Affinage

BASP1

Brain acid soluble protein 1 · UniProt P80723

Length
227 aa
Mass
22.7 kDa
Annotated
2026-06-09
100 papers in source corpus 44 papers cited in narrative 44 extracted findings
Cross-family judge faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

BASP1 (CAP-23/NAP-22) is an N-terminally myristoylated, intrinsically organized signaling protein that operates in two membrane-linked compartments to control actin-based cell morphology and lipid-dependent transcription (PMID:8193160, PMID:22939983). At the plasma membrane, myristoylation targets BASP1 to cholesterol-rich, detergent-insoluble raft microdomains, where it binds cholesterol, phosphatidylethanolamine, and polyphosphoinositides, self-associates into oligomers, and sequesters PI(4,5)P2 into clustered membrane domains (PMID:8193160, PMID:10409698, PMID:12271466, PMID:12922169, PMID:14989697). Together with the structurally related GAP-43 and MARCKS, BASP1 uses a basic effector domain to promote retention of PI(4,5)P2 and drive subplasmalemmal actin assembly, filopodia, and neurite outgrowth; deletion of the effector domain produces dominant-negative inhibition, and CAP-23/BASP1 knockout mice show defective nerve sprouting that GAP-43 can functionally replace (PMID:9344590, PMID:10871285, PMID:10871284, PMID:18438920). BASP1 is a PKC substrate phosphorylated at Ser5/6, and it binds Ca2+/calmodulin through a novel mode in which its myristoyl group inserts into a hydrophobic tunnel spanning both CaM lobes; phosphorylation or CaM binding regulates its membrane and lipid association (PMID:2148567, PMID:8034714, PMID:10207003, PMID:14765114). In the nucleus, BASP1 is a transcriptional corepressor for the Wilms' tumor protein WT1, co-occupying target promoters and converting WT1 from activator to repressor (PMID:14701728, PMID:19050011). This repression requires both N-terminal myristoylation, which recruits nuclear PIP2 and HDAC1, and a conserved cholesterol-interaction motif that directly delivers cholesterol to promoters; BASP1 cooperates with prohibitin to recruit BRG1, displace CBP, and remodel chromatin, removing active H3K9ac/H3K4me3 marks (lipidation-dependent) and adding repressive H3K27me3 (lipidation-independent) (PMID:22939983, PMID:24166496, PMID:34266955, PMID:35982799). Through these activities BASP1 acts as a tumor suppressor: it inhibits v-Myc transformation by withdrawing calmodulin from v-Myc, represses MYC via interaction with β-catenin and WNT pathway components, and modulates ERα/tamoxifen transcriptional responses (PMID:19297618, PMID:28492543, PMID:31944520, PMID:41785318). In vivo, the WT1-BASP1 complex maintains differentiated cell states, exemplified by adult taste receptor cells where loss of BASP1 de-represses Wnt and Shh target genes (PMID:31167803). BASP1 additionally promotes apoptosis and actin rearrangement in podocytes via WT1/p53 co-repression and participates in inflammatory and migratory programs in myeloid cells (PMID:20110383, PMID:33615732, PMID:37505219, PMID:42149339).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1994 High

    Established the molecular basis of BASP1 membrane association by showing N-terminal myristoylation is necessary for lipid binding, defining the lipid anchor that underlies its membrane functions.

    Evidence Baculovirus/E. coli expression with liposome binding assays comparing myristoylated and non-myristoylated forms

    PMID:8193160

    Open questions at the time
    • Lipid headgroup specificity not yet resolved
    • Did not address nuclear roles
  2. 1999 High

    Defined PKC/calmodulin regulation of BASP1, showing CaM binding requires the myristoyl group plus a basic N-terminal domain and is abolished by Ser5/6 phosphorylation, establishing a switch coupling phosphorylation to lipid/CaM association.

    Evidence In vitro PKC phosphorylation, calmodulin-binding and synthetic peptide assays with myristoylated vs non-myristoylated recombinant protein; earlier PKC substrate mapping

    PMID:10207003 PMID:2148567 PMID:8034714

    Open questions at the time
    • In-cell consequences of the phospho-switch not fully traced
    • Did not establish downstream effectors
  3. 2003 Medium

    Showed BASP1 binds cholesterol-dependent raft domains, protects and clusters them, oligomerizes, and sequesters PI(4,5)P2, defining how it organizes the inner-leaflet lipid environment.

    Evidence Triton fractionation, methyl-β-cyclodextrin extraction, liposome and planar-monolayer assays, analytical ultracentrifugation, AFM, FRET, and TIRFM with labeled PI(4,5)P2

    PMID:10409698 PMID:12271466 PMID:12718518 PMID:12922169 PMID:14989697 PMID:9030206

    Open questions at the time
    • Largely single-lab biophysical reconstitutions
    • In vivo raft clustering not directly imaged
  4. 2000 High

    Connected BASP1 membrane/lipid activity to a cellular function, demonstrating effector-domain-dependent promotion of subplasmalemmal actin, neurite outgrowth, and nerve sprouting, with GAP-43 able to substitute in vivo.

    Evidence Dominant-negative ΔED constructs, PC12 neurite assays, CAP-23 knockout and GAP-43 knockin mice, cytochalasin D phenocopy

    PMID:10871284 PMID:10871285 PMID:10958980 PMID:18438920 PMID:9344590

    Open questions at the time
    • Direct actin-regulatory partner at the cortex not defined
    • Distinction from GAP-43/MARCKS-specific roles incomplete
  5. 2004 High

    Resolved the structural mechanism of BASP1-calmodulin recognition, visualizing the myristoyl group threading a hydrophobic CaM tunnel, a binding mode distinct from canonical CaM targets.

    Evidence X-ray crystallography of myristoylated peptide/Ca2+-CaM complex, supported by SAXS

    PMID:11106163 PMID:14765114

    Open questions at the time
    • Functional consequence of the unusual CaM geometry in cells unaddressed
  6. 2004 High

    Identified BASP1's nuclear function as a WT1 transcriptional corepressor, recasting it from a purely membrane/cytoskeletal protein to a transcriptional regulator co-expressed with WT1 in developing nephron.

    Evidence Co-immunoprecipitation, transcription reporter assays, siRNA knockdown, immunohistochemistry; ChIP at endogenous Bak/c-myc/podocalyxin promoters

    PMID:14701728 PMID:19050011

    Open questions at the time
    • Mechanism of repression not yet defined
    • How a myristoylated protein acts in the nucleus unexplained
  7. 2009 High

    Established BASP1 as a tumor suppressor that inhibits v-Myc transformation, with the basic N-terminal domain required, linking its transcriptional and anti-oncogenic functions.

