Affinage

CEP135

Centrosomal protein of 135 kDa · UniProt Q66GS9

Length
1140 aa
Mass
133.5 kDa
Annotated
2026-06-09
28 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CEP135 is a conserved coiled-coil centriolar protein that acts as a structural linker between the inner SAS-6 cartwheel hub and the outer triplet microtubules, organizing centriole architecture and centrosomal microtubule nucleation throughout the cell cycle (PMID:11781336, PMID:23511974). Its N-terminal domain forms a parallel two-stranded coiled coil that directly binds tubulin and microtubules and bundles them through a 13-residue lysine-containing site (residues 96–108), while its C-terminus binds hSAS-6 and its N-terminus binds the microcephaly protein CPAP to drive centriole elongation; loss of these interactions yields short centrioles with abnormal triplet number and dominant-negative blockade of centriole assembly (PMID:23511974, PMID:27477386). Across Drosophila, Tetrahymena, and Chlamydomonas, CEP135/Bld10 connects cartwheel spokes to triplet microtubules, sets inter-triplet spacing and triplet number, and stabilizes basal bodies against mechanical force (PMID:23115304, PMID:22976301, PMID:36093892). CEP135 additionally serves as a centriolar platform for C-NAP1, whose Nek2-dependent phosphorylation releases it from CEP135 to trigger centrosome disjunction at mitotic entry, and binds the dynactin subunit p50/dynamitin to support PCM and γ-tubulin retention and MTOC function (PMID:14983524, PMID:18851962, PMID:24695856). A short antagonistic splice isoform, CEP135mini, represses centriole duplication by competing for centriolar recruitment of SAS-6, CPAP, and γ-tubulin, and an increased CEP135full:mini ratio—set by alternative polyadenylation—drives centrosome amplification and mitotic errors in breast cancer cells (PMID:26412126, PMID:30811267). Conditional loss in germ cells causes acrosome, flagellar, and head-to-tail connection defects leading to male infertility, linking CEP135 to spermatogenesis (PMID:40095067).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2000 Medium

    Establishing whether Cep135 is itself a structural building block, EM of overexpressed protein showed it self-assembles into filamentous polymers, framing it as an intrinsic structural component rather than a passive marker.

    Evidence Tagged full-length and truncated construct expression in CHO/Sf9 cells with electron microscopy

    PMID:10842375

    Open questions at the time
    • Polymers were seen on overexpression, not in endogenous centrioles
    • No partner or microtubule-linkage role yet defined
  2. 2002 High

    To define the cellular role of the 135-kDa centrosomal protein, RNAi and deletion-construct overexpression established that Cep135 organizes centrosomal microtubules and carries three independent centrosome-targeting domains.

    Evidence Monoclonal antibody identification, RNAi, deletion overexpression, immunofluorescence

    PMID:11781336

    Open questions at the time
    • Molecular partners unknown
    • No structural mechanism for microtubule organization
  3. 2004 High

    Identifying a functional partner, a yeast two-hybrid screen mapped a direct Cep135 C-terminus–p50/dynamitin interaction required for centrosomal targeting of p50 and retention of γ-tubulin and pericentrin.

    Evidence Yeast two-hybrid, co-IP, domain-mapped immunostaining, RNAi in CHO cells

    PMID:14983524

    Open questions at the time
    • Link between dynactin recruitment and centriole structure unresolved
    • No in vitro reconstitution
  4. 2008 Medium

    Addressing centrosome cohesion, depletion and mutant studies showed CEP135 is a platform required for centriolar localization of C-NAP1, with loss causing premature centrosome splitting.

    Evidence RNAi, mutant overexpression, immunofluorescence

    PMID:18851962

    Open questions at the time
    • Direct CEP135–C-NAP1 binding not yet biochemically mapped
    • Regulation of the interaction unknown
  5. 2012 High

    Cross-species genetics defined the conserved structural role: CEP135/Bld10 nucleates and stabilizes central-pair and triplet microtubules, links inner and outer centriolar components, and maintains basal body integrity against ciliary force.

