| 1998 |
RanBPM (RANBP9) localizes to the centrosome throughout the cell cycle, cosediments with centrosomal fractions by sucrose-density gradient centrifugation, and specifically interacts with GTP-Ran in two-hybrid assay. Overexpression causes ectopic microtubule nucleation sites colocalizing with gamma-tubulin, and anti-RanBPM antibodies inhibit microtubule aster formation. |
Yeast two-hybrid, sucrose-density gradient centrifugation, immunofluorescence, antibody inhibition assay |
The Journal of cell biology |
High |
9817760
|
| 2001 |
Full-length RanBPM encodes a 90 kDa protein (not 55 kDa) that forms a large protein complex of >670 kDa and localizes predominantly to both nucleus and cytoplasm surrounding the centrosome, not exclusively centrosomal as previously thought. Ran is detected in this complex when both are co-expressed. |
cDNA cloning, immunoprecipitation, gel filtration, immunofluorescence with multiple antibodies |
Gene |
High |
11470507
|
| 2002 |
RanBPM/RanBP9 interacts with the tyrosine kinase domain of MET receptor via its SPRY domain, both in vitro and in vivo, and this interaction is strengthened by HGF stimulation. RanBPM activates the Ras-Erk-SRE pathway by recruiting Sos to MET, and its N-terminal poly-PQ region is required for Sos recruitment. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, Ras-GTP loading assay, ERK phosphorylation assay, SRE-luciferase reporter |
The Journal of biological chemistry |
High |
12147692
|
| 2002 |
RanBPM interacts with the androgen receptor (AR) and glucocorticoid receptor (GR) but not estrogen receptor, and overexpression of RanBPM enhances AR and GR transcriptional activity in a ligand-dependent fashion. |
Yeast two-hybrid, GST pull-down, His-tag pull-down, transient transfection reporter assay in prostate cancer cell lines |
The Journal of biological chemistry |
High |
12361945
|
| 2002 |
RanBPM is ubiquitinated and undergoes proteasome-dependent degradation; it is a substrate for the deubiquitinase USP11, which directly interacts with RanBPM and inhibits its ubiquitination in a dose-dependent manner. |
Yeast two-hybrid, co-immunoprecipitation, pulse-chase with proteasome inhibitors, in vivo and in vitro ubiquitination assay, recombinant USP11 deubiquitination assay |
The Biochemical journal |
High |
12084015
|
| 2003 |
RanBPM forms a protein complex with Twa1 and Muskelin as identified by yeast two-hybrid and confirmed by co-immunoprecipitation and gel-filtration analysis. |
Yeast two-hybrid, co-immunoprecipitation, gel filtration |
Gene |
Medium |
12559565
|
| 2003 |
RanBPM interacts with the death domain of the p75 neurotrophin receptor (p75NTR) intracellular domain, as shown by yeast two-hybrid and co-immunoprecipitation in mammalian cells. |
Yeast two-hybrid, co-immunoprecipitation, domain mapping |
Biochemical and biophysical research communications |
Medium |
12963025
|
| 2004 |
RanBPM is a peripheral membrane protein phosphorylated on serine residues; phosphorylation is increased by stress stimuli and decreased by p38 kinase inhibitor SB203580. RanBPM interacts with the cytoplasmic domain of beta2 integrin LFA-1 and beta1 integrin in vitro and in vivo, co-localizes at the cell membrane, and synergizes with LFA-1 in AP-1-dependent transcriptional activation. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, immunofluorescence co-localization, AP-1 reporter assay, p38 inhibitor treatment |
The Journal of biological chemistry |
High |
14722085
|
| 2004 |
RanBP10, a paralog of RanBPM/RanBP9, interacts with MET via its SPRY domain but fails to recruit Sos and cannot activate Ras/Erk signaling, demonstrating that the N-terminal poly-PQ region of RanBPM is required for Sos recruitment and Ras/Erk pathway activation. |
Co-transfection, SRE-luciferase reporter, ERK phosphorylation, binding assay, domain deletion mutants |
Biochemical and biophysical research communications |
Medium |
14684163
|
| 2005 |