    Evidence Bicistronic v-myc co-expression, focus formation assays, N-terminal domain mutagenesis, Myc target gene analysis

    PMID:19297618

    Open questions at the time
    • Direct molecular target of inhibition not yet identified in this study
  8. 2013 High

    Defined the lipid-dependent repression mechanism, showing myristoylation recruits nuclear PIP2 and HDAC1, and that prohibitin cooperates with BASP1 to recruit BRG1, displace CBP, and remodel chromatin at WT1 promoters.

    Evidence Myristoylation-deficient mutants, ChIP and PIP2/HDAC1/BRG1/CBP recruitment assays, reciprocal Co-IP

    PMID:22939983 PMID:24166496

    Open questions at the time
    • Stoichiometry of the nuclear lipid-protein complex unresolved
    • How PIP2 is delivered to chromatin not detailed
  9. 2021 High

    Demonstrated a second nuclear lipid requirement: a conserved cholesterol-interaction motif directly recruits cholesterol to WT1 promoters, required for chromatin remodeling and differentiation control.

    Evidence Cholesterol-motif mutagenesis, ChIP for cholesterol, biosynthesis inhibitors, reporter and differentiation assays

    PMID:34266955

    Open questions at the time
    • How chromatin-bound cholesterol mechanistically enforces compaction unclear
  10. 2022 High

    Separated lipidation-dependent from lipidation-independent chromatin effects, showing myristoylation is required to remove active H3K9ac/H3K4me3 but not to deposit repressive H3K27me3.

    Evidence Myristoylation-deficient mutants with ChIP for histone marks, RNA-seq, ATAC-seq, tumor suppressor assays

    PMID:35982799

    Open questions at the time
    • Enzymatic machinery for each branch not fully assigned to BASP1 recruitment
  11. 2026 Medium

    Extended BASP1's tumor-suppressor mechanism across pathways, showing CaM withdrawal from v-Myc, ERα/tamoxifen selectivity, and β-catenin-dependent MYC repression in colorectal cancer.

    Evidence CaM displacement assays, Co-IP with ERα and β-catenin, ChIP at MYC promoter, transcriptome profiling, transformation and tumorigenesis assays

    PMID:21269271 PMID:28492543 PMID:31167803 PMID:31944520 PMID:41785318

    Open questions at the time
    • Whether membrane and nuclear pools execute these separately is unresolved
    • Most contexts established in single labs
  12. 2023 Medium

    Expanded BASP1 into immune and cytoskeletal disease contexts, implicating it in macrophage NLRP3 inflammasome activity, podocyte apoptosis, osteoclastogenesis, glioma chemoresistance, and neutrophil migration/NETs via vimentin.

    Evidence Cell-type-specific conditional knockout mice, knockdown/overexpression, RNA-seq, ChIP, Co-IP with vimentin, and functional disease-model assays

    PMID:20110383 PMID:33508088 PMID:33615732 PMID:33899275 PMID:36961398 PMID:37505219 PMID:37619639 PMID:42149339

    Open questions at the time
    • Whether these phenotypes share a common molecular mechanism is unknown
    • Direct effectors in each context only partially defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How BASP1 partitions between its plasma-membrane lipid-organizing role and its nuclear transcriptional-corepressor role, and what signals govern this compartmental switch, remains unresolved.
  • Trafficking/import mechanism for nuclear BASP1 unknown
  • Regulatory logic coupling membrane lipid binding to chromatin-bound lipid recruitment undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 5 GO:0140110 transcription regulator activity 4 GO:0008092 cytoskeletal protein binding 3 GO:0098772 molecular function regulator activity 3 GO:0060090 molecular adaptor activity 2
Localization
GO:0005886 plasma membrane 5 GO:0005634 nucleus 4 GO:0005856 cytoskeleton 4 GO:0005829 cytosol 2
Pathway
R-HSA-74160 Gene expression (Transcription) 4 R-HSA-1266738 Developmental Biology 3 R-HSA-162582 Signal Transduction 3 R-HSA-4839726 Chromatin organization 3 R-HSA-5357801 Programmed Cell Death 3
Partners
CALM1CAPZCTNNB1ESR1HDAC1PHBSMARCA4WT1
Complex memberships
WT1-BASP1 transcriptional repression complex