    Evidence Drosophila and Tetrahymena genetics, electron tomography, SIM, EM, MT-binding assays

    PMID:22898782 PMID:22976301 PMID:23115304

    Open questions at the time
    • Human counterpart of these structural roles not yet shown
    • Molecular determinants of inner-outer connection unmapped
  6. 2013 High

    Defining the core human mechanism, in vitro binding and dominant-negative assays established CEP135 as the linker bridging the hSAS-6 cartwheel hub to outer microtubules and to CPAP-driven centriole elongation; KO studies showed it restrains centrosome reduplication and preserves centriole structure.

    Evidence Co-IP, in vitro binding, RNAi, domain-mutant overexpression, EM; gene disruption in DT40 cells

    PMID:23511974 PMID:23864714

    Open questions at the time
    • Atomic basis of microtubule binding not yet resolved
    • How linker function integrates with reduplication control unclear
  7. 2014 High

    Mechanism of cohesion control and asymmetry was clarified: Nek2 multisite phosphorylation of C-Nap1 disrupts its mitotic binding to Cep135 to drive disjunction, and Drosophila Bld10 mediates Polo shedding to establish centrosome asymmetry.

    Evidence In vitro kinase assays, endogenous co-IP across cell cycle, phosphomutants; Drosophila mutant live imaging

    PMID:24695856 PMID:24954048

    Open questions at the time
    • Whether Polo shedding role is conserved in humans untested
    • Phosphosite-level control of CEP135 itself unknown
  8. 2015 Medium

    Discovery of an antagonistic regulatory layer: a short CEP135mini isoform with distinct cell-cycle localization represses centriole duplication by limiting recruitment of SAS-6, CPAP, and γ-tubulin.

    Evidence Isoform-specific overexpression/knockdown, immunofluorescence, cell-cycle staging

    PMID:26412126

    Open questions at the time
    • Direct competition mechanism not biochemically dissected
    • Single-lab finding
  9. 2016 High

    Structural work resolved the microtubule-binding mechanism: the N-terminal 158 residues form a parallel two-stranded coiled coil that binds and bundles microtubules via a lysine-rich 13-residue site.

    Evidence X-ray crystallography, SAXS, cryo-EM, in vitro MT binding/bundling, mutagenesis

    PMID:27477386

    Open questions at the time
    • Structure of SAS-6 and CPAP binding regions not solved
    • Full-length architecture unknown
  10. 2019 Medium

    Linking isoform balance to disease, manipulating the CEP135full:mini ratio (set by alternative polyadenylation) demonstrated that excess full-length drives centrosome amplification and mitotic errors in breast cancer cells.

    Evidence Isoform induction, centrosome/spindle phenotyping, polyadenylation-signal genome editing

    PMID:30811267

    Open questions at the time
    • Causal role in tumorigenesis in vivo untested
    • Upstream control of polyadenylation choice unknown
  11. 2022 Medium

    CRISPR KO and complex identification refined the picture: CEP135 supports PCM recruitment and MTOC function and forms a complex with satellite proteins SSX2IP and WDR8, though mitotic compensation permits viable proliferation.

    Evidence CRISPR KO, immunofluorescence, co-IP

    PMID:35406752

    Open questions at the time
    • Nature of mitotic compensation undefined
    • Functional role of SSX2IP/WDR8 complex unmapped
  12. 2022 High

    Cryo-EM and immunoEM in Chlamydomonas showed Bld10p/Cep135 crosslinks adjacent triplets and sets inter-triplet distance, controlling triplet number independently of the cartwheel.

    Evidence Chlamydomonas mutants, immunoEM with HA tagging, conventional and cryo-EM

    PMID:36093892

    Open questions at the time
    • Human conservation of inter-triplet spacing role not directly shown
    • Binding partners on the triplet side unidentified
  13. 2025 Medium

    Newer studies extended CEP135 function to upstream regulation (LZTS2 limits centrosomal CEP135 and MT nucleation), a distal luminal ring scaffold, and a tissue role in spermatogenesis via SPATA6/AKAP3.

