Affinage

NIPSNAP1

Protein NipSnap homolog 1 · UniProt Q9BPW8

Length
284 aa
Mass
33.3 kDa
Annotated
2026-06-10
22 papers in source corpus 17 papers cited in narrative 17 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NIPSNAP1 is a mitochondrially-targeted protein that links mitochondrial quality control to mitophagy, lipid metabolism, and stress signaling (PMID:30982665, PMID:37423391). It is imported via an N-terminal targeting sequence and engages the outer-membrane import receptor TOM22, with steady-state levels and folding maintained by the matrix chaperone HSP60 (PMID:20497468, PMID:28011268). Upon mitochondrial depolarization, NIPSNAP1 accumulates on the mitochondrial surface where it recruits ATG8 proteins and autophagy receptors to serve as an 'eat me' signal for mitophagy, a function it shares redundantly with NIPSNAP2; loss of Nipsnap1 in zebrafish reduces brain mitophagy and produces parkinsonian dopaminergic neuron loss and elevated oxidative stress (PMID:30982665). This surface-signaling step is gated by multiple post-translational and upstream inputs: UBE4B (but not Parkin) ubiquitinates NIPSNAP1 to strengthen its binding to the autophagy adaptors NDP52 and p62/SQSTM1, the deacetylase SIRT3 acts on NIPSNAP1 to support mitophagy, and the FUNDC1–NIPSNAP1/2 interaction at damaged mitochondria is phosphorylation-dependent and lies downstream of the NLRX1–FUNDC1 axis (PMID:41596759, PMID:37417912, PMID:33432610). NIPSNAP1 expression is itself controlled by IGF2BP2-dependent mRNA stability and, in cancer cells, by transcriptional repression via c-Myc–Miz1 (PMID:40539202, PMID:37340421). Independent of mitophagy, NIPSNAP1 localizes to the mitochondrial matrix in neurons where it binds branched-chain alpha-keto acid dehydrogenase and pyruvate dehydrogenase complex components, and it is required in brown adipose tissue for sustained non-shivering thermogenesis and fatty-acid beta-oxidation, interacting with mitochondrial and peroxisomal beta-oxidation machinery (SLC25A20, enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase) (PMID:20646061, PMID:37423391, PMID:40412760). It additionally inhibits the TRPV6 ion channel without altering its surface expression, mediates nocistatin-dependent modulation of pain transmission, and suppresses cancer-cell senescence by sequestering the FBXL14 E3 ligase to stabilize c-Myc and by promoting SIRT3–SOD2 interaction to limit ROS (PMID:18392847, PMID:22311985, PMID:37340421). The relative contribution of mitophagy versus broader metabolic quality control to its physiological role is unsettled: combined Nipsnap1/2 deletion impairs mitochondrial function and accelerates aging without blocking mitophagy despite Parkin accumulation (PMID:40517951).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2008 Medium

    Established the first molecular activity for NIPSNAP1 outside mitochondria, showing it acts as an auxiliary channel regulator.

    Evidence Pull-down, patch-clamp electrophysiology and surface biotinylation in heterologous cells

    PMID:18392847

    Open questions at the time
    • Mechanism of TRPV6 current inhibition without altered surface expression undefined
    • No structural basis for the interaction
    • Physiological relevance in native tissue not established
  2. 2010 Medium

    Defined NIPSNAP1 as a neuron-restricted mitochondrial matrix protein associating with key oxidative-decarboxylation enzyme complexes, suggesting a metabolic role.

    Evidence Subcellular fractionation, in vitro binding assay and immunohistochemistry in rat nervous tissue

    PMID:20646061

    Open questions at the time
    • Functional consequence of binding BCKA/pyruvate dehydrogenase complexes not tested
    • In vitro binding not validated by reciprocal endogenous Co-IP
    • Whether NIPSNAP1 regulates these complexes' activity unknown
  3. 2010 Medium

    Identified the mitochondrial import route and a disease-relevant interaction partner, linking NIPSNAP1 localization to APP biology.

    Evidence Co-IP in transfected COS7 cells and mouse brain, N-terminal targeting sequence analysis

    PMID:20497468

    Open questions at the time
    • Functional significance of APP–NIPSNAP1 interaction unclear
    • Mechanism by which APP disrupts NIPSNAP1 localization not resolved
  4. 2012 Medium

    Showed NIPSNAP1 is required for nocistatin-mediated pain modulation, establishing a surface/synaptic function for an N-terminally truncated form.