Evidence

Reading pass · 44 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 CAP-23 (BASP1) is a substrate for protein kinase C (PKC) in vitro, and is phosphorylated in a PMA-sensitive manner in cultured cells. The PKC phosphorylation site was mapped to Ser-6. The protein is particle-bound/cortical cytoskeleton-associated and contains basic NH2- and COOH-terminal domains. In vitro PKC phosphorylation assay with purified PKC; PMA stimulation of cultured cells; cDNA sequencing and deduced primary structure analysis The Journal of cell biology High 2148567
1994 NAP-22 (BASP1) is an in vitro substrate for PKC; the phosphorylation site is Ser6 (mapped using E. coli-expressed deletion mutants). Calmodulin inhibits PKC-mediated phosphorylation of NAP-22 in a dose-dependent manner, and this inhibition is stronger than for GAP-43. Phosphorylation of NAP-22 by PKC inhibits its association with calmodulin. The dissociation constant for the NAP-22/calmodulin interaction is lower than for GAP-43/calmodulin. In vitro PKC phosphorylation assay; deletion mutant mapping in E. coli; fluorescence spectroscopy with dansyl-labeled calmodulin The Journal of biological chemistry High 8034714
1994 NAP-22 (BASP1) is N-terminally myristoylated (demonstrated in baculovirus expression system), and the myristoylation confers membrane/liposome binding activity. Without myristoylation, the protein does not bind liposomes. Baculovirus expression system; E. coli expression; liposome binding assay Biochimica et biophysica acta High 8193160
1997 NAP-22 (BASP1) and GAP-43 are identified as major protein components of the Triton-insoluble low-density membrane fraction (lipid raft fraction) of rat brain, co-localizing with trimeric G proteins, GPI-anchored proteins (Thy-1, N-CAM-120), and protein tyrosine kinases (src, fyn). Biochemical fractionation (Triton X-100 extraction, density gradient centrifugation); Western blotting Biochimica et biophysica acta Medium 9030206
1997 CAP-23 (BASP1), GAP-43, and MARCKS (GMC) share surface accumulation patterns and cell surface activities when overexpressed: they induce peripheral actin dynamics, filopodia, and blebs. These activities require both acylation-mediated membrane targeting and the GMC-type effector domain sequence. Dominant-negative constructs lacking the effector domain suppress peripheral actin assembly. Transfection/overexpression; deletion/fusion construct analysis; double-label immunocytochemistry; morphological assays in cultured cells Experimental cell research Medium 9344590
1999 CAP-23/NAP-22 (BASP1) binding to calmodulin is directly dependent on N-terminal myristoylation. Only the myristoylated form of recombinant CAP-23/NAP-22 binds calmodulin. The calmodulin-binding site comprises the myristoyl moiety together with a nine-amino-acid N-terminal basic domain. PKC phosphorylation of Ser5 (rat numbering; Ser6 in earlier work) abolishes calmodulin binding. PKC phosphorylation of CAP-23/NAP-22 itself is also myristoylation-dependent. Recombinant myristoylated and non-myristoylated protein production in E. coli; calmodulin-binding assays; synthetic peptide binding assays; PKC phosphorylation assays The Journal of biological chemistry High 10207003
1999 NAP-22 (BASP1) localizes to cholesterol-dependent membrane microdomains (rafts) in neurons. Cholesterol extraction by methyl-β-cyclodextrin solubilizes NAP-22 from rafts. Purified NAP-22 binds liposomes made from phosphatidylcholine and cholesterol in a cholesterol dose-dependent manner. Calmodulin inhibits this lipid binding. Methyl-β-cyclodextrin cholesterol extraction; liposome binding assay; dose-response analysis The Journal of biological chemistry High 10409698
2000 CAP-23 (BASP1), GAP-43, and MARCKS (GMC) accumulate at plasmalemmal rafts where they codistribute with PI(4,5)P2 and promote its retention and clustering. This activity depends on the basic effector domain (ED) of each protein; constructs lacking the ED function as dominant inhibitors. In PC12 cells, these proteins augment NGF- and substrate-induced peripheral actin structures and neurite outgrowth; DeltaED mutants suppress these activities. Dominant-negative GAP43(DeltaED) also interfered with peripheral nerve regeneration and sprouting in transgenic mice. Transfection with full-length and DeltaED constructs; fluorescence imaging; PI(4,5)P2 co-distribution assay; PC12 cell neurite outgrowth assay; transgenic mouse models The Journal of cell biology High 10871285
2000 CAP-23 (BASP1) knockout mice exhibit a pronounced phenotype including defective stimulus-induced nerve sprouting at the adult neuromuscular junction. CAP-23 knockout sensory neurons show striking alterations in neurite outgrowth phenocopied by low-dose cytochalasin D (actin barbed-end capper). GAP-43 can functionally substitute for CAP-23 in vivo (knockin mice expressing GAP-43 instead of CAP-23 are essentially normal). CAP-23 and GAP-43 share roles in promoting subplasmalemmal actin cytoskeleton accumulation. Knockout mouse generation and characterization; transgenic rescue (overexpression of CAP-23 or GAP-43 in adult motoneurons); knockin mouse (GAP-43 replacing CAP-23); cytochalasin D phenocopy; cultured sensory neuron analysis The Journal of cell biology High 10871284
2000 During development of neuronal polarity in cultured hippocampal neurons, NAP-22 (BASP1) is initially distributed evenly among short processes and then sorted preferentially into the axon. NAP-22 colocalizes with the axonal marker tau and with VAMP-2 (synaptic vesicle marker), but not with the dendritic marker MAP-2. In cerebellar granule cells, NAP-22 accumulates in synaptic glomeruli during synapse maturation, suggesting a role in synapse maturation/maintenance rather than initial axon outgrowth. Immunofluorescence of cultured hippocampal neurons at multiple developmental stages; confocal microscopy; co-localization with axonal/dendritic markers Neuroscience research Medium 10958980
2000 The myristoylated N-terminal nonapeptide of CAP-23/NAP-22 binds Ca2+/calmodulin without inducing the compact globular structure seen with other CaM-target complexes. Small-angle X-ray scattering shows that one myr-peptide molecule does not change CaM structure, but two molecules induce a structural change; the complex at saturation retains an extended (not globular) conformation. This indicates a novel mode of CaM-target interaction distinct from canonical non-myristoylated targets. Small-angle X-ray scattering (SAXS); calmodulin-peptide binding assays with myristoylated synthetic peptide Protein science Medium 11106163