RanBPM interacts with the neural cell adhesion molecule L1 via its N-terminal SPRY domain both in vivo and in GST pull-down assays. Overexpression of N-terminal RanBPM (N-RanBPM) reduces L1-triggered ERK1/2 activation by 50% and inhibits L1-mediated neurite outgrowth and branching in primary neurons. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, L1 antibody patching, ERK phosphorylation assay, neurite outgrowth assay in primary neurons |
Journal of neurochemistry |
High |
16000162
|
| 2005 |
RanBPM directly binds to the extreme C-terminal region of p73alpha but not p53, inhibits ubiquitination of p73alpha, extends its half-life, induces nuclear co-localization of both proteins, and enhances p73alpha proapoptotic activity. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, immunofluorescence, ubiquitination assay, apoptosis assay |
Oncogene |
High |
15558019
|
| 2005 |
RanBPM interacts with the Axl and Sky/Tyro3 receptor tyrosine kinases; the SPRY-LisH domain region of RanBPM is required for this interaction, and endogenous Axl and RanBPM constitutively interact in multiple mammalian cell lines. |
Yeast two-hybrid, co-immunoprecipitation (cell-free and mammalian), domain deletion analysis |
The international journal of biochemistry & cell biology |
Medium |
15964779
|
| 2006 |
RanBPM physically interacts with Plexin-A1 and this complex is regulated by MICAL expression. Overexpression of RanBPM with PlexinA1 reduces cell spreading and strongly inhibits axonal outgrowth; truncated RanBPM or RanBPM siRNA knockdown reduces Sema3A responsiveness, establishing RanBPM as a mediator of Sema3A signaling through Plexin-A. |
Yeast two-hybrid, co-immunoprecipitation, cell spreading assay, axonal outgrowth assay in vitro and in vivo, siRNA knockdown |
The Journal of neuroscience |
High |
16672672
|
| 2006 |
RanBPM interacts with the N-terminus of CD39/ecto-NTPDase1 via its SPRY domain and co-expression of RanBPM substantially diminishes NTPDase activity of recombinant CD39 in COS-7 cells; an N-terminus-deleted CD39 mutant shows no inhibition. |
Yeast two-hybrid, co-immunoprecipitation, NTPDase activity assay, domain deletion mutants |
The Biochemical journal |
Medium |
16478441
|
| 2006 |
RanBPM acts as a coactivator for thyroid hormone receptors (TRs) in a ligand-independent manner; the C-terminal region of RanBPM mediates binding to the TR DNA-binding domain, and the N-terminal polyglutamine region of RanBPM is required for stimulating TR transactivation. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, luciferase reporter assay, domain deletion analysis |
Journal of molecular endocrinology |
Medium |
16595702
|
| 2007 |
RanBPM is a core component of the CTLH complex, which includes Muskelin, p48EMLP, p44CTLH, ARMC8alpha, and ARMC8beta; each component was confirmed by co-immunoprecipitation in Cos-7 cells and pull-down with bacterially expressed Twa1. |
Tandem MS with anti-RanBPM antibody, co-immunoprecipitation, GST pull-down with bacterially expressed Twa1, in vitro translation |
Gene |
High |
17467196
|
| 2008 |
RanBPM interacts with EBV immediate-early protein Rta via the SPRY domain of RanBPM; this interaction promotes sumoylation of Rta by SUMO-E2 (Ubc9), which enhances Rta transactivation activity of viral lytic genes. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, confocal microscopy, sumoylation assay, luciferase reporter |
Journal of molecular biology |
Medium |
18455188
|
| 2008 |
Muskelin subcellular localization is coregulated with RanBP9; knockdown of either muskelin or RanBP9 results in protrusive cell morphologies with enlarged cell perimeters. Muskelin's C-terminus controls both cytoplasmic restraint and RanBP9 interaction. RanBP9 knockdown produces equivalent morphological alterations to muskelin knockdown. |
Subcellular fractionation, siRNA/shRNA knockdown, rescue with cDNA constructs, live cell microscopy |
The Journal of cell biology |
High |
18710924
|
| 2008 |