    Evidence Affinity-bead pulldown from synaptosomal membranes and behavioral assays in NIPSNAP1-deficient mice

    PMID:22311985

    Open questions at the time
    • How a mitochondrial protein reaches the cell surface unexplained
    • Downstream signaling from the NST–NIPSNAP1 interaction not mapped
  5. 2016 Medium

    Resolved how NIPSNAP1 protein levels are maintained, identifying HSP60 as a chaperone preventing its aggregation.

    Evidence Co-IP, in vitro translation/aggregation assays, native gels and HSP60 knockdown

    PMID:28011268

    Open questions at the time
    • Discrepancy in reported submitochondrial localization (inner-membrane space vs matrix)
    • Whether HSP60 directly folds NIPSNAP1 versus indirect stabilization unclear
  6. 2016 Medium

    Linked NIPSNAP1 to inflammatory signaling, showing it supports NF-kB-driven cytokine production and is a clarithromycin target.

    Evidence Drug-conjugated Sepharose pulldown, siRNA knockdown, cytokine ELISA and NF-kB reporter in epithelial cells

    PMID:27998764

    Open questions at the time
    • Direct molecular mechanism connecting NIPSNAP1 to NF-kB not defined
    • Reliance on knockdown without genetic confirmation
  7. 2016 Medium

    Demonstrated NIPSNAP1 loss exacerbates inflammatory pain and identified PGE2/cAMP-PKA as a regulator of its expression.

    Evidence NIPSNAP1 KO mice in formalin/carrageenan/CFA pain models, p-ERK Western blot, in situ hybridization and DRG pharmacology

    PMID:27030720

    Open questions at the time
    • Mechanism connecting NIPSNAP1 to spinal ERK phosphorylation unresolved
    • Relationship to its mitochondrial functions unclear
  8. 2019 High

    Defined the core mitophagy function: depolarization-induced surface accumulation of NIPSNAP1 recruits ATG8 and autophagy receptors as an 'eat me' signal, with in vivo neurodegenerative consequences.

    Evidence Imaging, reciprocal Co-IP/pulldown for ATG8 and receptors, and zebrafish knockout with behavioral/histological readouts

    PMID:30982665

    Open questions at the time
    • How a matrix protein relocates to the outer surface mechanistically unexplained
    • Redundancy with NIPSNAP2 complicates loss-of-function interpretation
  9. 2021 Medium

    Placed NIPSNAP1 downstream of the NLRX1–FUNDC1 axis, showing the FUNDC1 interaction is phosphorylation-dependent and required to initiate mitophagy.

    Evidence Co-IP, Western blot, siRNA knockdown and in vivo/in vitro overexpression

    PMID:33432610

    Open questions at the time
    • Direct vs indirect FUNDC1–NIPSNAP1 contact not established
    • Phospho-residues governing the interaction not mapped
  10. 2023 Medium

    Identified SIRT3 deacetylation of NIPSNAP1 as a regulatory input controlling mitophagy in liver fibrosis.

    Evidence SIRT3 KO mouse, knockdown/overexpression epistasis, LC3/p62 and colocalization assays

    PMID:37417912

    Open questions at the time
    • Acetylation sites not mapped by mutagenesis
    • Whether deacetylation directly alters NIPSNAP1 activity vs indirect effect unclear
  11. 2023 Medium

    Revealed a mitophagy-independent role in suppressing cancer-cell senescence via FBXL14 sequestration/c-Myc stabilization and SIRT3–SOD2-mediated ROS control, embedded in a c-Myc–Miz1 feedback loop.

    Evidence MS proteomics, RNAi, Co-IP, luciferase and proteasome assays, ROS flow cytometry and xenografts

    PMID:37340421

    Open questions at the time
    • Whether the cytosolic FBXL14 sequestration occurs at the same pool as mitochondrial NIPSNAP1 unclear
    • Single-lab mechanism not independently replicated
  12. 2023 Medium

    Established a metabolic requirement for NIPSNAP1 in sustained brown-fat thermogenesis and beta-oxidation, distinct from mitophagy.

    Evidence Nipsnap1 KO mice, whole-body and cellular respirometry, immunoblot and RT-qPCR

    PMID:37423391

    Open questions at the time
    • Molecular mechanism by which NIPSNAP1 supports beta-oxidation not defined
    • Direct substrates/enzyme partners not identified in this study
  13. 2025 Medium

    Mapped NIPSNAP1 into the mitochondrial/peroxisomal beta-oxidation interaction network and showed gain-of-function enhances energy expenditure.