2002 NAP-22 (BASP1) binds cholesterol, phosphatidylethanolamine (PE), and polyphosphoinositides in liposome assays. N-terminal myristoylation is essential for liposome binding. The lipid-binding region is within the N-terminal 60 amino acids. In COS7 cells, NAP-22 is recovered in a Triton-insoluble low-density fraction and colocalizes with PE and cholesterol at the membrane. In vitro liposome binding assay with expressed truncation mutants; COS7 cell transfection; subcellular fractionation; immunostaining Journal of neuroscience research Medium 12271466
2003 Native NAP-22 (myristoylated) binds to cholesterol-rich raft-like domains in planar-supported monolayers and remains bound after nonionic detergent extraction; demyristoylated NAP-22 does not bind these domains. NAP-22 protects cholesterol-rich domains during methyl-β-cyclodextrin extraction. The lateral mobility of NAP-22 in model membranes is much lower than other raft components, indicating both cholesterol binding and inter-NAP-22 interactions. Fluorescence microscopy on planar-supported lipid monolayers; nonionic detergent extraction; methyl-β-cyclodextrin treatment; lateral mobility measurement Biochemistry Medium 12718518
2003 NAP-22 self-associates in solution: sedimentation velocity reveals oligomeric forms; myristoylation is required for oligomerization (non-myristoylated form shows no oligomerization). The monomer is highly asymmetric. Sedimentation equilibrium shows reversible monomer-oligomer equilibrium followed by slower, more irreversible larger aggregates. Oligomerization contributes to lipid selectivity during membrane binding. Analytical ultracentrifugation (sedimentation velocity and equilibrium); atomic force microscopy; fluorescence resonance energy transfer Biochimica et biophysica acta Medium 12922169
2004 Crystal structure of myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin was solved. The myristoyl group passes through a hydrophobic tunnel formed by the hydrophobic pockets in both N- and C-terminal domains of CaM. This is a novel mode of CaM-target binding, distinct from canonical non-myristoylated CaM-binding motifs. Several amino-acid residues in addition to the myristoyl group contribute to CaM binding. X-ray crystallography of myristoylated peptide/Ca2+-CaM complex The EMBO journal High 14765114
2004 BASP1 is a transcriptional cosuppressor for the Wilms' tumor suppressor protein WT1. BASP1 and WT1 associate within the nuclei of cells that naturally express both proteins. BASP1 confers WT1 cosuppressor activity in transfection assays. Elimination of endogenous BASP1 by knockdown augments transcriptional activation by WT1. BASP1 is expressed in developing nephron structures and in podocyte cells coincident with WT1. Functional transcription assay; co-immunoprecipitation; siRNA knockdown of endogenous BASP1; immunohistochemistry Molecular and cellular biology High 14701728
2004 A myristoylated N-terminal NAP-22 peptide causes cholesterol-dependent partitioning/sequestering of PI(4,5)P2 into membrane domains in bilayers. This is demonstrated by quenching of fluorescence of BODIPY-TMR-labeled PI(4,5)P2 and by TIRFM. Fluorescence spectroscopy; total internal reflectance fluorescence microscopy (TIRFM) on lipid bilayers The Biochemical journal Medium 14989697
2008 BASP1-induced neurite outgrowth in PC12E2 cells and hippocampal neurons requires N-terminal myristoylation (Gly-1 mutation abolishes the effect), but is independent of Ser-5 phosphorylation. BASP1-induced neurite outgrowth is additive with NCAM-mediated outgrowth and is not inhibited by dominant-negative constructs of FGFR, Src-family kinases, PKC, GSK3β, spectrin, or tau (which do inhibit NCAM-mediated outgrowth). Co-expression experiments demonstrate BASP1 and GAP-43 can substitute for each other in NCAM-independent outgrowth, but BASP1 cannot substitute for GAP-43 in NCAM-mediated outgrowth. PC12E2 cell and primary hippocampal neuron transfection; site-directed mutagenesis (Gly1, Ser5 mutations); dominant-negative co-expression; morphometric neurite analysis Journal of neuroscience research High 18438920
2008 During apoptosis, BASP1 (hBASP1) translocates from the nucleus to the cytoplasm in a caspase-dependent manner. A monoclonal antibody (9B1) preferentially labels the cytoplasmic form of BASP1 in apoptotic cells, not the nuclear form in normal cells. Novel monoclonal antibody generation; LC/MS/MS identification; immunostaining of apoptotic cells; caspase inhibitor experiments Biochemical and biophysical research communications Medium 18457665
2009 BASP1 inhibits v-myc-induced cell transformation. The BASP1 gene is specifically suppressed by the v-myc oncogene (not by other oncogenic agents). Bicistronic co-expression of BASP1 with v-myc blocks transformation. Ectopic BASP1 expression renders fibroblasts resistant to v-myc transformation and attenuates the transformed phenotype of v-myc-transformed cells. BASP1 inhibition of v-myc also prevents transcriptional activation or repression of known Myc target genes. Mutational analysis shows the basic N-terminal domain (myristoylation site, calmodulin-binding domain, putative NLS) is essential for the inhibitory function. Retroviral bicistronic co-expression; ectopic BASP1 expression; N-terminal domain mutagenesis; focus formation assay; Myc target gene expression analysis Proceedings of the National Academy of Sciences of the United States of America High 19297618
2009 NAP-22 (BASP1) interacts directly with the actin-capping protein CapZ in a pull-down assay; bacterially expressed (non-myristoylated) NAP-22 also binds CapZ, indicating the N-terminal myristoyl group is not required for this interaction. NAP-22 binding shows no effect on the actin nucleation activity of CapZ in centrifugation and viscometric assays. Pull-down assay with NAP-22-Sepharose; mass spectrometry identification; Western blotting; E. coli recombinant protein binding; actin nucleation assay Journal of neuroscience research Medium 19267422
2008 WT1 and BASP1 both occupy the promoters of Bak, c-myc, and podocalyxin genes in podocyte precursor cells (demonstrated by ChIP). During differentiation-induced upregulation of podocalyxin, BASP1 promoter occupancy is reduced relative to WT1. Repressive WT1/BASP1 co-occupancy of c-myc and Bak promoters is maintained during differentiation, and these genes are downregulated. BASP1 promoter occupancy is regulated by BASP1 sumoylation. Chromatin immunoprecipitation (ChIP); podocyte precursor cell differentiation model; gene expression analysis; SUMO modification assay Nucleic acids research High 19050011