RanBPM interacts with metabotropic glutamate receptors mGlu2, and other group II and group III receptors (except mGlu6), and is expressed in the inner plexiform layer of the retina co-localizing with mGlu8b. |
Yeast two-hybrid screen, co-immunoprecipitation, immunofluorescence co-localization |
FEBS letters |
Medium |
18555800
|
| 2008 |
RanBPM modulates Cav3.1 T-type Ca2+ channel currents; it binds to the intracellular loop between transmembrane domains I and II of Cav3.1, increases Cav3.1 currents in whole-cell patch-clamp, and abolishes PKC-mediated inhibition of Cav3.1 currents. |
Yeast two-hybrid, co-immunoprecipitation, whole-cell patch-clamp electrophysiology, PKC activator treatment |
Biochemical and biophysical research communications |
Medium |
18801335
|
| 2009 |
RanBPM/RanBP9 promotes BACE1 cleavage of APP and Abeta generation by scaffolding APP, LRP, and BACE1 together via its N-terminal SPRY-LisH domains; it reduces cell surface APP, accelerates APP internalization, and increases APP association with lipid rafts. siRNA knockdown of endogenous RanBP9 significantly reduces Abeta generation in CHO cells and primary neurons. |
Co-immunoprecipitation, cell surface biotinylation, internalization assay, lipid raft fractionation, Abeta ELISA, siRNA knockdown in primary neurons |
The Journal of biological chemistry |
High |
19251705
|
| 2009 |
RanBPM functions as an activator of apoptotic pathways induced by DNA damage: transient RanBPM expression induces caspase activation; siRNA knockdown of RanBPM prevents DNA damage-induced caspase-3 and caspase-2 activation. Following ionizing radiation, RanBPM relocalizes progressively from nucleus to cytoplasm, and RanBPM downregulation is associated with decreased mitochondria-associated Bax and upregulated Bcl-2. |
Transient transfection, siRNA knockdown, caspase activation assay, cell viability assay, subcellular fractionation, Western blot, ionizing radiation treatment |
Molecular cancer research : MCR |
Medium |
19996306
|
| 2009 |
RanBPM constitutively associates with mu opioid receptor (MOP) and reduces agonist-induced endocytosis of MOP by interfering with beta-arrestin2 translocation, without affecting MOP-mediated inhibition of adenylyl cyclase. |
Yeast two-hybrid, co-immunoprecipitation in HEK293 cells, adenylyl cyclase inhibition assay, receptor internalization assay, beta-arrestin2-GFP translocation assay |
Neuroscience letters |
Medium |
19788913
|
| 2010 |
RanBPM interacts with citron kinase (CITK) and co-localizes at adherens junctions in developing neocortex. In utero RNAi knockdown of RanBPM decreases CITK polarization at the ventricular surface, increases cells in mitosis, decreases cells in cytokinesis, and the mitosis effect is reversed in CITK-mutant embryos (epistasis). |
Yeast two-hybrid, co-immunoprecipitation, protein overlay, in utero RNAi, genetic epistasis with CITK mutants, immunofluorescence |
Developmental neurobiology |
High |
19790105
|
| 2010 |
RanBPM interacts with TrkB receptor and overexpression enhances BDNF-induced MAPK and Akt activation; siRNA knockdown of RanBPM reduces BDNF-induced MAPK and Akt activation, neuronal morphogenesis, and BDNF-mediated trophic effects. |
Co-immunoprecipitation, ERK/Akt phosphorylation assay, neuronal morphogenesis assay, siRNA knockdown |
Journal of neurochemistry |
Medium |
20403074
|
| 2011 |
RanBPM is essential for mammalian gametogenesis: RanBPM knockout mice are sterile in both sexes, with spermatogenesis arrested at late pachytene-diplotene stages of prophase I and premature ovarian failure due to depletion of germ cell pool at end of prophase I. Chimeric mice show cell-autonomous action of RanBPM in germ cells. |
Knockout mouse generation, histological analysis, chimera analysis, meiotic staging |
Development (Cambridge, England) |
High |
21561988
|
| 2012 |
RanBPM overexpression disrupts integrin-dependent cell attachment and spreading, decreases Pyk2/paxillin signaling and talin/vinculin localization at focal adhesions, and accelerates endocytosis of beta1-integrin and LRP. Conversely, RanBP9 knockdown promotes cell attachment, spreading, focal adhesion signaling, and increases surface beta1-integrin. |
