Affinage

CRIP1

Cysteine-rich protein 1 · UniProt P50238

Length
77 aa
Mass
8.5 kDa
Annotated
2026-06-09
40 papers in source corpus 21 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

CRIP1 is a compact double-zinc-finger LIM-domain protein, structurally organized into N-terminal CCHC and C-terminal CCCC zinc modules that pack into a single folded unit (PMID:8632452), and it functions as a multifunctional signaling scaffold that couples post-translational modification of partner proteins to transcriptional and metabolic reprogramming, predominantly characterized in cancer contexts. A recurrent theme is its control of protein turnover through E3 ligase and deubiquitinase machinery: CRIP1 bridges the E3 ligase STUB1 to BBOX1 to drive BBOX1 ubiquitination and degradation, lowering carnitine and acetylcarnitine to reduce β-catenin acetylation and promote its nuclear accumulation (PMID:35775648), recruits UBE3A to ubiquitinate MFGE8 to activate NF-κB-driven matrix degradation (PMID:41067282), and assembles a USP7/PA200 complex that stabilizes PA200 to co-regulate proteasome activity and autophagy (PMID:38199044). CRIP1 also acts as a direct binding partner of NF-κB/p65, facilitating importin-dependent nuclear translocation and transcription of chemokines including CXCL1, CXCL5 and CXCL12 that shape an immunosuppressive tumor microenvironment (PMID:37541772, PMID:41854522). In DNA repair, CRIP1 binds the RAD51 core domain together with BRCA2 and enables KPNA4-mediated nuclear import to promote homologous recombination (PMID:34262130). CRIP1 activity is tuned by site-specific modification — PRMT5 and PRMT1 deposit distinct arginine methylations that differentially engage Wnt/β-catenin versus p38 signaling (PMID:41079921), and MOF-mediated K49 lactylation lets CRIP1 sequester p21 from CDK2 to drive cell-cycle progression (PMID:42258744). Across multiple settings CRIP1 modulates the Wnt/β-catenin axis (PMID:29959029, PMID:37224580) and constrains metabolic reprogramming, suppressing glycolysis (PMID:41670839, PMID:41986400) and TFAM-dependent mitochondrial biogenesis (PMID:39905216).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1996 High

    Established the physical architecture of CRIP1 as a two-module zinc-binding LIM protein, defining the structural basis for its later scaffolding roles.

    Evidence NMR solution structure with NOE-derived restraints and zinc coordination analysis of rat CRIP

    PMID:8632452

    Open questions at the time
    • Structure alone does not reveal protein partners or cellular function
    • No mapping of which surfaces mediate protein-protein interactions
  2. 1992 Low

    Initial functional hypothesis framed CRIP as an intestinal zinc transport protein, raising the question of whether zinc binding is structural or transport-related.

    Evidence Biochemical zinc-binding observations in intestinal mucosa (narrative review)

    PMID:1407754

    Open questions at the time
    • Single narrative review without detailed methodology
    • Transport function not reconciled with later signaling/scaffold roles
  3. 2002 Medium

    Linked CRIP1 to immune regulation by showing overexpression shifts cytokine balance toward a Th2 profile, the first in vivo functional consequence.

    Evidence Transgenic mouse overexpression with LPS/mitogen challenge and influenza infection

    PMID:12006348

    Open questions at the time
    • Molecular mediators of the cytokine shift not identified
    • No mechanistic link to a defined signaling pathway
  4. 2008 Medium

    Placed the CRIP ortholog in a CDC-42/GEF cytoskeletal pathway, suggesting a conserved role in apical cytoskeletal organization of polarized epithelia.

    Evidence Genetic cloning and epistasis of exc-9 with exc-5 in C. elegans tubule morphology

    PMID:18384766

    Open questions at the time
    • Direct molecular partners of EXC-9 not defined
    • Relevance to mammalian CRIP1 cytoskeletal function untested
  5. 2013 Medium

    Defined CRIP1 as a negative regulator of MAPK/Akt signaling and proliferation in breast cancer, establishing a tumor-suppressive activity in some contexts.

