DNAH9 (dynein axonemal heavy chain 9) is a beta-type heavy chain of the outer dynein arm (ODA), the ATPase motor that drives the beating of motile cilia by sliding outer doublet microtubules towards their minus ends. It has the dynein heavy chain architecture of an N-terminal tail that assembles into the arm and a C-terminal AAA+ motor head with a microtubule-binding stalk. In human respiratory cilia DNAH9 is restricted to the distal part of the axoneme, where it forms type 2 ODAs together with the gamma chain DNAH5 and the intermediate chain DNAI2; the proximal ODAs instead contain its paralog DNAH11, and human sperm ODAs contain a third beta paralog, DNAH17. DNAH9 binds the ODA docking complex subunit ODAD1 (CCDC114) through its N-terminal tail, which is thought to dock distal ODAs onto the doublet. DNAH9 is expressed early in airway ciliogenesis, before cilia appear, and in pit cells of the embryonic node. Biallelic loss-of-function variants cause primary ciliary dyskinesia 40 (CILD40). Distal type 2 ODAs are lost, cilia beat more slowly with a subtle waveform defect, and respiratory symptoms are mild, but situs inversus and other laterality defects are common.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003341 cilium movement | IMP PMID:30471717 Mutations in Outer Dynein Arm Heavy Chain DNAH9 Cause Motile... | ACCEPT | Summary: DNAH9-mutant respiratory cilia lose distal type 2 ODAs and beat more slowly with a subtle waveform defect; Paramecium knockdown confirms a conserved role in motility. Reason: Core biological process. Supporting Evidence: PMID:30471717 This confers a reduced beating frequency with a subtle beating pattern defect affecting the motility of the distal cilia portion. PMID:30471717 Paramecium DNAH9 knockdown confirms an evolutionarily conserved function for DNAH9 in cilia motility and ODA stability. |
| GO:0005515 protein binding | IPI PMID:30471718 Recessive DNAH9 Loss-of-Function Mutations Cause Laterality ... | MODIFY | Summary: Yeast two-hybrid and co-immunoprecipitation show that the DHC1 region of DNAH9 (aa 201-859) binds the ODA docking complex subunit ODAD1 (CCDC114). Reason: The interaction is real and informative: it is proposed to dock type 2 ODAs onto the doublet. Protein binding says nothing about this. ODAD1 is a subunit of the outer dynein arm docking complex (GO:0120228), so protein-containing complex binding is the closest informative existing term; a dedicated docking-complex binding term does not exist (see suggested_questions). Proposed replacements: protein-containing complex binding Supporting Evidence: PMID:30471718 We conclude that DNAH9 is essential for ODA type 2 assembly and our data indicate that docking of ODAs type 2 occurs via direct interaction of DNAH9 with the docking complex protein CCDC114. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro-based ATP binding from the dynein heavy chain AAA+ motor domain. Reason: Correct: the DNAH9 motor head carries the AAA1 P-loop that binds and hydrolyses ATP, but ATP binding is a generic part of the motor activity captured by the microtubule motor activity annotations. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function. |
| GO:0005814 centriole | IDA GO_REF:0000052 | MARK AS OVER ANNOTATED | Summary: Human Protein Atlas immunofluorescence of DNAH9 at the centriole. Reason: DNAH9 acts in the distal axoneme of motile cilia. Antibody signal at centrioles in cultured cells is not supported by any other study; at most it could reflect basal-body accumulation of unassembled dynein, as seen for DNAH5 in mutant cells. Not a functional location. Supporting Evidence: PMID:30471717 DNAH9 and its partner heavy chain DNAH5 localize to type 2 ODAs of the distal cilium |
| GO:0005930 axoneme | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT annotation (node PTN000073047) placing the axonemal outer-arm beta heavy chains in the axoneme. Reason: Consistent with direct immunofluorescence of DNAH9 in respiratory ciliary axonemes. Supporting Evidence: PMID:18950741 Respiratory cilia contain at least two distinct ODA types: type 1, DNAH9 negative and DNAH5 positive (proximal ciliary axoneme); and type 2, DNAH9 and DNAH5 positive (distal ciliary axoneme). |
| GO:0005930 axoneme | IDA PMID:11104725 Characterization of an axonemal dynein heavy chain expressed... | ACCEPT | Summary: Antibodies to this dynein heavy chain (later named DNAH9) stain the cilia of mature airway epithelium. Reason: Direct localization in airway cilia. Supporting Evidence: PMID:11104725 immunohistochemical localization of the gene product confirmed its presence in the cilia of mature airway epithelium |