Cell attachment/spreading assay, focal adhesion immunostaining, Pyk2/paxillin phosphorylation assay, cell surface biotinylation, endocytosis assay, siRNA knockdown, transgenic primary neurons |
FASEB journal |
High |
22223749
|
| 2012 |
RanBP9 overexpression promotes apoptosis and potentiates Abeta-induced neurotoxicity by activating/dephosphorylating cofilin; siRNA knockdown of cofilin abolishes both Abeta- and RanBP9-induced apoptosis, establishing the RanBP9-cofilin pathway as a mediator of neurodegeneration. |
Transgenic mouse overexpression, siRNA knockdown, cofilin phosphorylation assay, apoptosis assay, neurotoxicity assay |
Cell death and differentiation |
High |
22361682
|
| 2013 |
RanBPM interacts with the TRAF6 C-terminus via its SPRY domain, influences TRAF6 ubiquitination, and depresses the TRAF6-triggered NF-kappaB signaling pathway. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, FRET, NF-kB reporter assay, ubiquitination assay |
Molecular and cellular biochemistry |
Medium |
21805090
|
| 2013 |
RanBP9 physically interacts with p73 and increases endogenous p73alpha levels at both transcriptional and post-translational levels; knockdown of p73 by siRNA blocks RanBP9- and Abeta-induced mitochondria-mediated cell death, and knockdown of RanBP9 suppresses p73-induced apoptosis, demonstrating cooperative roles. |
Co-immunoprecipitation, siRNA knockdown (bidirectional epistasis), mitochondrial membrane potential assay, cytochrome c release assay, apoptosis assay |
Cell death & disease |
High |
23348590
|
| 2013 |
RanBP9 delays clearance of cytosolic Ca2+ mediated by the mitochondrial calcium uniporter through cofilin translocation to mitochondria and oxidative mechanisms; RanBP9 also retards anterograde axonal transport of mitochondria and decreases synaptic mitochondrial activity. |
Calcium imaging, ROS measurement, mitochondrial transport assay, cofilin localization assay in primary hippocampal neurons |
FASEB journal |
Medium |
23982146
|
| 2013 |
RanBPM interacts with TGF-beta receptor I (TbetaRI) and abrogates TbetaRI-TRAF6 interaction; RanBPM depresses TGF-beta-induced TRAF6 ubiquitination, NF-kappaB signaling, and blocks TbetaRI nuclear accumulation. |
Yeast two-hybrid, co-immunoprecipitation, GST pull-down, TbetaRI nuclear localization assay, NF-kB reporter, ubiquitination assay |
Cellular signalling |
Medium |
24103590
|
| 2013 |
COPS5/Jab1 interacts with RanBP9, stabilizes RanBP9 protein by extending its half-life, and thereby increases Abeta generation; siRNA knockdown of COPS5 reduces Abeta generation. |
Yeast two-hybrid, co-immunoprecipitation, protein stability (half-life) assay, Abeta ELISA, siRNA knockdown |
The Journal of biological chemistry |
Medium |
23926111
|
| 2014 |
RanBP9 positively regulates SSH1 (Slingshot homolog 1) levels and mediates Abeta-induced translocation of cofilin to mitochondria and induction of cofilin-actin pathology in cells, primary neurons, and in vivo; RanBP9 reduction in APP/PS1 mice protects against cofilin-actin pathology, synaptic damage, gliosis, and Abeta accumulation, and significantly enhances LTP. |
Western blot for SSH1 levels, cofilin localization assay, cofilin-actin rod assay, siRNA knockdown, in vivo genetic reduction (APP/PS1 x RanBP9 hemizygous), LTP electrophysiology, behavioral memory test |
Cell death & disease |
High |
25741591
|
| 2014 |
AXL and LRP-1 do not interact directly but rely on RANBP9, which binds both AXL and LRP-1, to form a tripartite complex that mediates DC efferocytosis; AXL binds apoptotic cells while LRP-1 triggers internalization. Targeted deletion of DC-specific LRP-1, AXL, or RANBP9 in mice increases AC accumulation, impairs viral antigen CD8+ T cell activation, and decreases survival. |
Co-immunoprecipitation, targeted genetic deletion in mice, in vivo spleen efferocytosis assay, antigen cross-presentation coculture assay, HSV-1 infection model |