2010 BASP1 promotes apoptosis in diabetic nephropathy tubular cells. Overexpression of BASP1 induces cell death with apoptotic features; siRNA-mediated BASP1 knockdown protects tubular cells from apoptosis. In apoptotic cells, BASP1 colocalizes with actin at the cell periphery (in contrast to cytoplasmic localization in normal cells). BASP1 cDNA overexpression; siRNA knockdown; flow cytometry for apoptosis; confocal microscopy for subcellular localization Journal of the American Society of Nephrology Medium 20110383
2011 WT1 and BASP1 together redirect K562 myelogenous leukemia cell differentiation: co-expression of WT1 and BASP1 diverts the PMA-induced differentiation programme to a neuronal-like morphology with extensive arborization and expression of neurite outgrowth/synapse formation genes. BASP1 is recruited to WT1-binding sites and suppresses WT1-mediated transcriptional activation at multiple WT1 target genes. Cells acquire functional response to the neurotransmitter ATP. Stable cell line co-expression; ChIP; gene expression profiling; morphological analysis; ATP response functional assay The Biochemical journal Medium 21269271
2011 NAP-22 (BASP1) interacts with synaptojanin-1 in a pull-down assay confirmed by LC-MS/MS and Western blotting. NAP-22 inhibits the phosphatase activity of synaptojanin-1 in a dose-dependent manner. The inhibitory region for 5-phosphatase and the PIP2-binding region in NAP-22 overlap, suggesting NAP-22 competes with PIP2 for synaptojanin-1. Pull-down assay with brain-derived NAP-22-Sepharose; LC-MS/MS identification; Western blotting; in vitro phosphatase activity assay Journal of neuroscience research Medium 21932368
2012 Transcriptional repression by the WT1-BASP1 complex requires N-terminal myristoylation of BASP1. Myristoylated BASP1 binds to nuclear PIP2, which is recruited to the promoter regions of WT1-dependent target genes. BASP1 myristoylation and PIP2 association are required for BASP1's interaction with HDAC1, which is recruited to the promoter to mediate transcriptional repression. Myristoylation-deficient BASP1 mutant analysis; chromatin immunoprecipitation; PIP2 co-immunoprecipitation; HDAC1 recruitment assay; transcription reporter assay Cell reports High 22939983
2013 Prohibitin is part of the WT1-BASP1 transcriptional repression complex. Prohibitin interacts with BASP1, colocalizes with BASP1 in the nucleus, and is recruited to the promoter regions of WT1 target genes in a BASP1-dependent manner. Prohibitin and BASP1 cooperate to recruit the chromatin remodeling factor BRG1 to WT1-responsive promoters, causing dissociation of CBP. Prohibitin also cooperates with BASP1 for PIP2 and HDAC1 recruitment to WT1 target gene promoters. Co-immunoprecipitation; nuclear co-localization (immunofluorescence); ChIP; BRG1 and CBP recruitment assays; HDAC1/PIP2 ChIP Oncogene High 24166496
2013 NAP-22 (BASP1) interacts directly with glutamic acid decarboxylase (GAD65 and GAD67) in a pull-down assay confirmed by LC-MS/MS and Western blotting. Interaction was confirmed in vitro with bacterially expressed GST-GAD65 and GST-GAD67. NAP-22 shows partial co-localization with GAD65 and GAD67 in cultured neurons. Binding of NAP-22 has no effect on the enzymatic activity of GAD65 or GAD67. Pull-down assay; LC-MS/MS; Western blotting; GST fusion protein binding assay; immunofluorescence co-localization; GAD enzymatic activity assay Neuroscience letters Medium 23376695
2014 BASP1 interacts with the abrin A chain (ribosome-inactivating toxin subunit) and sequesters it to the cell nucleus, reducing the toxin's ability to inhibit protein synthesis. Nuclear localization of the abrin A chain is dependent on BASP1 expression levels. Cells with higher BASP1 expression show increased nuclear A chain and greater resistance to abrin toxicity. Co-immunoprecipitation; subcellular fractionation; protein synthesis inhibition assay; BASP1-variable cell line comparison; siRNA and overexpression The Biochemical journal Medium 24350992
2017 BASP1 interacts with oestrogen receptor α (ERα); this interaction is enhanced by tamoxifen in breast cancer cells. BASP1 acts as a major selectivity factor for tamoxifen transcriptional response: 40% of tamoxifen-regulated genes are BASP1-dependent, including several genes associated with tamoxifen resistance. BASP1 elicits tumour-suppressor activity in breast cancer cells and enhances antitumourigenic effects of tamoxifen. Co-immunoprecipitation of BASP1 and ERα; tamoxifen treatment; siRNA knockdown of BASP1; transcriptome analysis; cell viability/proliferation assays Cell death & disease Medium 28492543
2018 NAP-22 (BASP1) interacts with dynamin I in an affinity screening pull-down. NAP-22 (bacterially expressed) partially inhibits the GTPase activity of dynamin I, and this inhibition is reversed by the addition of calmodulin. NAP-22 also inhibits the activation of dynamin GTPase by acidic phospholipid (phosphatidylserine), suggesting NAP-22 competes for dynamin binding sites on acidic membrane lipids. Affinity pull-down screening; mass spectrometry; Western blotting; GTPase activity assay with recombinant proteins; calmodulin rescue experiment Neuroscience letters Medium 29604406
2019 In vivo, the WT1-BASP1 complex is required to maintain the differentiated state of adult taste receptor cells. In the absence of BASP1 (conditional knockout mouse), WT1-dependent target genes from the Wnt and Shh pathways that are normally repressed become de-repressed, and taste cell composition and function are altered. BASP1 and WT1 co-occupy target gene promoters in adult taste cells. Conditional BASP1 knockout mouse; ChIP; taste cell functional assays; gene expression analysis Life science alliance High 31167803
2020 Membrane-bound BASP1 increases EGFR signaling and stabilizes EGFR proteins by facilitating their escape from the ubiquitin-proteasome pathway. Activation of EGFR reciprocally recruits more BASP1 to the plasma membrane, generating a positive feedback loop between BASP1 and EGFR. Proteomic analysis; tyrosine kinase activity assay; ubiquitin-proteasome pathway inhibitor experiments; BASP1 knockdown/overexpression; in vitro and in vivo functional assays Theranostics Medium 33042262
2020 The effector domain of BASP1 interacts with calmodulin (CaM), and excess BASP1 or a synthetic BASP1 effector domain peptide displaces v-Myc from CaM. BASP1 co-expression decreases the protein stability of v-Myc. Suppression of v-Myc-triggered transcriptional activation and cell transformation by BASP1 is compensated by ectopic CaM, demonstrating that BASP1-mediated withdrawal of CaM from v-Myc is a crucial event in the inhibition. CaM binding/displacement assay with BASP1 peptide; v-Myc protein stability assay; CaM overexpression rescue; cell transformation assay; transcription assay Molecular oncology Medium 31944520