    Evidence IP-MS network mapping, AAV adipose-specific overexpression, metabolic cage and Seahorse assays

    PMID:40412760

    Open questions at the time
    • Whether NIPSNAP1 directly regulates SLC25A20/enoyl-CoA hydratase activity untested
    • Mechanism coordinating peroxisomal and mitochondrial oxidation unresolved
  14. 2025 Medium

    Identified UBE4B as the E3 ligase ubiquitinating NIPSNAP1 to drive autophagy-adaptor binding, defining a Parkin-independent ubiquitin input to mitophagy.

    Evidence Co-IP, ubiquitination and mitophagy reporter assays in HEK293T/HeLa and Parkin-null cells with lysosome inhibition

    PMID:41596759

    Open questions at the time
    • Ubiquitination sites and chain type not mapped
    • How ubiquitination biochemically strengthens NDP52 binding unclear
  15. 2025 Low

    Implicated m6A-reader IGF2BP2 in stabilizing NIPSNAP1 mRNA to control mitophagy in hepatic ischemia-reperfusion.

    Evidence AAV overexpression, siRNA knockdown, hypoxia/reoxygenation model and RNA-binding/m6A analysis

    PMID:40539202

    Open questions at the time
    • m6A-reader regulation inferred from binding without full functional dissection
    • NIPSNAP1-specific rescue not orthogonally validated
  16. 2025 Medium

    Challenged the mitophagy-centric model: combined Nipsnap1/2 deletion impairs mitochondrial function and accelerates aging but does not block mitophagy despite Parkin accumulation.

    Evidence Nipsnap1/2 double-KO mice with mitochondrial function, mitophagy flux, RNA-seq and aging phenotyping

    PMID:40517951

    Open questions at the time
    • Reconciliation with prior mitophagy phenotypes unresolved
    • The non-mitophagy quality-control mechanism not molecularly defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how NIPSNAP1 physically relocates from the mitochondrial interior to the outer surface, and whether its mitophagy signaling or its metabolic/quality-control roles dominate physiologically.
  • No mechanism for matrix-to-surface translocation
  • Conflicting mitophagy requirement between single-organism KO and mammalian DKO
  • No structural model integrating its diverse binding partners

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 2 GO:0098772 molecular function regulator activity 1 GO:0140313 molecular sequestering activity 1
Localization
GO:0005739 mitochondrion 3 GO:0005886 plasma membrane 2
Pathway
R-HSA-9612973 Autophagy 3 R-HSA-1430728 Metabolism 2 R-HSA-1852241 Organelle biogenesis and maintenance 2
Partners
APPFBXL14FUNDC1HSP60NIPSNAP2SIRT3TOM22UBE4B