    Evidence RNAi epistasis with imaging; U-ExM and cryo-ET; conditional germ-cell KO with EM, proteomics, co-IP

    PMID:40095067 PMID:40521914 PMID:bio_10.1101_2025.06.17.660204

    Open questions at the time
    • CEP135's direct role in the luminal ring inferred from C2CD3 depletion, not CEP135 manipulation (preprint)
    • Mechanism of LZTS2 regulation of CEP135 unknown
    • How germ-cell partners connect to centriolar structural role unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How CEP135's distinct binding interfaces (SAS-6, CPAP, C-NAP1, p50, satellite and luminal-ring partners) are spatially and temporally coordinated on a single molecule to build, link, and maintain the centriole remains unresolved.
  • No full-length structure integrating multiple interaction domains
  • Order of assembly and competition among partners undefined
  • In vivo disease relevance of isoform imbalance untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 4 GO:0008092 cytoskeletal protein binding 4 GO:0060090 molecular adaptor activity 3
Localization
GO:0005815 microtubule organizing center 4 GO:0005856 cytoskeleton 2 GO:0005929 cilium 2
Pathway
R-HSA-1640170 Cell Cycle 3 R-HSA-1852241 Organelle biogenesis and maintenance 3 R-HSA-1474165 Reproduction 1
Partners
AKAP3CEP250CPAPDCTN2SASS6SPATA6SSX2IPWDR8
Complex memberships
CEP135–SSX2IP–WDR8 complexdistal centriole luminal ring (C2CD3/SFI1/centrin-2/CEP135/NA14)