2021 BASP1 requires interaction with cholesterol in the cell nucleus for transcriptional repression. BASP1 interacts with cholesterol through a conserved cholesterol interaction motif, and directly recruits cholesterol to the promoter regions of WT1 target genes. Mutation of BASP1 to ablate cholesterol interaction, or treatment with cholesterol biosynthesis inhibitors, inhibits BASP1's transcriptional repressor function. The BASP1-cholesterol interaction is required for BASP1-dependent chromatin remodeling and control of cell differentiation programs. Cholesterol interaction motif mutagenesis; ChIP for cholesterol at promoters; cholesterol biosynthesis inhibitor treatment; transcription reporter assay; chromatin remodeling assay; cell differentiation assay Proceedings of the National Academy of Sciences of the United States of America High 34266955
2021 BASP1 deletion in podocytes protects against podocyte injury in diabetic nephropathy. BASP1 promotes actin cytoskeleton rearrangements and apoptosis in podocyte cell line (MPC5). BASP1 activates the p53 pathway through co-repression with WT1: p53 pathway molecules are downregulated in BASP1 knockdown podocytes treated with high glucose. Podocyte-specific BASP1 knockout mouse; BASP1 knockdown and overexpression in MPC5 cells; apoptosis assay; actin cytoskeleton imaging; p53 pathway molecule expression analysis Acta physiologica Medium 33615732
2021 Truncated YY1 (YY1B, 52 residues containing first two zinc fingers) interacts with BASP1 through a 339KLK341 motif in YY1. This interaction is required for selective inhibition of SMC (but not EC) proliferation. BASP1 overexpression mimics YY1B's selective inhibition of SMC growth; BASP1 siRNA partially rescues SMC from YY1B-mediated growth inhibition. YY1B reduces neointima formation in rat carotid balloon injury model. GST pull-down; mass spectrometry identification of BASP1; 339KLK341 to 339AAA341 mutagenesis; siRNA rescue; in vivo rat carotid balloon injury model with adenoviral overexpression Cardiovascular research Medium 33508088
2021 Basp1 promotes angiogenesis by upregulating β-catenin gene expression and the Dll4/Notch1 signaling pathway. Basp1 knockdown in primary mouse brain endothelial and human microvascular endothelial cells reduces migration in a dosage-dependent manner. CRISPR-Cas9 knockout of basp1 in zebrafish embryos causes severely disrupted vessel formation. CRISPR-Cas9 basp1 knockout in zebrafish; siRNA inhibition in endothelial cells; migration assay; β-catenin and Dll4/Notch1 pathway gene expression analysis FASEB journal Medium 33899275
2022 BASP1 modifies chromatin through both lipid-dependent and lipid-independent mechanisms. Removal of active histone modifications H3K9ac and H3K4me3 by BASP1 requires N-terminal myristoylation, whereas placement of the repressive H3K27me3 modification does not require BASP1 lipidation. Approximately 50% of BASP1 target genes show lipidation-dependent chromatin compaction and transcriptional repression. BASP1's tumor suppressor activity is also partially dependent on myristoylation. Myristoylation-deficient BASP1 mutant; ChIP for histone modifications (H3K9ac, H3K4me3, H3K27me3); RNA-seq; ATAC-seq; tumor suppressor functional assay iScience High 35982799
2023 Myeloid-specific deletion of Basp1 in mice attenuates diet-induced NASH pathologies. Macrophages lacking Basp1 exhibit diminished response to pro-inflammatory stimuli, impaired NLRP3 inflammasome activation, and reduced cytokine secretion. Myeloid-specific Basp1 conditional knockout mouse; bulk and single-cell RNA sequencing; in vitro macrophage stimulation; NLRP3 inflammasome activation assay; cytokine measurement Hepatology Medium 37505219
2023 BASP1 downregulation promotes temozolomide resistance in gliomas through epigenetic activation of the FBXO32/NF-κB/MGMT axis. Loss of BASP1 results in removal of TRIM37/EZH2 complex-mediated repressive histone modifications (H2A-ub, H3K27me3) and addition of WDR5/MLL complex-mediated active modifications (H3K4me3, H3K9ac) on the FBXO32 promoter, leading to FBXO32 upregulation, IκBα ubiquitin-dependent degradation, and MGMT upregulation. BASP1 knockdown; ChIP for histone modifications at FBXO32 promoter; TRIM37/EZH2 and WDR5/MLL complex analysis; ubiquitin-dependent degradation assay; in vitro and in vivo temozolomide resistance assay Molecular cancer research Medium 36961398
2023 BASP1 down-regulates RANKL-induced osteoclastogenesis. RANKL rapidly down-regulates BASP1 expression in bone marrow macrophages. BASP1 knockdown or knockout enhances RANKL-induced osteoclastogenesis, cell-cell fusion, and mineral-degrading ability. BASP1 knockdown increases expression of osteoclastogenic transcription factor Nfatc1 and its downstream targets (Dc-stamp, Ctsk, Itgb3, Mmp9). Ectopic BASP1 produces opposite effects. BASP1 knockdown/knockout in primary BMMs and RAW 264.7 cells; ectopic BASP1 overexpression; osteoclastogenesis assay; TRAP staining; mineral degradation assay; Nfatc1 target gene expression analysis Experimental cell research Medium 37619639
2026 BASP1 interacts with β-catenin and binds to the MYC promoter, leading to transcriptional repression of MYC. In colorectal cancer cells, BASP1 activation suppresses multiple WNT/β-catenin/TCF pathway proteins including TNIK (a kinase that phosphorylates TCF7L2 required for MYC transcriptional activation). BASP1 also represses the transformed phenotype (contact inhibition, anchorage-independent growth, tumor formation). Stable cell lines with BASP1 overexpression or CRISPR-mediated promoter reactivation; proteome and transcriptome analyses; Co-IP for β-catenin-BASP1; ChIP at MYC promoter; TNIK inhibitor experiment; colony formation and tumorigenesis assays Proceedings of the National Academy of Sciences of the United States of America Medium 41785318
2026 Basp1 interacts directly with Vimentin in neutrophils (demonstrated by protein docking and co-immunoprecipitation), promoting cytoskeletal rearrangement essential for neutrophil migration and NETs formation. Silencing Basp1 in vitro impairs both neutrophil migration and NETs formation, with correlated downregulation of chemotaxis-related and NETs-related genes. Conditional myeloid Basp1 KO reduces neutrophil infiltration and NETs formation in TBI model. Co-immunoprecipitation; protein docking; Basp1 siRNA knockdown; myeloid conditional KO mouse; bulk RNA-seq; NETs and migration functional assays in TBI model Molecular neurobiology Medium 42149339