    Evidence siRNA knockdown with immunoblotting, proliferation and invasion assays in T47D and BT474 cells

    PMID:23570421

    Open questions at the time
    • Direct molecular target within MAPK/Akt pathway not identified
    • Mechanism of cdc2 dephosphorylation unresolved
  6. 2018 Medium

    Identified CRIP1 as an activator of Wnt/β-catenin signaling driving EMT, an apparently opposite role to its breast-cancer suppression, indicating context-dependent function.

    Evidence Gain/loss-of-function with EMT and Wnt marker immunoblotting, migration/invasion assays in cervical cancer

    PMID:29959029

    Open questions at the time
    • Direct mechanism of Wnt pathway engagement not shown
    • No partner protein identified at this stage
  7. 2021 High

    Resolved a direct molecular mechanism by which CRIP1 promotes homologous recombination, binding the RAD51 core domain with BRCA2 and enabling nuclear import.

    Evidence Co-IP, MS, domain mapping, KPNA4-dependent import imaging, drug sensitivity assays

    PMID:34262130

    Open questions at the time
    • Structural basis of the CRIP1-RAD51-BRCA2 complex not solved
    • How AKT-driven deubiquitination of CRIP1 is regulated unclear
  8. 2022 High

    Established CRIP1 as an adaptor that bridges an E3 ligase to a substrate, linking BBOX1 degradation through carnitine metabolism to β-catenin nuclear accumulation.

    Evidence Co-IP, ubiquitination/degradation assays, BBOX1 K240 mutagenesis, acetylation and β-catenin localization assays

    PMID:35775648

    Open questions at the time
    • Whether CRIP1 directs STUB1 to other substrates unknown
    • Quantitative contribution of carnitine vs other inputs to β-catenin acetylation not defined
  9. 2023 High

    Defined CRIP1 as a direct NF-κB/p65 binding partner that drives chemokine transcription and immunosuppression, connecting it to the tumor immune microenvironment.

    Evidence Reciprocal Co-IP, RNA-seq, ChIP, orthotopic allograft, flow cytometry in PDAC

    PMID:37541772

    Open questions at the time
    • Whether CRIP1 modifies p65 or merely chaperones it unresolved
    • Mapping of the CRIP1-p65 interaction interface absent
  10. 2023 Medium

    Reinforced a Wnt/β-catenin role in AML by positioning CRIP1 upstream of axin1, with pharmacological rescue establishing pathway epistasis.

    Evidence shRNA knockdown, immunoblotting, SKL2001 rescue, growth/migration assays in U937 and THP1

    PMID:37224580

    Open questions at the time
    • Direct molecular link between CRIP1 and axin1 not shown
    • Mechanism of axin1 upregulation upon CRIP1 loss unknown
  11. 2024 High

    Showed CRIP1 scaffolds a USP7/PA200 complex to dually regulate proteasome activity and autophagy, extending its role in protein homeostasis.

    Evidence TAP/MS, Co-IP, proteasome activity and autophagy assays, xenograft in multiple myeloma

    PMID:38199044

    Open questions at the time
    • Stoichiometry and assembly order of the complex undefined
    • How CRIP1 selects USP7 substrates beyond PA200 unknown
  12. 2024 Medium

    Identified CRIP1 as a suppressor of glycolytic reprogramming in AML, linking it to metabolic control of leukemic cells.

    Evidence shRNA knockdown with glucose/lactate assays, LDHA immunoblotting, 2-DG sensitivity across two papers

    PMID:41670839 PMID:41986400

    Open questions at the time
    • Direct molecular target controlling LDHA/glycolysis not defined
    • Connection to CRIP1's other pathways unestablished
  13. 2025 Medium

    Revealed that arginine methylation by PRMT5 and PRMT1 at distinct residues acts as a molecular switch routing CRIP1 toward Wnt/β-catenin or p38 signaling to drive tumor recurrence.