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 Cep135 is a 135-kDa coiled-coil centrosomal protein that localizes to the centrosome throughout the cell cycle, independent of the microtubule network. It distributes in association with electron-dense pericentriolar material. Three independent centrosome-targeting domains were identified by deletion construct analysis. Overexpression or RNAi suppression both caused disorganization of interphase and mitotic spindle microtubules, establishing a role in centrosomal microtubule organization. Monoclonal antibody identification, deletion construct overexpression, RNA interference, immunofluorescence microscopy The Journal of cell biology High 11781336
2000 Overexpressed Cep135 assembles into filamentous polymers and whorl-like particles composed of ~7 nm parallel dense lines both at the centrosome and in the cytoplasm, with the polymer architecture dependent on specific domains of the protein, indicating Cep135 is a structural self-assembling component of the centrosome. Transient transfection of HA/GFP-tagged full-length and truncated constructs in CHO cells and baculovirus expression in Sf9 cells, electron microscopy Microscopy research and technique Medium 10842375
2004 Cep135 directly interacts with the p50 dynactin subunit (dynamitin) via the C-terminal sequence of Cep135 binding the central domain of p50. This interaction is required for centrosomal targeting of p50; exogenous p50 lacking the Cep135-binding domain failed to localize to the centrosome. Altered levels of either protein displaced the other as well as γ-tubulin and pericentrin, leading to microtubule disorganization. Yeast two-hybrid screen, co-immunoprecipitation, immunostaining of co-expressed binding domains in CHO cells, RNAi, overexpression Cell motility and the cytoskeleton High 14983524
2008 CEP135 acts as a platform protein for C-NAP1 at the centriole. Depletion of CEP135 caused premature centrosome splitting accompanied by specific reduction of centrosomal C-NAP1 levels. Ectopic expression of CEP135 mutant proteins also caused centrosome splitting with reduced centrosomal C-NAP1, establishing CEP135 as required for C-NAP1 centriolar localization. RNAi knockdown, overexpression of CEP135 mutants, immunofluorescence microscopy Experimental cell research Medium 18851962
2012 CEP135/Bld10 can bind and stabilize microtubules and is required for the early steps of central microtubule pair formation in Drosophila flagella. Assembly of the central MT pair begins prior to meiotic divisions with nucleation of a singlet MT within the basal body, and BLD10/CEP135 is essential for this early nucleation step. Drosophila genetic analysis, electron microscopy of spermatogenesis, MT binding/stabilization assays Developmental cell High 22898782
2012 In Tetrahymena, Bld10/Cep135 is an outer cartwheel domain protein that stabilizes basal bodies to resist the forces generated by ciliary beating. Bld10 promotes stability of the A- and C-tubules of the triplet microtubules and proper positioning of the triplet MT blades. In bld10Δ cells, ciliary beating forces promote basal body disassembly, revealing a role in basal body maintenance distinct from its assembly role. Tetrahymena genetic deletion, electron microscopy, live-cell analysis of basal body dynamics Molecular biology of the cell High 23115304
2012 In Drosophila, Cep135/Bld10 is not essential for cartwheel formation or establishing the ninefold symmetry of centrioles. However, absence of Cep135/Bld10 leads to increased centriole width and progressive cartwheel disassembly over time. Cep135/Bld10 localizes between inner (SAS-6, Ana2) and outer (Asl, DSpd-2, D-PLP) centriolar components and stabilizes the connection between these inner and outer components. Drosophila Cep135/Bld10 mutant analysis, electron tomography, 3D structured illumination microscopy (SIM) Journal of cell science High 22976301
2013 Human CEP135 directly interacts with hSAS-6 via its carboxyl-terminus and with microtubules via its amino-terminus. CEP135 also interacts with microcephaly protein CPAP via its amino-terminal domain. CEP135 depletion perturbed centriolar localization of CPAP, blocked CPAP-induced centriole elongation, and caused abnormal centriole structures with altered numbers of MT triplets and shorter centrioles. A CEP135 mutant lacking the hSAS-6 interaction had a dominant-negative effect on centriole assembly, establishing CEP135 as a linker between the SAS-6 cartwheel hub and outer MTs. Co-immunoprecipitation, in vitro binding assays, RNAi depletion, overexpression of domain mutants, immunofluorescence and electron microscopy The EMBO journal High 23511974
2013 Disruption of Cep135 in DT40 chicken cells produces viable cells with a small decrease in centriole numbers, increased monopolar spindles, and an atypical structure in the centriole lumen by electron microscopy. Cep135 loss significantly increases centrosome amplification after S-phase arrest (hydroxyurea treatment), indicating Cep135 inhibits centrosome reduplication during S-phase delay and is required for structural integrity of centrioles. Targeted gene disruption in DT40 cells, electron microscopy, flow cytometry, immunofluorescence Molecular biology of the cell High 23864714
2014 Nek2-mediated multisite phosphorylation of C-Nap1's C-terminal domain perturbs its interaction with Cep135. Interaction between endogenous C-Nap1 and Cep135 is specifically lost in mitosis. Phosphorylation of C-Nap1 leads to loss of oligomerization and centrosome association, and loss of Cep135 binding contributes to centrosome disjunction at mitotic entry. In vitro kinase assay, co-immunoprecipitation of endogenous proteins across cell cycle stages, phosphomimetic/non-phosphorylatable mutant analysis Journal of cell science High 24695856