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2019 NIPSNAP1 (and NIPSNAP2) accumulate on the mitochondrial surface upon mitochondrial depolarization, where they recruit autophagy receptors and ATG8 proteins to function as 'eat me' signals for mitophagy. NIPSNAP1 and NIPSNAP2 have redundant functions in mitophagy. Zebrafish lacking functional Nipsnap1 show reduced mitophagy in the brain and parkinsonian phenotypes including loss of dopaminergic neurons, reduced motor activity, and increased oxidative stress. Cell imaging, protein localization assays, Co-IP/pulldown for ATG8 and autophagy receptor interactions, zebrafish knockout model with behavioral and histological readouts Developmental cell High 30982665
2008 NIPSNAP1 was identified as a novel auxiliary protein that inhibits TRPV6 ion channel activity. Pull-down assays confirmed physical interaction; electrophysiological recordings showed NIPSNAP1 abolishes TRPV6 currents. Biotinylation assays demonstrated that TRPV6 plasma membrane expression did not change in the presence of NIPSNAP1, indicating the inhibition is independent of reduced cell-surface channel expression. Bioinformatics, pull-down assay, electrophysiology (patch-clamp), biotinylation surface expression assay, RT-PCR, immunohistochemistry Pflugers Archiv : European journal of physiology Medium 18392847
2012 NIPSNAP1 was identified as a cell-surface interacting protein for the neuropeptide nocistatin (NST) in synaptosomal membranes. The N-terminal truncated 29-kDa form (not the 33-kDa precursor) interacts with NST and is present on the cell surface and in synaptic membranes/mitochondria. NIPSNAP1-deficient mice completely lack NST-mediated inhibition of N/OFQ-evoked tactile allodynia, establishing NIPSNAP1 as required for NST pain-modulating function. High-performance affinity latex bead pulldown from synaptosomal membranes, NIPSNAP1-deficient mouse behavioral assays (tactile allodynia), protein fractionation/Western blot The Journal of biological chemistry Medium 22311985
2010 NIPSNAP1 is localized to the mitochondrial matrix in neurons. In vitro binding assays showed NIPSNAP1 binds to the branched-chain alpha-keto acid (BCKA) dehydrogenase complex components (dihydrolipoyl-transacylase and -transacetylase) and pyruvate dehydrogenase complex components. NIPSNAP1 expression is restricted to neurons (pyramidal, Purkinje, motor, dopaminergic, and noradrenergic neurons) in rat nervous system. Subcellular fractionation, in vitro binding assay, immunohistochemistry, immunofluorescence The European journal of neuroscience Medium 20646061
2010 NIPSNAP1 interacts with amyloid precursor protein (APP) family members. The interaction was confirmed in transiently transfected COS7 cells and in mouse brain. NIPSNAP1 is targeted to mitochondria via its N-terminal targeting sequence and interacts with the outer mitochondrial membrane chaperone TOM22. APP overexpression disrupts NIPSNAP1 mitochondrial localization and downregulates NIPSNAP1 levels in cultured cells. Co-immunoprecipitation in transfected COS7 cells and mouse brain lysates, mitochondrial targeting sequence analysis, Western blot The European journal of neuroscience Medium 20497468
2016 NIP-SNAP-1 and NIP-SNAP-2 are maintained by HSP60 chaperone activity. Co-immunoprecipitation identified HSP60 and p62/SQSTM1 as binding partners. Native gel electrophoresis and filter trap assays showed human HSP60 prevented aggregation of newly synthesized NIP-SNAP-2 in an in vitro translation system. HSP60 knockdown decreased NIP-SNAP-1 and -2 expression levels. NIP-SNAP-1 and -2 localize to the mitochondrial inner membrane space, while HSP60 localizes to the matrix. Co-immunoprecipitation, native gel electrophoresis, filter trap assay, in vitro translation system, siRNA knockdown, subcellular fractionation Biochemical and biophysical research communications Medium 28011268
2016 NIPSNAP1 (NIP-SNAP-1) was identified as a clarithromycin (CAM)-binding protein using CAM-conjugated Sepharose affinity pulldown. Knockdown of NIP-SNAP-1 or -2 suppressed LPS-induced IL-8 and IL-6 production and NF-κB activity in epithelial cell lines, revealing NIPSNAP1 role in NF-κB-mediated cytokine production. Affinity pulldown with drug-conjugated Sepharose, proteome analysis, siRNA knockdown, cytokine ELISA, NF-κB reporter assay Biochemical and biophysical research communications Medium 27998764
2021 Phosphorylated FUNDC1 (driven by reduced NLRX1 expression) cannot interact with NIPSNAP1 and NIPSNAP2 on the outer membrane of damaged mitochondria, thereby failing to initiate mitophagy. This was demonstrated by immunoprecipitation showing the FUNDC1–NIPSNAP1/2 interaction is phosphorylation-dependent, placing NIPSNAP1 downstream of the NLRX1–FUNDC1 axis in mitophagy signaling. Co-immunoprecipitation, Western blot, siRNA knockdown, in vitro and in vivo overexpression models Cell proliferation Medium 33432610