    Evidence Site-specific mutagenesis (R16/R26/R68), pathway reporters, PRMT inhibitors in senescent SCLC

    PMID:41079921

    Open questions at the time
    • How methylation alters CRIP1 partner binding mechanistically unclear
    • Single-lab finding without independent confirmation
  14. 2025 High

    Demonstrated MOF-mediated K49 lactylation lets CRIP1 sequester p21 from CDK2, providing a metabolite-sensing route to cell-cycle progression validated in vivo.

    Evidence Lactylation assays, K49R mutagenesis, CRIP1-p21-CDK2 Co-IP, AAV rescue in arthritis mouse models

    PMID:42258744

    Open questions at the time
    • Whether lactylation affects CRIP1's other interactions untested
    • Structural basis of p21 sequestration not resolved
  15. 2025 Medium

    Extended CRIP1's E3-recruiting adaptor role to UBE3A-mediated MFGE8 degradation, linking it to NF-κB activation and matrix degradation in osteoarthritis.

    Evidence IP/MS, Co-IP, proteasome inhibitor rescue, KD/OE in chondrocytes and OA mouse model

    PMID:41067282

    Open questions at the time
    • Whether CRIP1 directs UBE3A to additional substrates unknown
    • Direct binding interfaces not mapped
  16. 2025 Medium

    Connected CRIP1 to transcriptional control of lipogenesis and ER stress by promoting NFATC2 occupancy at the SREBF1 promoter in melanoma.

    Evidence RNA-seq, ChIP, dual-luciferase reporter, ROS measurement, pharmacological rescue, xenograft

    PMID:42134671

    Open questions at the time
    • Whether CRIP1 directly contacts NFATC2 or chromatin unclear
    • Single-lab study
  17. 2025 Medium

    Identified CRIP1 as a suppressor of TFAM-mediated mitochondrial biogenesis, complementing its glycolytic-suppression role in metabolic regulation.

    Evidence Gain/loss-of-function lines, OCR, mtDNA and ATP assays, TFAM immunoblotting in melanoma

    PMID:39905216

    Open questions at the time
    • No direct CRIP1-TFAM binding shown
    • Mechanism of TFAM protein-level suppression unresolved
  18. 2025 Low

    A preprint links CRIP1 to amyloid pathology, with recombinant CRIP1 accelerating Aβ fibril formation in vitro.

    Evidence In vitro Aβ-binding and fibril kinetics assays with recombinant CRIP1 (preprint)

    PMID:bio_10.1101_2025.10.08.25337413

    Open questions at the time
    • Single in vitro assay from a preprint, not independently replicated
    • No cellular or in vivo validation of the Aβ interaction

Open questions

Synthesis pass · forward-looking unresolved questions
  • How CRIP1's single LIM-domain scaffold selects among its many reported partners (NF-κB, RAD51/BRCA2, STUB1/BBOX1, USP7/PA200, UBE3A) and how this is governed by its post-translational modifications across cell types remains unresolved.
  • No unifying structural model of CRIP1-partner selectivity
  • Modification-dependent interactome not systematically mapped
  • Reconciliation of tumor-suppressive vs oncogenic roles across tissues incomplete

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0098772 molecular function regulator activity 2 GO:0140110 transcription regulator activity 2
Localization
GO:0005634 nucleus 2 GO:0005829 cytosol 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-392499 Metabolism of proteins 3 R-HSA-168256 Immune System 2 R-HSA-1640170 Cell Cycle 1 R-HSA-73894 DNA Repair 1
Partners
BBOX1BRCA2PA200RAD51RELASTUB1UBE3AUSP7
Complex memberships
CRIP1-BRCA2-RAD51 complexCRIP1/USP7/PA200 complex