The Journal of clinical investigation |
High |
24509082
|
| 2014 |
RanBPM promotes aggresome formation through interaction with HDAC6 and inhibition of its deacetylase activity; IR promotes RanBPM relocalization to aggresomes where it colocalizes with ubiquitin, dynein, and HDAC6. RanBPM deletion (LisH/CTLH domain) prevents both HDAC6 interaction and aggresome formation. |
Co-immunoprecipitation, HDAC6 deacetylase activity assay, confocal co-localization, shRNA knockdown, domain deletion mutants, aggresome formation assay |
Biology open |
High |
24795145
|
| 2014 |
RanBPM interacts with Tip60 histone acetyltransferase; this interaction dramatically relocalizes RanBPM to nuclear speckles, redirects AICD away from transcription factories, and has a negative effect on AICD-mediated nuclear signaling and AFT complex formation, reducing expression of AICD-regulated genes. |
Co-immunoprecipitation, confocal microscopy, reporter gene assay, nuclear spot formation assay |
Journal of Alzheimer's disease : JAD |
Medium |
25024339
|
| 2015 |
RanBPM subcellular localization is controlled by: (1) a dominant N-terminal proline/glutamine-rich motif conferring nuclear localization; (2) a C-terminal motif minimally contributing nuclear targeting; (3) a nuclear export signal (NES) whose mutation prevents cytoplasmic accumulation; and (4) cytoplasmic retention via protein-protein interactions through SPRY and LisH/CTLH domains. In the cytoplasm, RanBPM partially colocalizes with and associates with alpha-tubulin; in the nucleus it associates with chromatin. |
Systematic deletion/mutation analysis in RanBPM shRNA background, immunofluorescence, subcellular fractionation, co-immunoprecipitation with alpha-tubulin, chromatin association assay |
PloS one |
High |
25659156
|
| 2015 |
RanBPM (RanBPM55 isoform) binds Zta of EBV; acts as intermediary in Rta-Zta complex formation; enhances Zta-dependent transcriptional activity via inhibition of Zta sumoylation; RanBPM shRNA reduces synergistic activity of Zta and Rta and inhibits expression of lytic proteins. |
Co-immunoprecipitation, GST pull-down, luciferase reporter, sumoylation assay, shRNA knockdown |
The Journal of general virology |
Medium |
25900136
|
| 2016 |
RanBPM is an inhibitor of ERK signaling: RanBPM knockdown stimulates ERK phosphorylation and Bcl-2 upregulation; RanBPM inhibits MEK/ERK activation by active RasV12 and c-Raf, forms a complex with active c-Raf (via its C-terminal kinase domain), decreases binding of Hsp90 to c-Raf, and reduces endogenous c-Raf protein levels. Loss of RanBPM increases cell proliferation and migration. |
siRNA/shRNA knockdown, ERK phosphorylation assay, Ras activation assay, co-immunoprecipitation with c-Raf and Hsp90, cell proliferation and migration assay |
PloS one |
High |
23118896
|
| 2016 |
RanBPM crystal structure of the IUS-SPRY domain (including ~70 upstream residues) was determined; it forms a beta-sandwich fold with flanking helices. The SPRY domain surface binds a 20-mer peptide of DDX-4 (residues 228-247) with KD ~13 μM via a shallow binding surface formed by conserved loops, and mutagenesis identifies critical residues for this interaction. |
X-ray crystallography, isothermal titration calorimetry/binding assay, site-directed mutagenesis |
Journal of molecular biology |
High |
27622290
|
| 2016 |
RanBPM binds c-Kit receptor and is necessary for normal c-Kit protein expression in mouse testis and hematopoietic lineages; RanBPM deletion reduces c-Kit protein but not mRNA, indicating post-translational regulation specific to c-Kit. |
Co-immunoprecipitation, knockout mouse analysis, protein and mRNA quantification (Western blot and RT-PCR) |
Oncotarget |
Medium |
27835883
|
| 2016 |
RanBP9/TSSC3 complex, formed via RanBP9 SPRY domain and TSSC3 PH domain, forms a ternary complex with Src that suppresses both Src and Src-dependent Akt pathway activations, promotes anoikis, and suppresses metastasis in vivo. |