2014 The Drosophila ortholog Bld10 (Cep135) is required to establish centrosome asymmetry in neuroblasts by mediating shedding of Polo kinase from the mother centrosome. bld10 mutants fail to downregulate Polo and PCM from the mother centrosome, generating two active MTOCs, causing spindle alignment defects, centrosome segregation errors, and incorrect retention of the older mother centrosome by neuroblasts. Drosophila bld10 mutant analysis, live imaging, immunofluorescence microscopy Current biology : CB High 24954048
2016 The N-terminal 158 residues of human CEP135 form a parallel two-stranded coiled-coil structure. This domain binds tubulin, protofilaments, and microtubules in vitro and induces MT bundle formation. A 13-amino-acid segment (residues 96–108) represents the major MT-binding site, containing three lysine residues that contribute to the MT bundling activity. X-ray crystallography, small-angle X-ray scattering (SAXS), cryo-electron microscopy, fluorescence microscopy, in vitro MT binding/bundling assays, site-directed mutagenesis Structure (London, England : 1993) High 27477386
2015 A short splice isoform of CEP135 (CEP135mini) represses centriole duplication by limiting centriolar localization of CEP135full binding partners SAS-6 and CPAP, and pericentriolar localization of γ-tubulin. CEP135mini and CEP135full have distinct and complementary centrosomal localizations during the cell cycle; CEP135mini decreases from centrosomes at anaphase onset, which is proposed to allow new centriole assembly. Isoform-specific overexpression and knockdown, immunofluorescence microscopy, cell cycle staging Current biology : CB Medium 26412126
2019 The ratio of full-length CEP135 (CEP135full) to CEP135mini is increased in breast cancer cell lines with high centrosome amplification. Inducing expression of CEP135full increases centrosome amplification frequency, multipolar spindles, anaphase-lagging chromosomes, and micronuclei; inducing CEP135mini reduces centrosome number. The differential isoform expression is regulated by alternative polyadenylation. Directed mutations near the CEP135mini alternative polyadenylation signal reduce the CEP135full:mini ratio and decrease centrosome amplification. Isoform-specific induction in breast cancer cell lines, immunofluorescence for centrosome number and spindle phenotypes, genome editing of polyadenylation signal Molecular biology of the cell Medium 30811267
2022 CEP135 loss-of-function (CRISPR knockout) in human cells causes compromised PCM recruitment, reduced MTOC function, and premature centrosome splitting with imbalanced PCMs during interphase. However, defective CEP135 KO centrosomes compensate during mitosis to establish balanced spindle poles, allowing unperturbed mitosis and regular cell proliferation. CEP135 was also found to form a complex with centriolar satellite proteins SSX2IP and WDR8 before centrosome assembly. CRISPR knockout, immunofluorescence microscopy, co-immunoprecipitation Cells Medium 35406752
2022 In Chlamydomonas, Bld10p/Cep135 connects cartwheel spokes to triplet microtubules and determines the inter-triplet distance in the centriole, thereby regulating the number of triplet microtubules in a cartwheel-independent manner. Truncated Bld10p in cartwheel-deficient centrioles significantly reduces the inter-triplet distance and frequently generates eight-microtubule centrioles. Immunoelectron microscopy localized hemagglutinin-tagged Bld10p along two lines connecting adjacent triplets, corresponding to crosslinking structures identified by conventional and cryo-EM. Chlamydomonas mutant analysis, immunoelectron microscopy with HA epitope tagging, conventional and cryo-electron microscopy The EMBO journal High 36093892
2025 LZTS2 negatively regulates centrosomal CEP135 levels. Depletion of LZTS2 increases microtubule nucleation at the centrosome, and this effect is dependent on CEP135 since depletion of LZTS2 partially rescues impaired centrosome microtubule nucleation caused by CEP135 knockdown. RNAi knockdown of LZTS2 and CEP135, fluorescence microscopy for centrosomal CEP135 levels and microtubule nucleation assays, epistasis analysis Cytoskeleton (Hoboken, N.J.) Medium 40521914
2025 CEP135 is a component of a luminal ring network at the distal centriole that includes C2CD3/SFI1/centrin-2/CEP135/NA14. C2CD3 depletion destabilizes this luminal ring network, placing CEP135 within an architectural scaffold at the distal centriole lumen connected to the distal microtubule cap and appendages. Ultrastructure Expansion Microscopy (U-ExM), iterative U-ExM, cryo-electron tomography, RNAi depletion bioRxivpreprint Medium bio_10.1101_2025.06.17.660204
2025 CEP135 interacts with spermatogenic proteins SPATA6 and AKAP3, regulating their expression and stability. Conditional knockout of Cep135 in premeiotic germ cells (Stra8-Cre) causes defects in acrosome formation, flagellum structure, and head-to-tail connections during spermatogenesis, leading to oligoasthenoteratozoospermia and male infertility, without affecting premeiosis. Conditional knockout (Stra8-Cre × Cep135flox/flox), scanning and transmission electron microscopy, proteomics, co-immunoprecipitation Cellular and molecular life sciences : CMLS Medium 40095067
2023 CEP135 promotes endothelial cell migration by mediating centrosome polarization and microtubule stability. CEP135 siRNA inhibits in vivo angiogenesis. CEP135 affects spindle orientation and mediates cell cycle progression in endothelial cells. A tubulin turbidity assay confirmed CEP135 promotes microtubule stabilization. siRNA knockdown, tube formation assay, in vivo angiogenesis assay, wound healing and transwell migration assays, tubulin turbidity assay, flow cytometry Frontiers in bioscience (Landmark edition) Low 38062802