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. The Journal of cell biology 512 10871285
2000 Shared and unique roles of CAP23 and GAP43 in actin regulation, neurite outgrowth, and anatomical plasticity. The Journal of cell biology 228 10871284
2020 GAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases. Frontiers in cell and developmental biology 140 33015061
2004 BASP1 is a transcriptional cosuppressor for the Wilms' tumor suppressor protein WT1. Molecular and cellular biology 114 14701728
2005 Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1. International review of cytology 99 16125549
2002 Transcriptional upregulation of SCG10 and CAP-23 is correlated with regeneration of the axons of peripheral and central neurons in vivo. Molecular and cellular neurosciences 98 12213442
1999 Cholesterol-dependent localization of NAP-22 on a neuronal membrane microdomain (raft). The Journal of biological chemistry 89 10409698
2004 Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin. The EMBO journal 87 14765114
2009 Inhibition of Myc-induced cell transformation by brain acid-soluble protein 1 (BASP1). Proceedings of the National Academy of Sciences of the United States of America 85 19297618
2010 BASP1 promotes apoptosis in diabetic nephropathy. Journal of the American Society of Nephrology : JASN 83 20110383
1997 The motility-associated proteins GAP-43, MARCKS, and CAP-23 share unique targeting and surface activity-inducing properties. Experimental cell research 76 9344590
2008 Characterization of BASP1-mediated neurite outgrowth. Journal of neuroscience research 71 18438920
1990 Identification, localization, and primary structure of CAP-23, a particle-bound cytosolic protein of early development. The Journal of cell biology 69 2148567
2012 Repression of transcription by WT1-BASP1 requires the myristoylation of BASP1 and the PIP2-dependent recruitment of histone deacetylase. Cell reports 66 22939983
2008 Dynamic interaction between WT1 and BASP1 in transcriptional regulation during differentiation. Nucleic acids research 65 19050011
1997 The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties. Biochimie 63 9310187
1999 Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-22. Direct involvement of protein myristoylation in calmodulin-target protein interaction. The Journal of biological chemistry 58 10207003
1994 Inhibitory effect of calmodulin on phosphorylation of NAP-22 with protein kinase C. The Journal of biological chemistry 55 8034714
1997 Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain. Biochimica et biophysica acta 52 9030206
2008 Identification of novel aberrant methylation of BASP1 and SRD5A2 for early diagnosis of hepatocellular carcinoma by genome-wide search. International journal of oncology 47 18949357
2003 Binding of NAP-22, a calmodulin-binding neuronal protein, to raft-like domains in model membranes. Biochemistry 40 12718518
2011 WT1 and its transcriptional cofactor BASP1 redirect the differentiation pathway of an established blood cell line. The Biochemical journal 37 21269271
2021 LncRNA BASP1-AS1 interacts with YBX1 to regulate Notch transcription and drives the malignancy of melanoma. Cancer science 35 34533860
2004 Cholesterol-dependent partitioning of PtdIns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa). The Biochemical journal 35 14989697
1999 Immunohistochemical localization of a novel acidic calmodulin-binding protein, NAP-22, in the rat brain. Neuroscience 35 10391449
2015 Albumin-induced apoptosis of tubular cells is modulated by BASP1. Cell death & disease 34 25675304
2020 Targeting positive feedback between BASP1 and EGFR as a therapeutic strategy for lung cancer progression. Theranostics 33 33042262
2021 Podocyte apoptosis in diabetic nephropathy by BASP1 activation of the p53 pathway via WT1. Acta physiologica (Oxford, England) 32 33615732
2002 Lipid binding activity of a neuron-specific protein NAP-22 studied in vivo and in vitro. Journal of neuroscience research 31 12271466
2018 Methylation-associated silencing of BASP1 contributes to leukemogenesis in t(8;21) acute myeloid leukemia. Experimental & molecular medicine 30 29674693
2013 Prohibitin is required for transcriptional repression by the WT1-BASP1 complex. Oncogene 29 24166496
2020 LINC00473 inhibits vascular smooth muscle cell viability to promote aneurysm formation via miR-212-5p/BASP1 axis. European journal of pharmacology 28 31954705
2017 BASP1 interacts with oestrogen receptor α and modifies the tamoxifen response. Cell death & disease 27 28492543
1997 Biochemical evidence for the presence of NAP-22, a novel acidic calmodulin binding protein, in the synaptic vesicles of rat brain. Neuroscience letters 26 9086473
2010 Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers. The FEBS journal 24 21156029
1994 Expression and myristoylation of NAP-22 using a baculovirus transfer vector system. Biochimica et biophysica acta 24 8193160
2020 The brain acid-soluble protein 1 (BASP1) interferes with the oncogenic capacity of MYC and its binding to calmodulin. Molecular oncology 23 31944520
2000 The binding of myristoylated N-terminal nonapeptide from neuro-specific protein CAP-23/NAP-22 to calmodulin does not induce the globular structure observed for the calmodulin-nonmyristylated peptide complex. Protein science : a publication of the Protein Society 22 11106163
2021 Cholesterol is required for transcriptional repression by BASP1. Proceedings of the National Academy of Sciences of the United States of America 21 34266955
2006 Tracking peptide-membrane interactions: insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly. Journal of structural biology 21 16889981
2003 Natural N-terminal fragments of brain abundant myristoylated protein BASP1. Biochimica et biophysica acta 21 12829256
2020 BASP1 Suppresses Cell Growth and Metastasis through Inhibiting Wnt/β-Catenin Pathway in Gastric Cancer. BioMed research international 20 33426068
2016 High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder. The FEBS journal 20 26918762
2010 The assessment of methylated BASP1 and SRD5A2 levels in the detection of early hepatocellular carcinoma. International journal of oncology 20 19956849
2003 The arrangement of cholesterol in membranes and binding of NAP-22. Chemistry and physics of lipids 20 12598036
2009 Biochemical interaction of an actin-capping protein, CapZ, with NAP-22. Journal of neuroscience research 18 19267422
2005 Induction of raft-like domains by a myristoylated NAP-22 peptide and its Tyr mutant. The FEBS journal 18 15794765
2021 Truncated YY1 interacts with BASP1 through a 339KLK341 motif in YY1 and suppresses vascular smooth muscle cell growth and intimal hyperplasia after vascular injury. Cardiovascular research 17 33508088
2020 WT1 activates transcription of the splice factor kinase SRPK1 gene in PC3 and K562 cancer cells in the absence of corepressor BASP1. Biochimica et biophysica acta. Gene regulatory mechanisms 17 33017668
2021 BASP1 labels neural stem cells in the neurogenic niches of mammalian brain. Scientific reports 15 33692421
2009 Subcellular and regional location of "brain" proteins BASP1 and MARCKS in kidney and testis. Acta histochemica 15 19683798
2008 Novel antibody to human BASP1 labels apoptotic cells post-caspase activation. Biochemical and biophysical research communications 15 18457665