Co-immunoprecipitation, domain interaction mapping, Src/Akt activity assay, anoikis assay, anchorage-independent growth assay, in vivo metastasis model |
Cell death & disease |
Medium |
28032865
|
| 2016 |
ATM kinase phosphorylates RanBP9 on at least two residues (S181 and S603) in response to ionizing radiation; this promotes nuclear accumulation of RanBP9 in an ATM-dependent manner. RanBP9 silencing delays activation of ATM, Chk2, gamma-H2AX, and p53, and reduces homologous recombination-dependent DNA repair efficiency. |
Phosphorylation mapping, ATM inhibition, subcellular fractionation, siRNA knockdown, HR repair assay, gamma-H2AX foci analysis |
Oncotarget |
High |
26943034
|
| 2017 |
RanBP9 physically interacts with tau and with Hsp90/Hsc70 chaperone complexes; RanBP9 overexpression or knockdown directly increases or decreases tau levels in vitro and in vivo. RanBP9 enhances ATPase activities of Hsp90 and Hsc70 in vitro, and counteracts anti-tau efficacy of Hsp90/Hsc70 inhibitors. Genetic RanBP9 reduction ameliorates tauopathy in Tau-P301S mice. |
Co-immunoprecipitation, ATPase activity assay in vitro, overexpression/knockdown with tau quantification, Hsp90/Hsc70 inhibitor treatment, in vivo Tau-P301S mouse model with synaptic and plasticity readouts |
Human molecular genetics |
High |
29016855
|
| 2017 |
RanBPM, together with the CTLH complex members (muskelin, Twa1, MAEA, Rmnd5A), associates with HDAC6 and restricts cell migration through inhibition of HDAC6 alpha-tubulin deacetylase activity; RanBPM association with microtubules requires HDAC6; increased cell migration from RanBPM loss is due to relief of HDAC6 inhibition. |
Co-immunoprecipitation, HDAC6 deacetylase activity assay (acetylated alpha-tubulin levels), wound healing migration assay, confocal microscopy, shRNA knockdown of multiple CTLH members |
BMC cancer |
High |
28668087
|
| 2017 |
CLOCK interacts with RANBP9 in mouse testis (validated by co-immunoprecipitation in vitro and in vivo); RANBP9 also interacts with the spliceosome component SF3B3, and CLOCK interacts with SF3B3, suggesting RANBP9 mediates CLOCK's involvement in alternative splicing during spermatogenesis. |
Yeast two-hybrid, co-immunoprecipitation in vitro and in mouse testis, RNA-immunoprecipitation followed by high-throughput sequencing (RIP-Seq) |
Gene |
Medium |
29126923
|
| 2023 |
RanBPM physically interacts with p21 protein, deubiquitinates p21 by recruiting USP11 to maintain p21 protein stability, and translocates to the nucleus upon DNA damage in an ATM-dependent manner. RanBPM knockdown decreases p21 levels; overexpression increases p21 regardless of p53 status. RanBPM regulates DDR in a p21-dependent manner. |
Co-immunoprecipitation, in vivo ubiquitylation assay, protein stability assay, ATM inhibitor treatment, nuclear translocation analysis, p21-dependent functional rescue |
Cellular oncology |
High |
37676377
|
| 2025 |
In lung macrophages in vivo, RanBP9 is co-immunoprecipitated with all known CTLH complex members; the lung RanBP9-associated proteome includes macrophage-specific proteins and players in innate immune response, DNA damage response, metabolism, and mitochondrial function, revealing CTLH-complex-dependent and independent interactors. |
In vivo mouse model (RanBP9-TurnX x LysM-Cre), dual-tag co-immunoprecipitation with mass spectrometry, comparative proteomics |
Cell death discovery |
Medium |
40223093
|
| 2025 |
RANBP9 and RANBP10 independently support formation of the CTLH complex E3 ligase; they balance each other's expression, and acute overexpression of either reshapes the NSCLC cell proteome and ubiquitylome. Higher RANBP9/RANBP10 ratio associates with greater proliferation. RANBP9 and RANBP10 act as partial antagonists modulating CTLH complex ubiquitylation output. |
Inducible overexpression and loss-of-function cell lines, proteomics, ubiquitylome mass spectrometry, cell proliferation assay |
Journal of experimental & clinical cancer research |
Medium |
40883813
|