Source papers

Stage 0 corpus · 28 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 Human microcephaly protein CEP135 binds to hSAS-6 and CPAP, and is required for centriole assembly. The EMBO journal 166 23511974
2012 A truncating mutation of CEP135 causes primary microcephaly and disturbed centrosomal function. American journal of human genetics 138 22521416
2002 Characterization of Cep135, a novel coiled-coil centrosomal protein involved in microtubule organization in mammalian cells. The Journal of cell biology 119 11781336
2017 A homozygous CEP135 mutation is associated with multiple morphological abnormalities of the sperm flagella (MMAF). Gene 114 28866084
2012 BLD10/CEP135 is a microtubule-associated protein that controls the formation of the flagellum central microtubule pair. Developmental cell 83 22898782
2012 Bld10/Cep135 stabilizes basal bodies to resist cilia-generated forces. Molecular biology of the cell 62 23115304
2012 Drosophila Cep135/Bld10 maintains proper centriole structure but is dispensable for cartwheel formation. Journal of cell science 58 22976301
2008 A novel function of CEP135 as a platform protein of C-NAP1 for its centriolar localization. Experimental cell research 55 18851962
2014 Multisite phosphorylation of C-Nap1 releases it from Cep135 to trigger centrosome disjunction. Journal of cell science 53 24695856
2014 The centriolar protein Bld10/Cep135 is required to establish centrosome asymmetry in Drosophila neuroblasts. Current biology : CB 44 24954048
2020 An update of pathogenic variants in ASPM, WDR62, CDK5RAP2, STIL, CENPJ, and CEP135 underlying autosomal recessive primary microcephaly in 32 consanguineous families from Pakistan. Molecular genetics & genomic medicine 32 32677750
2016 The Human Centriolar Protein CEP135 Contains a Two-Stranded Coiled-Coil Domain Critical for Microtubule Binding. Structure (London, England : 1993) 29 27477386
2019 CEP135 isoform dysregulation promotes centrosome amplification in breast cancer cells. Molecular biology of the cell 25 30811267
2013 Abnormal centrosomal structure and duplication in Cep135-deficient vertebrate cells. Molecular biology of the cell 24 23864714
2004 Interaction of Cep135 with a p50 dynactin subunit in mammalian centrosomes. Cell motility and the cytoskeleton 24 14983524
2015 A Short CEP135 Splice Isoform Controls Centriole Duplication. Current biology : CB 18 26412126
2022 Bld10p/Cep135 determines the number of triplets in the centriole independently of the cartwheel. The EMBO journal 8 36093892
2022 Mitotic Maturation Compensates for Premature Centrosome Splitting and PCM Loss in Human cep135 Knockout Cells. Cells 7 35406752
2000 Filamentous polymers induced by overexpression of a novel centrosomal protein, Cep135. Microscopy research and technique 7 10842375
2023 CP110 and CEP135 localize near the proximal and distal centrioles of cattle and human spermatozoa. microPublication biology 5 37822686
2018 The Association of CEP135 rs4865047 and NPY2R rs1902491 Single Nucleotide Polymorphisms (SNPs) with Rapid Progression of Proliferative Diabetic Retinopathy in Patients with Type 1 Diabetes Mellitus. Medical science monitor : international medical journal of experimental and clinical research 5 30531682
2024 CP110 and CEP135 Localize Near the Proximal Centriolar Remnants of Mice Spermatozoa. microPublication biology 3 38351906
2021 CEP135 associated primary microcephaly-A rare presentation in early second trimester. European journal of medical genetics 3 33933664
2025 Loss of Cep135 causes oligoasthenoteratozoospermia and male infertility in mice. Cellular and molecular life sciences : CMLS 2 40095067
2023 miR-26b Targets CEP135 Gene to Regulate Nasopharyngeal Carcinoma Proliferation and Migration by NF-κB Pathway. Molecular biotechnology 2 36820950
2023 Centrosomal Protein CEP135 Regulates the Migration and Angiogenesis of Endothelial Cells in a Microtubule-Dependent Manner. Frontiers in bioscience (Landmark edition) 1 38062802
2026 Single-cell inflammatory signaling defines a novel CEP135+ endothelial subtype associated with glioma progression. Translational oncology 0 41861657
2025 LZTS2 Negatively Regulates Centrosomal CEP135 Levels and Microtubule Nucleation. Cytoskeleton (Hoboken, N.J.) 0 40521914

Missed literature

Know a paper Affinage missed for CEP135? Flag it for the maintainers and the community.

No submissions yet.