| GO:0005930 axoneme | IDA PMID:11839535 Axonemal dynein expression in human fetal tracheal epitheliu... | ACCEPT | Summary: DNAH9 antigen labels new ciliary beds in human fetal trachea. Reason: Consistent with axonemal localization. Supporting Evidence: PMID:11839535 From 12 to 22 wk, immunocytochemical labeling of new ciliary beds was prominent |
| GO:0005930 axoneme | IDA PMID:15750039 Mislocalization of DNAH5 and DNAH9 in respiratory cells from... | ACCEPT | Summary: DNAH9 shows a regional distribution along the respiratory ciliary axoneme. Reason: Direct localization. Supporting Evidence: PMID:15750039 In normal ciliated airway epithelium, DNAH5 and DNAH9 show a specific regional distribution along the ciliary axoneme, indicating the existence of at least two distinct ODA types. |
| GO:0005930 axoneme | IDA PMID:18950741 DNAI2 mutations cause primary ciliary dyskinesia with defect... | ACCEPT | Summary: DNAH9 marks distal type 2 ODAs in the respiratory axoneme. Reason: Direct localization. Supporting Evidence: PMID:18950741 Respiratory cilia contain at least two distinct ODA types: type 1, DNAH9 negative and DNAH5 positive (proximal ciliary axoneme); and type 2, DNAH9 and DNAH5 positive (distal ciliary axoneme). |
| GO:0005930 axoneme | IDA PMID:23849778 ARMC4 mutations cause primary ciliary dyskinesia with random... | ACCEPT | Summary: DNAH9 staining used as a distal ODA marker in the ARMC4 study. Reason: The abstract does not name DNAH9, but the curator had the full text, and axonemal DNAH9 is shown in several other papers. Supporting Evidence: PMID:23849778 We demonstrate that ARMC4 is an axonemal protein that is necessary for proper targeting and anchoring of ODAs. |
| GO:0005930 axoneme | IDA PMID:31178125 Mutations in DNAH17, Encoding a Sperm-Specific Axonemal Oute... | ACCEPT | Summary: DNAH9 is found along the respiratory ciliary axoneme but not along the sperm axoneme. Reason: Direct localization in respiratory cilia. Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0005930 axoneme | IEA GO_REF:0000120 | ACCEPT | Summary: Combined electronic annotation of axoneme. Reason: Agrees with the IDA annotations. Supporting Evidence: PMID:18950741 Respiratory cilia contain at least two distinct ODA types: type 1, DNAH9 negative and DNAH5 positive (proximal ciliary axoneme); and type 2, DNAH9 and DNAH5 positive (distal ciliary axoneme). |
| GO:0007017 microtubule-based process | IEA GO_REF:0000117 | TOO GENERAL | Summary: ARBA prediction of microtubule-based process. Reason: True but uninformative: microtubule-based process is entailed by the cilium movement process asserted elsewhere in this review, which is the specific process this motor drives. Supporting Evidence: PMID:31178125 the outer dynein arms (ODAs), through ATPase activity of their heavy chains (HCs), play a major role for cilia and flagella beating |
| GO:0007018 microtubule-based movement | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro mapping to microtubule-based movement. Reason: True but very general: the movement produced by this motor is microtubule sliding within the axoneme, and microtubule-based movement is entailed by the cilium movement process asserted elsewhere in this review. Supporting Evidence: PMID:31178125 the outer dynein arms (ODAs), through ATPase activity of their heavy chains (HCs), play a major role for cilia and flagella beating |
| GO:0008569 minus-end-directed microtubule motor activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT places minus-end-directed motor activity at the deep dynein heavy chain node PTN000743491, grounded in experimental data for cytoplasmic and axonemal dyneins from yeast, Dictyostelium and C. elegans. Reason: DNAH9 sits inside this clade and retains an intact motor domain, so there is no reason to think the inherited activity was lost. This is the core molecular function of an outer dynein arm heavy chain. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Produces force towards the minus ends of microtubules PMID:31178125 the outer dynein arms (ODAs), through ATPase activity of their heavy chains (HCs), play a major role for cilia and flagella beating |
| GO:0008569 minus-end-directed microtubule motor activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro mapping of the dynein heavy chain motor domain to minus-end-directed microtubule motor activity. Reason: DNAH9 is a full-length outer dynein arm heavy chain with all six AAA modules and a stalk ending in a microtubule-binding domain. Axonemal dyneins walk towards microtubule minus ends, which is what drives sliding of adjacent doublets. Consistent with the IBA and with the ODA-loss phenotypes. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Produces force towards the minus ends of microtubules PMID:31178125 the outer dynein arms (ODAs), through ATPase activity of their heavy chains (HCs), play a major role for cilia and flagella beating |
