants, PP1α knockdown, soft agar colony formation, lung metastasis mouse model |
Cell death & disease |
Medium |
41053024
|
| 2025 |
IIIG9 (PP1R32) forms a protein complex with PP1α (PPP1CA) at adherens junctions and cilia in polarized ependymal and MDCK cells. FRET analysis confirmed high-efficiency interaction between IIIG9 and PP1α in the cytoplasm and near the plasma membrane. The IIIG9-PP1α interaction at adherens junctions is proposed to regulate cell polarity. |
RT-qPCR with laser microdissection, confocal co-localization, FRET analysis, proximity ligation assay (PLA), co-immunoprecipitation |
Fluids and barriers of the CNS |
Medium |
41566508
|
| 2025 |
PP1A removes activation-loop phosphorylation from AMPK (α-subunit) while AMPK autophosphorylation sites remain protected, establishing an asymmetric phosphatase control that creates persistent regulatory states in kinase activation. |
Hybrid precision mass spectrometry (intact mass + bottom-up + top-down MS), in vitro phosphatase competition assay |
bioRxiv preprintpreprint |
Medium |
bio_10.1101_2025.10.10.681638
|
| 2025 |
PPP1CA interacts with YAP1 and dephosphorylates it, inducing YAP1 nuclear translocation and activation of Hippo pathway target oncogenes in hepatocellular carcinoma. PPP1CA knockdown combined with YAP1 inhibitors synergistically suppresses HCC tumor growth in vivo. |
Co-immunoprecipitation, phospho-YAP western blot, nuclear fractionation, xenograft mouse model, synergy assay with YAP1 inhibitors |
Cellular signalling |
Medium |
40513845
|
| 2025 |
PP1A (PPP1CA) inhibits ferroptosis in hepatocellular carcinoma cells by dephosphorylating Keap1 at site 104 (S104), which disrupts Keap1-Nrf2 interaction and enhances transcription of ferroptosis-related markers and immune checkpoint PD-L1. PP1A knockdown alleviates T cell exhaustion and improves the efficacy of Lenvatinib plus immune checkpoint inhibitor combination therapy. |
Transcriptomic analysis, ferroptosis metabolite profiling (ROS, Fe2+, lipid-ROS, GSH), PP1A knockdown, Keap1 phosphorylation western blot, single-cell sequencing, co-culture T cell assays, in vivo tumor models |
Advanced science |
Medium |
40344394
|