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 CRIP1 (rat CRIP) is a 76-residue LIM-domain protein that binds two equivalents of zinc, forming N-terminal CCHC (Cys3, Cys6, His24, Cys27) and C-terminal CCCC (Cys30, Cys33, Cys51, Cys55) modules. The modules pack via hydrophobic interactions forming a compact structure; CCHC and CCCC modules each contain two orthogonally-arrayed antiparallel beta-sheets with a C-terminal alpha-helix. NMR spectroscopy (homonuclear and 1H-15N heteronuclear), 500 NOE-derived distance restraints, J-coupling and proton chemical shift analysis Journal of molecular biology High 8632452
1992 CRIP1 binds zinc in intestinal mucosa during absorption and functions as an intestinal zinc transport protein; high dietary zinc does not affect CRIP concentration but greatly increases metallothionein, which may compete with CRIP to decrease zinc absorption. Biochemical zinc-binding assays in intestinal mucosa Nutrition reviews Low 1407754
2002 Transgenic mice overexpressing rat CRIP show altered cytokine patterns: reduced IFN-gamma and IL-2, and elevated IL-6 and IL-10, upon LPS challenge or mitogen stimulation, indicating CRIP operates in a cellular pathway that shifts cytokine balance toward Th2; CRIP overexpression also caused delayed viral clearance after influenza infection. Transgenic mouse model with LPS challenge, mitogen stimulation of splenocytes, delayed-type hypersensitivity assay, influenza infection model American journal of physiology. Endocrinology and metabolism Medium 12006348
2008 In C. elegans, CRIP homologues (EXC-9 and a second paralogue) maintain apical cytoskeletal flexibility in polarized epithelial cells to regulate tubule diameter; EXC-9 shows genetic interaction with the EXC-5 guanine exchange factor that regulates CDC-42 activity, placing CRIP in a CDC-42/GEF pathway controlling cytoskeletal organization. Genetic cloning of exc-9, epistasis analysis with exc-5 and other exc genes in C. elegans, tubule morphology phenotype analysis Developmental biology Medium 18384766
2013 CRIP1 knockdown in T47D and BT474 breast cancer cells increased phosphorylation of MAPK and Akt, reduced phosphorylation of cdc2, and significantly elevated cell proliferation and invasion in vitro, indicating CRIP1 negatively regulates MAPK/Akt signaling and cell cycle progression. siRNA knockdown, immunoblotting, WST-1 proliferation assay, invasion assay Molecular cancer Medium 23570421
2018 CRIP1 overexpression in cervical cancer cells promotes migration, invasion, and epithelial-mesenchymal transition by activating the Wnt/β-catenin signaling pathway, increasing protein levels of c-myc, cyclin D1, and cytoplasmic β-catenin. Transient transfection overexpression and siRNA knockdown, western blot for EMT markers and Wnt pathway components, migration/invasion assays, immunohistochemistry Life sciences Medium 29959029
2021 CRIP1 promotes homologous recombination (HR) DNA repair by: (1) stabilizing BRCA2 to counteract FBXO5-targeted RAD51 degradation; (2) binding directly to the RAD51 core domain (residues 184–257) in coordination with BRCA2 to facilitate masking of the RAD51 nuclear export signal; and (3) enabling KPNA4-mediated nuclear import of the CRIP1-BRCA2-RAD51 complex. Upon DNA damage, CRIP1 is deubiquitinated and upregulated by activated AKT signaling. Co-immunoprecipitation, mass spectrometry screening, siRNA knockdown, domain mapping, cisplatin/epirubicin/olaparib sensitivity assays, RAD51 nuclear enrichment imaging Oncogene High 34262130
2022 CRIP1 interacts with the E3 ligase STUB1 and BBOX1, promoting BBOX1 ubiquitination at lysine 240 and proteasomal degradation, thereby reducing carnitine levels. Reduced acetylcarnitine decreases β-catenin acetylation and promotes nuclear accumulation of β-catenin, facilitating cancer stem-like properties in hepatocellular carcinoma. Co-immunoprecipitation, ubiquitination assay, proteasomal degradation assay, BBOX1 K240 mutagenesis, acetylation analysis, β-catenin nuclear localization assay The EMBO journal High 35775648
2023 CRIP1 binds to NF-κB/p65 and facilitates its nuclear translocation in an importin-dependent manner in pancreatic ductal adenocarcinoma cells, leading to transcriptional activation of CXCL1 and CXCL5, which promote chemotactic migration of myeloid-derived suppressor cells and immunosuppression. Co-immunoprecipitation, RNA sequencing, mass spectrometry, chromatin immunoprecipitation, orthotopic allograft model, flow cytometry, multiplexed imaging Gut High 37541772
2023 CRIP1 silencing in AML (U937 and THP1) cells causes inactivation of the Wnt/β-catenin pathway through upregulation of axin1 protein, and the Wnt/β-catenin agonist SKL2001 rescues the growth and migration defects induced by CRIP1 knockdown, placing CRIP1 upstream of axin1/β-catenin in AML. Lentiviral shRNA knockdown, western blot, pharmacological rescue with SKL2001, growth/migration/colony assays, cell cycle analysis Leukemia research Medium 37224580