| GO:0030286 dynein complex | IBA GO_REF:0000033 | MODIFY | Summary: PAINT annotation of dynein complex at the deep dynein heavy chain node. Reason: Correct but too general. The PAINT tree places the outer-arm gamma heavy chain (DNAH5) under an outer dynein arm node, but the beta heavy chains DNAH9 and DNAH11 receive only the generic dynein complex term. The specific complex for DNAH9 is the outer dynein arm. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000743491 Β· PTN000743491 SUPPORTS TRANSFER Dynein complex membership is correct for all descendants but less specific than outer dynein arm. Proposed replacements: outer dynein arm Supporting Evidence: PMID:31178125 However, the contribution of the different HCs (Ξ³-type: DNAH5 and DNAH8 and Ξ²-type: DNAH9, DNAH11, and DNAH17) in ODAs from both organelles is unknown. |
| GO:0030286 dynein complex | IEA GO_REF:0000002 | MODIFY | Summary: InterPro mapping to the generic dynein complex. Reason: Correct but too general. DNAH9 is a heavy chain of the axonemal outer dynein arm. Proposed replacements: outer dynein arm Supporting Evidence: PMID:31178125 However, the contribution of the different HCs (Ξ³-type: DNAH5 and DNAH8 and Ξ²-type: DNAH9, DNAH11, and DNAH17) in ODAs from both organelles is unknown. |
| GO:0031514 motile cilium | IDA PMID:31178125 Mutations in DNAH17, Encoding a Sperm-Specific Axonemal Oute... | ACCEPT | Summary: DNAH9 is present in respiratory motile cilia. Reason: Correct; more specific terms (9+2 motile cilium, distal portion of axoneme) also apply. Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0031514 motile cilium | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location mapping to motile cilium. Reason: Correct but general. Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0036126 sperm flagellum | IDA PMID:39503742 DNAH3 deficiency causes flagellar inner dynein arm loss and ... | UNDECIDED | Summary: Annotation from a DNAH3 sperm study, presumably from DNAH9 immunostaining of human sperm. Reason: This conflicts with PMID:31178125, which found DNAH9 absent from the human sperm axoneme, and with the replacement of DNAH9 by DNAH17 in sperm ODAs. The cached text of PMID:39503742 mentions DNAH9 only in a Discussion list of PCD-causing DNAH genes and the figure is not available, so the basis of the annotation cannot be checked here. Not removed because the curator saw the figures. Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0036157 outer dynein arm | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer of outer dynein arm from mouse Dnah9. Reason: Core cellular component: DNAH9 is the beta heavy chain of distal (type 2) ODAs and binds the docking complex, DNAH5 and DNAI2. Supporting Evidence: PMID:30471717 DNAH9 and its partner heavy chain DNAH5 localize to type 2 ODAs of the distal cilium PMID:30471718 Consistent with our high-resolution IF microscopy results, we found interaction of DNAH9 fragment 4 containing the DHC2 domain with both DNAH5 fragments and full-length DNAI2, indicating that DNAH9 is indeed interacting with ODA proteins localized in the distal ciliary axonemes (Figures S19B and S19C). |
| GO:0045505 dynein intermediate chain binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT annotation at node PTN000743491, grounded in Dictyostelium cytoplasmic dynein heavy chain data. Reason: The axonemal ODA heavy chains also assemble with intermediate chains (DNAI1/DNAI2), so placing the function at the shared dynein heavy chain node is defensible for this branch. Kept as a structural, non-core binding activity. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Part of the ciliary outer dynein arms (ODAs), at least consisting of dynein axonemal heavy chains, light chains and intermediate chains |
| GO:0045505 dynein intermediate chain binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro (IPR026983, dynein heavy chain family) mapping to dynein intermediate chain binding. Reason: Outer dynein arms contain the intermediate chains DNAI1 and DNAI2 bound to the heavy-chain tails, so the binding is plausible. It is a structural interaction within the complex rather than the protein's primary activity. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Part of the ciliary outer dynein arms (ODAs), at least consisting of dynein axonemal heavy chains, light chains and intermediate chains |