2011 Inhibitory effect of NAP-22 on the phosphatase activity of synaptojanin-1. Journal of neuroscience research 14 21932368
2000 Changes in the localization of NAP-22, a calmodulin binding membrane protein, during the development of neuronal polarity. Neuroscience research 14 10958980
2023 Myeloid-specific ablation of Basp1 ameliorates diet-induced NASH in mice by attenuating pro-inflammatory signaling. Hepatology (Baltimore, Md.) 13 37505219
2022 The BASP1 transcriptional corepressor modifies chromatin through lipid-dependent and lipid-independent mechanisms. iScience 13 35982799
2019 The WT1-BASP1 complex is required to maintain the differentiated state of taste receptor cells. Life science alliance 13 31167803
2013 Interaction of NAP-22 with brain glutamic acid decarboxylase (GAD). Neuroscience letters 12 23376695
2023 BASP1 promotes high glucose-induced endothelial apoptosis in diabetes via activation of EGFR signaling. Journal of diabetes investigation 11 36756695
2011 Immunoelectron microscopic study of BASP1 and MARCKS location in the early and late rat spermatids. Acta histochemica 11 21764106
2003 Quaternary structure of the neuronal protein NAP-22 in aqueous solution. Biochimica et biophysica acta 11 12922169
2023 Dihydroartemisinin inhibits EMT of glioma via gene BASP1 in extrachromosomal DNA. Biochemical and biophysical research communications 10 37473527
2021 Identification of Basp1 as a novel angiogenesis-regulating gene by multi-model system studies. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 10 33899275
2004 Motor, sensory and autonomic nerve terminals containing NAP-22 immunoreactivity in the rat muscle. Brain research 10 14988044
2023 Downregulation of BASP1 Promotes Temozolomide Resistance in Gliomas via Epigenetic Activation of the FBXO32/NF-κB/MGMT Axis. Molecular cancer research : MCR 9 36961398
2023 Circ_0008285 silencing suppresses angiotensin II-induced vascular smooth muscle cell apoptosis in thoracic aortic aneurysm via miR-150-5p/BASP1 axis. Thoracic cancer 9 37337843
2021 The actin-cytoskeleton associating protein BASP1 regulates neural progenitor localization in the neural tube. Genesis (New York, N.Y. : 2000) 9 34897971
2015 Ganglioside contained in the neuronal tissue-enriched acidic protein of 22 kDa (NAP-22) fraction prepared from the detergent-resistant membrane microdomain of rat brain inhibits the phosphatase activity of calcineurin. Journal of neuroscience research 9 25981177
2012 ¹H, ¹³C and ¹⁵N resonance assignments of human BASP1. Biomolecular NMR assignments 9 23179057
2008 BASP1 in the lens. Journal of cellular biochemistry 9 18655186
2003 Specificity of membrane binding of the neuronal protein NAP-22. The Journal of membrane biology 9 12962277
2022 LINC00599 influences smoke-related chronic obstructive pulmonary disease and regulates CSE-induced epithelial cell apoptosis and inflammation by targeting miR-212-5p/BASP1 axis. Human & experimental toxicology 8 36541900
1998 Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa neuronal tissue-enriched acidic protein) homologs. Molecules and cells 8 9749536
2004 Localization of the Cl(-)-ATPase activity on NAP-22 enriched membrane microdomain (raft) of rat brain. Neuroscience letters 7 15193776
1999 Immunohistochemical demonstration of a neuronal calmodulin-binding protein, NAP-22, in the rat spinal cord. Brain research 7 10407094
2015 Tight binding of NAP-22 with acidic membrane lipids. Neuroscience letters 6 26101831
2014 Sequestration of the abrin A chain to the nucleus by BASP1 increases the resistance of cells to abrin toxicity. The Biochemical journal 6 24350992
2008 Morphological analysis on the distribution of membrane lipids and a membrane protein, NAP-22, during neuronal development in vitro. Journal of molecular histology 6 18521709
2025 WTAP-mediated m6A modification on BASP1 mRNA contributes to ferroptosis in AAA. General thoracic and cardiovascular surgery 5 39969669
2025 From inflammation to remodelling: A novel BASP1+ monocyte subset as a catalyst for acute aortic dissection. Journal of advanced research 5 40057028
2018 Interaction of dynamin I with NAP-22, a neuronal protein enriched in the presynaptic region. Neuroscience letters 5 29604406
2025 LncRNA BASP1-AS1 drives PCBP2 K115 lactylation to suppress ferroptosis and confer oxaliplatin resistance in gastric cancer. Free radical biology & medicine 4 40914325
2023 BASP1 down-regulates RANKL-induced osteoclastogenesis. Experimental cell research 4 37619639
2013 BASP1 and its N-end fragments (BNEMFs) dynamics in rat brain during development. Neurochemical research 4 23579388
2025 Design of lipid-based formulations for oral delivery of a BASP1 peptide targeting MYC-dependent gastrointestinal cancer cells. Journal of controlled release : official journal of the Controlled Release Society 3 40185335
2023 BASP1 knockdown suppresses chondrocyte apoptosis and extracellular matrix degradation in vivo and in vitro: A possible therapeutic approach for osteoarthritis. Experimental cell research 3 37207971
2009 Mutational screening of BASP1 and transcribed processed pseudogene TPPsig-BASP1 in patients with Möbius syndrome. Journal of genetics and genomics = Yi chuan xue bao 3 19376485
2026 Reactivation of the silenced BASP1 gene suppresses oncogenic WNT signaling in human colorectal cancer cells. Proceedings of the National Academy of Sciences of the United States of America 2 41785318
2024 LncRNA BASP1-AS1 is a positive regulator of stemness and pluripotency in human SH-SY5Y neuroblastoma cells. Biochemical and biophysical research communications 2 39303525
2020 The effects of phospholipids and fatty acids on the oligomer formation of NAP-22. Neuroscience letters 2 32750402
2026 Single-cell analysis identifies BASP1 as a driver of drug resistance and cell plasticity in oral squamous cell carcinoma. The Journal of biological chemistry 1 41506484
2025 BASP1/HTRA2 axis, targeted by miR-7a-5p, exerted a pro-apoptosis role in myocardial ischemia/reperfusion injury. Toxicology and applied pharmacology 1 40484205
2025 Membrane binding and clustering of NAP-22, a neuron-enriched intrinsically disordered protein. Biophysical journal 1 41163390
2025 BASP1, targeted by miR-185-5p, promotes atherosclerosis via VSMC proliferation and inflammation. American journal of translational research 1 41415108
2024 Oligomerization and aggregation of NAP-22 with several metal ions. Neuroscience letters 1 38184017
2013 [Amyloid-like oligomers of presynaptic protein BASP1]. Rossiiskii fiziologicheskii zhurnal imeni I.M. Sechenova 1 25470949
2008 Effect of exogenous calcium deficit on blood pressure and modification of brain proteins GAP-43 and BASP1 in SHR and WKY rats. Bulletin of experimental biology and medicine 1 19039922
1996 [Specific properties and primary structure of BASP1 protein, initially detected in neuronal axonal terminals]. Biokhimiia (Moscow, Russia) 1 9035734
2026 Brain Acid-Soluble Protein 1 (BASP1) maintains germinal centers by regulating germinal center B cell survival. Journal of immunology (Baltimore, Md. : 1950) 0 41171696
2026 Basp1 Intensifies Neutrophil Migration and NETs Formation in Traumatic Brain Injury. Molecular neurobiology 0 42149339

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