2024 CRIP1 simultaneously binds deubiquitinase USP7 and proteasome coactivator PA200, forming a CRIP1/USP7/PA200 complex. CRIP1 promotes proteasome activity and autophagosome maturation by facilitating USP7-mediated deubiquitination and stabilization of PA200, thereby dually regulating protein homeostasis in multiple myeloma cells. Co-immunoprecipitation with tandem affinity purification/mass spectrometry (TAP/MS), RNA-seq, proteasome activity assay, autophagy assay, xenograft model EBioMedicine High 38199044
2023 Single-cell RNA sequencing of human fetal epicardium identified CRIP1 as a regulator of epicardial epithelial-to-mesenchymal transition (EMT), with expression distinguishing epithelial from mesenchymal subpopulations. Single-cell RNA sequencing of isolated human fetal epicardium, population-specific marker analysis Stem cell reports Low 37390825
2025 PRMT5-mediated symmetric dimethylation of CRIP1 at R26/R68 activates the Wnt/β-catenin pathway to promote stemness in senescent SCLC cells post-chemotherapy; subsequently, PRMT1-mediated asymmetric dimethylation of CRIP1 at R16 suppresses the p38 pathway to accelerate proliferation of stem-like cells and drive rapid tumor recurrence. Arginine methylation assays, site-specific mutagenesis (R16, R26, R68), Wnt/β-catenin and p38 pathway reporter/immunoblot assays, PRMT1/PRMT5 inhibitor treatments, PELI1 E3 ligase regulation of PRMTs International journal of biological sciences Medium 41079921
2025 CRIP1 recruits the E3 ubiquitin ligase UBE3A to MFGE8 in chondrocytes, promoting MFGE8 ubiquitination and proteasomal degradation, which activates the NF-κB pathway (p65 phosphorylation) and drives ECM degradation in osteoarthritis. Immunoprecipitation/mass spectrometry, label-free quantitative proteomics, Co-IP, proteasome inhibitor rescue, CRIP1 KD/OE in primary chondrocytes and OA mouse model Biochemical pharmacology Medium 41067282
2025 CRIP1 undergoes MOF-mediated lactylation at K49 in rheumatoid arthritis synovial fibroblasts. Lactylated CRIP1 binds and sequesters the cell-cycle inhibitor p21 away from CDK2, facilitating G1/S cell cycle transition and synovial proliferation. AAV delivery of a K49R lactylation-deficient CRIP1 mutant significantly reduced synovial proliferation. Protein lactylation assays, MOF writer identification, K49R mutagenesis, co-immunoprecipitation of CRIP1-p21-CDK2, AAV gene delivery, CIA and humanized NSG mouse models JCI insight High 42258744
2026 In triple-negative breast cancer, macrophage-expressed HTRA1 associates with CRIP1 to facilitate CRIP1 binding to NF-κB, activating downstream CXCL12 transcription; this leads to T-cell egress from tumors and limits immunotherapy efficacy. Co-immunoprecipitation (HTRA1-CRIP1-NF-κB), single-cell and spatial transcriptomics, macrophage-specific Htra1 knockout mouse model, pharmacological CXCL12/CXCR4 blockade Cancer immunology research Medium 41854522
2025 CRIP1 promotes NFATC2 binding to the SREBF1 promoter, driving SREBF1 transcription; elevated SREBF1 increases intracellular ROS levels, thereby activating endoplasmic reticulum stress and promoting malignant phenotypes in melanoma cells. RNA sequencing, chromatin immunoprecipitation (ChIP), dual-luciferase reporter, western blot, ROS measurement, 4-PBA/NAC pharmacological intervention, xenograft model Biochemical pharmacology Medium 42134671
2025 CRIP1 inhibits mitochondrial biogenesis in melanoma cells by suppressing the protein levels of TFAM (mitochondrial transcription factor A), reducing mitochondrial DNA copy number, ATP production, respiratory capacity, and oxidative phosphorylation protein expression. CRIP1 overexpression and knockdown stable lines, western blot, immunofluorescence, OCR (oxygen consumption rate), mitochondrial DNA assay, cytosolic ATP assay Scientific reports Medium 39905216
2025 In vitro, recombinant CRIP1 bound Aβ peptide and accelerated amyloid fibril formation, providing a mechanistic link between CRIP1 and vascular amyloid pathology in cerebral amyloid angiopathy. In vitro Aβ-binding assay and fibril formation kinetics assay with recombinant CRIP1 bioRxivpreprint Low bio_10.1101_2025.10.08.25337413
2024 CRIP1 knockdown in AML cells (OCI-AML3) increases glucose uptake, lactate production, and LDHA protein expression, indicating CRIP1 normally suppresses glycolytic reprogramming. CRIP1-deficient cells show enhanced sensitivity to the glycolytic inhibitor 2-DG. Lentiviral shRNA knockdown, glucose consumption assay, lactate secretion assay, western blot (LDHA, HK2, MCL1), flow cytometry cell death assay Molecular biology reports / Scientific reports Medium 41670839 41986400