2023 SIRT3, a mitochondrial deacetylase, specifically deacetylates NIPSNAP1 and PINK1 to regulate mitophagy in liver fibrosis. SIRT3 knockout deepened liver fibrosis severity. Simultaneous interference with NIPSNAP1 (or PINK1) and SIRT3 overexpression disrupted SIRT3's beneficial effects on mitophagy and fibrosis, establishing NIPSNAP1 as a downstream effector of SIRT3 deacetylation. SIRT3 KO mouse model, siRNA knockdown, protein overexpression, LC3-II/I and p62 assay, colocalization (TOM20/LAMP1), acetylation analysis Journal of cellular physiology Medium 37417912
2023 NIPSNAP1 prevents senescence in cancer cells through dual mechanisms: (1) it sequesters the E3 ubiquitin ligase FBXL14 to prevent proteasome-mediated c-Myc turnover, and (2) it promotes interaction between SIRT3 and SOD2 to maintain ROS below the threshold needed to induce cell cycle arrest. NIPSNAP1 levels are themselves subject to transcriptional repression by the c-Myc–Miz1 complex, forming a feedback loop. Mass spectrometry proteomics, RNAi knockdown, Co-IP (NIPSNAP1-FBXL14, SIRT3-SOD2), luciferase reporter assay, proteasome degradation assay, flow cytometry (ROS), xenograft model Journal of translational medicine Medium 37340421
2023 Nipsnap1 localizes to the mitochondrial matrix in brown adipose tissue (BAT), increases expression in response to cold and β3-adrenergic stimulation, and is required for long-term non-shivering thermogenesis maintenance. Nipsnap1 knockout mice cannot sustain cold-induced energy expenditure or normal body temperature and show severe defects in beta-oxidation capacity, linking NIPSNAP1 to lipid metabolism in BAT. Nipsnap1 knockout mouse generation, whole-body respirometry, cellular and mitochondrial respiration assay, immunoblotting, RT-qPCR Molecular metabolism Medium 37423391
2016 NIPSNAP1-deficient mice show increased nociceptive responses in the late phase of the formalin test and exacerbated prolonged inflammatory pain (carrageenan and CFA models), with enhanced phosphorylation of ERK in the spinal dorsal horn. Prostaglandin E2 stimulates NIPSNAP1 mRNA expression via the cAMP-PKA signaling pathway in dorsal root ganglion cells. NIPSNAP1 KO mice, formalin/carrageenan/CFA behavioral pain models, Western blot (p-ERK), in situ hybridization, pharmacological treatment of isolated DRG cells Molecular pain Medium 27030720
2025 Nipsnap1 interacts with proteins involved in both mitochondrial and peroxisomal fatty acid beta-oxidation in brown adipocytes, including solute carrier family 25 member 20 and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase. Adipose-specific overexpression of Nipsnap1 increases energy expenditure by ~20% through lipid utilization and increases beta-oxidation by ~39% in primary brown adipocytes. Immunoprecipitation-mass spectrometry protein-protein network mapping, AAV-mediated adipose-specific overexpression, metabolic cage respirometry, Seahorse mitochondrial respiration assay The Journal of nutrition Medium 40412760
2025 UBE4B is an E3 ubiquitin ligase for NIPSNAP1 that catalyzes NIPSNAP1 ubiquitination in HEK293T and HeLa cells under mitochondrial depolarization, promoting lysosome-dependent NIPSNAP1 degradation and enhancing interaction of NIPSNAP1 with autophagy adaptors NDP52 and p62/SQSTM1. UBE4B-mediated NIPSNAP1 ubiquitination facilitates mitophagy in Parkin-null HeLa cells specifically through strengthening NIPSNAP1–NDP52 binding. Parkin does not ubiquitinate NIPSNAP1. Co-immunoprecipitation, ubiquitination assay in HEK293T and HeLa cells, Parkin-null cell line, lysosome inhibition assay, mitophagy reporter assay International journal of molecular sciences Medium 41596759
2025 Loss of NIPSNAP1 and NIPSNAP2 (double knockout mice) impairs mitochondrial function and enhances glycolysis but does NOT affect mitophagy despite significant Parkin accumulation, suggesting NIPSNAP1/2 role in mitochondrial quality control is not solely through mitophagy. DKO mice show accelerated aging phenotypes including reduced muscle strength, fibrosis, and inflammation. Nipsnap1/2 double knockout mouse, mitochondrial function assays, mitophagy flux assay (Parkin accumulation), RNA-seq, metabolic and aging phenotyping Metabolism: clinical and experimental Medium 40517951
2025 IGF2BP2 functions as an m6A reader that binds NIPSNAP1 mRNA and regulates its stability. NIPSNAP1 overexpression promotes mitophagy and maintains mitochondrial dynamics in hepatic ischemia-reperfusion, while NIPSNAP1 knockdown impairs mitophagy and disrupts mitochondrial dynamics. AAV-mediated gene overexpression in vivo, siRNA knockdown, hypoxia/reoxygenation cell model, mitophagy assay, mitochondrial dynamics imaging, RNA-binding protein pulldown/m6A analysis World journal of gastroenterology Low 40539202
2024 NIPSNAP1 and NIPSNAP2 knockdown reduces mitochondrial oxygen consumption rate (OCR) and impairs TLR4-mediated IL-8 production, linking NIPSNAP1/2 to mitochondrial quality control supporting cytokine signaling. However, individual or double KO of NIPSNAP1/2 did not impair IL-8 secretion or OCR, indicating compensation or off-target effects in the KD experiments. Clarithromycin suppresses IL-8 production by reducing OCR via functional inhibition of NIPSNAP1 and 2. RNA interference KD, CRISPR KO, Seahorse OCR assay, cytokine ELISA, TLR4 stimulation Scientific reports Low 38287119