Source papers

Stage 0 corpus · 40 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 Hypomethylation of WNT5A, CRIP1 and S100P in prostate cancer. Oncogene 117 17486081
2007 CB1 cannabinoid receptor activity is modulated by the cannabinoid receptor interacting protein CRIP 1a. Molecular pharmacology 112 17895407
2023 CRIP1 fosters MDSC trafficking and resets tumour microenvironment via facilitating NF-κB/p65 nuclear translocation in pancreatic ductal adenocarcinoma. Gut 92 37541772
2019 CRIP: predicting circRNA-RBP-binding sites using a codon-based encoding and hybrid deep neural networks. RNA (New York, N.Y.) 73 31537716
1996 Structure of the cysteine-rich intestinal protein, CRIP. Journal of molecular biology 55 8632452
2022 CRIP1 suppresses BBOX1-mediated carnitine metabolism to promote stemness in hepatocellular carcinoma. The EMBO journal 54 35775648
2008 Identification and rational redesign of peptide ligands to CRIP1, a novel biomarker for cancers. PLoS computational biology 49 18670594
2013 The impact of cysteine-rich intestinal protein 1 (CRIP1) in human breast cancer. Molecular cancer 46 23570421
2002 Overexpression of CRIP in transgenic mice alters cytokine patterns and the immune response. American journal of physiology. Endocrinology and metabolism 43 12006348
2018 CRIP1 promotes cell migration, invasion and epithelial-mesenchymal transition of cervical cancer by activating the Wnt/β‑catenin signaling pathway. Life sciences 38 29959029
2021 CRIP1 cooperates with BRCA2 to drive the nuclear enrichment of RAD51 and to facilitate homologous repair upon DNA damage induced by chemotherapy. Oncogene 31 34262130
2011 CRIP1 expression is correlated with a favorable outcome and less metastases in osteosarcoma patients. Oncotarget 30 22202598
1995 Activation of Moloney murine leukemia virus LTR enhances the titer of recombinant retrovirus in psi CRIP packaging cells. Gene therapy 21 8593605
2024 CRIP1 involves the pathogenesis of multiple myeloma via dual-regulation of proteasome and autophagy. EBioMedicine 19 38199044
2008 CRIP homologues maintain apical cytoskeleton to regulate tubule size in C. elegans. Developmental biology 19 18384766
2019 Genome-wide identification of AGO18b-bound miRNAs and phasiRNAs in maize by cRIP-seq. BMC genomics 18 31419938
2017 The Impact of Cysteine-Rich Intestinal Protein 1 (CRIP1) on Thyroid Carcinoma. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 16 29059670
2013 Combining peptide and DNA for protein assay: CRIP1 detection for breast cancer staging. ACS applied materials & interfaces 13 24328073
1998 Mapping of the human cysteine-rich intestinal protein gene CRIP1 to the human chromosomal segment 7q11.23. Genomics 13 9480758
2023 CRIP1 supports the growth and migration of AML-M5 subtype cells by activating Wnt/β-catenin pathway. Leukemia research 10 37224580
2023 Single-cell analysis of human fetal epicardium reveals its cellular composition and identifies CRIP1 as a modulator of EMT. Stem cell reports 9 37390825