Source papers

Stage 0 corpus · 22 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2019 NIPSNAP1 and NIPSNAP2 Act as "Eat Me" Signals for Mitophagy. Developmental cell 128 30982665
2021 NLRX1/FUNDC1/NIPSNAP1-2 axis regulates mitophagy and alleviates intestinal ischaemia/reperfusion injury. Cell proliferation 84 33432610
1998 Characterization of the human NIPSNAP1 gene from 22q12: a member of a novel gene family. Gene 48 9661659
2023 SIRT3 regulates mitophagy in liver fibrosis through deacetylation of PINK1/NIPSNAP1. Journal of cellular physiology 25 37417912
2008 Identification of Nipsnap1 as a novel auxiliary protein inhibiting TRPV6 activity. Pflugers Archiv : European journal of physiology 25 18392847
2012 Identification of NIPSNAP1 as a nocistatin-interacting protein involving pain transmission. The Journal of biological chemistry 20 22311985
2010 Neuronal localization of the mitochondrial protein NIPSNAP1 in rat nervous system. The European journal of neuroscience 20 20646061
2005 Expression of calpastatin, minopontin, NIPSNAP1, rabaptin-5 and neuronatin in the phenylketonuria (PKU) mouse brain: possible role on cognitive defect seen in PKU. Neurochemistry international 19 15863237
2010 Sequence variants in four candidate genes (NIPSNAP1, GBAS, CHCHD1 and METT11D1) in patients with combined oxidative phosphorylation system deficiencies. Journal of inherited metabolic disease 17 24137763
2013 Chromosomal structural variations during progression of a prostate epithelial cell line to a malignant metastatic state inactivate the NF2, NIPSNAP1, UGT2B17, and LPIN2 genes. Cancer biology & therapy 15 23792589
2010 Interaction of a novel mitochondrial protein, 4-nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1 (NIPSNAP1), with the amyloid precursor protein family. The European journal of neuroscience 15 20497468
2023 NIPSNAP1 directs dual mechanisms to restrain senescence in cancer cells. Journal of translational medicine 12 37340421
2016 Mitochondrial proteins NIP-SNAP-1 and -2 are a target for the immunomodulatory activity of clarithromycin, which involves NF-κB-mediated cytokine production. Biochemical and biophysical research communications 10 27998764
2016 Involvement of NIPSNAP1, a neuropeptide nocistatin-interacting protein, in inflammatory pain. Molecular pain 9 27030720
2023 Nipsnap1-A regulatory factor required for long-term maintenance of non-shivering thermogenesis. Molecular metabolism 7 37423391
2016 NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat shock protein 60. Biochemical and biophysical research communications 5 28011268
2025 NIPSNAP1 and NIPSNAP2 facilitate healthy aging independent of mitophagy. Metabolism: clinical and experimental 2 40517951
2024 The clarithromycin-binding proteins NIPSNAP1 and 2 regulate cytokine production through mitochondrial quality control. Scientific reports 2 38287119
2025 The Mitochondrial Brown Adipose Tissue Maintenance Factor Nipsnap1 Interfaces Directly With the β-Oxidation Protein Machinery in Rodents. The Journal of nutrition 1 40412760
2024 The Mitochondrial Brown Adipose Tissue Maintenance Factor Nipsnap1 Interfaces Directly with the Beta-Oxidation Protein Machinery. bioRxiv : the preprint server for biology 1 39763994
2026 UBE4B Mediates Mitophagy via NIPSNAP1 Ubiquitination and NDP52 Recruitment. International journal of molecular sciences 0 41596759
2025 N6-methyladenosine reader IGF2BP2 regulates NIPSNAP1-mediated mitophagy and mitochondrial dynamics to alleviate hepatic ischemia-reperfusion injury. World journal of gastroenterology 0 40539202

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