2021 CRIP1 expression in monocytes related to hypertension. Clinical science (London, England : 1979) 9 33782695
2016 CRIP1, a novel immune-related protein, activated by Enterococcus faecalis in porcine gastrointestinal epithelial cells. Gene 9 27836662
2014 Comparative expression analysis of cysteine-rich intestinal protein family members crip1, 2 and 3 during Xenopus laevis embryogenesis. The International journal of developmental biology 9 26154325
1992 Cysteine-rich intestinal protein (CRIP): a new intestinal zinc transport protein. Nutrition reviews 7 1407754
2022 Comprehensive Analysis of CRIP1 Expression in Acute Myeloid Leukemia. Frontiers in genetics 6 35938037
2025 CRIP1 inhibits cutaneous melanoma progression through TFAM-mediated mitochondrial biogenesis. Scientific reports 4 39905216
2024 CRIP1 regulates osteogenic differentiation of bone marrow stromal cells and pre-osteoblasts via the Wnt signaling pathway. Biochemical and biophysical research communications 4 38936225
2022 Comprehensive Analysis of CRIP1 in Patients with Ovarian Cancer, including ceRNA Network, Immune-Infiltration Pattern, and Clinical Benefit. Disease markers 4 35140819
2025 PRMT1/PRMT5-Mediated Differential Arginine Methylation of CRIP1 Promotes the Recurrence of Small Cell Lung Cancer after Chemotherapy. International journal of biological sciences 1 41079921
2026 CRIP1 knockdown enhances glycolytic dependence and increases sensitivity to 2-Deoxy-D-Glucose in acute myeloid leukemia. Molecular biology reports 0 41670839
2026 HTRA1+ Macrophages Induce T-cell Egress through CRIP1/NF-κB/CXCL12 to Limit the Effects of Immunotherapy in Triple-Negative Breast Cancer. Cancer immunology research 0 41854522
2026 Molecular insights into CRIP1 as an immunometabolic regulator revealed by CRIP1 knockout and single-cell transcriptomics. Frontiers in immunology 0 41972184
2026 CRIP1 functions as an oncogene in acute myeloid leukemia by modulating glycolytic metabolic reprogramming. Scientific reports 0 41986400
2026 CRIP1 promotes docetaxel resistance and immune-associated cell death modulation in prostate cancer. Frontiers in pharmacology 0 41988531
2026 The CRIP1/NFATC2/SREBF1 axis drives melanoma progression by promoting reactive oxygen species-mediated endoplasmic reticulum stress activation. Biochemical pharmacology 0 42134671
2026 Lactate programs CRIP1 protein lactylation to drive synovial proliferation in rheumatoid arthritis. JCI insight 0 42258744
2025 CRIP1 exacerbates osteoarthritis progression by recruiting UBE3A to induce the ubiquitination-mediated degradation of MFGE8. Biochemical pharmacology 0 41067282
2025 Discovering CRIP1: a novel core gene in osteoarthritis pathogenesis. Hereditas 0 41107987
2011 [The Paris cell for collecting preoccupying information (la CRIP 75): an organization at the heart of child protection]. Archives de pediatrie : organe officiel de la Societe francaise de pediatrie 0 21816589

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