| GO:0051959 dynein light intermediate chain binding | IBA GO_REF:0000033 | REMOVE | Summary: PAINT places light intermediate chain binding at the deep dynein heavy chain node PTN000743491. All the descendant experimental evidence comes from cytoplasmic dynein 1 heavy chain (human DYNC1H1, mouse and rat Dync1h1). Reason: Premise: the outer dynein arm contains no light intermediate chain subunit. It is built from heavy, intermediate and light chains (UniProt SUBUNIT, quoted below), whereas light intermediate chains (DYNC1LI1/2, DYNC2LI1) are subunits of cytoplasmic dyneins. An ODA heavy chain therefore has no light intermediate chain partner to bind, so the claim is not merely under-evidenced but unlikely to be correct. The PAINT node is too deep for this function: every WITH/FROM donor is a cytoplasmic dynein 1 heavy chain, and the axonemal ODA heavy-chain branch should not inherit the activity. This is an electronic inference contradicted on structural grounds, so REMOVE rather than MARK_AS_OVER_ANNOTATED. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN000743491 Β· PTN000743491 SUPPORTS SOURCE BUT NOT TARGET Deep dynein heavy chain node; light intermediate chain binding is grounded only in cytoplasmic dynein 1 heavy chains. UniProtKB:Q14204 Β· DYNC1H1 SUPPORTS SOURCE BUT NOT TARGET Cytoplasmic dynein 1 heavy chain binds DYNC1LI1/2; axonemal outer arm dyneins have no LIC subunit. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Part of the ciliary outer dynein arms (ODAs), at least consisting of dynein axonemal heavy chains, light chains and intermediate chains |
| GO:0051959 dynein light intermediate chain binding | IEA GO_REF:0000002 | REMOVE | Summary: InterPro family mapping to dynein light intermediate chain binding. Reason: Premise: the outer dynein arm contains no light intermediate chain subunit. It is built from heavy, intermediate and light chains (UniProt SUBUNIT, quoted below), whereas light intermediate chains (DYNC1LI1/2, DYNC2LI1) are subunits of cytoplasmic dyneins. The InterPro family mapping therefore transfers a cytoplasmic-dynein interaction to an axonemal heavy chain that has no light intermediate chain partner; the claim is unlikely to be correct, not merely under-supported, so it is removed. Supporting Evidence: file:human/DNAH9/DNAH9-uniprot.txt Part of the ciliary outer dynein arms (ODAs), at least consisting of dynein axonemal heavy chains, light chains and intermediate chains |
| GO:0060294 cilium movement involved in cell motility | IBA GO_REF:0000033 | MODIFY | Summary: PAINT annotation of cilium movement involved in cell motility at node PTN000743491, grounded largely in sperm-flagellar and protist dynein heavy chains. Reason: The node placement is reasonable for the dynein family as a whole, but DNAH9 is a respiratory-type outer dynein arm heavy chain. It is absent from the human sperm axoneme, where DNAH8 and DNAH17 replace it, so in humans it drives cilia that move fluid (airway, and nodal cilia for left-right patterning) rather than cells. Cilium movement that moves extracellular fluid is the accurate process. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: PANTHER:PTN000743491 Β· PTN000743491 SUPPORTS SOURCE BUT NOT TARGET Function holds for sperm-flagellar and protist dynein heavy chains; the human respiratory ODA heavy chains act in fluid-moving cilia. Proposed replacements: epithelial cilium movement involved in extracellular fluid movement Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0097229 sperm end piece | IDA GO_REF:0000052 | MARK AS OVER ANNOTATED | Summary: Human Protein Atlas immunofluorescence signal in the sperm end piece. Reason: Contradicted by direct immunofluorescence with validated antibodies showing that DNAH9 is absent from the human sperm axoneme, whose ODA beta heavy chain is DNAH17 (PMID:31178125). Cross-reaction of the HPA antibody with DNAH17 is a plausible explanation. Not removed because the HPA images were not re-examined here. Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0097229 sperm end piece | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA machine-learning prediction of sperm end piece. Reason: Electronic prediction contradicted by direct immunofluorescence: the human sperm ODA beta heavy chain is DNAH17, not DNAH9. Supporting Evidence: PMID:31178125 We show that DNAH17 and DNAH8, but not DNAH5, DNAH9, or DNAH11, colocalize with Ξ±-tubulin along the sperm axoneme, whereas the reverse picture is observed in respiratory cilia |
| GO:0097729 9+2 motile cilium | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT annotation placing dynein heavy chains in 9+2 motile cilia. Reason: Consistent with immunofluorescence of DNAH9 in the axonemes of 9+2 respiratory cilia. Supporting Evidence: PMID:18950741 Respiratory cilia contain at least two distinct ODA types: type 1, DNAH9 negative and DNAH5 positive (proximal ciliary axoneme); and type 2, DNAH9 and DNAH5 positive (distal ciliary axoneme). |
| GO:0097729 9+2 motile cilium | IDA PMID:26909801 DNAH11 Localization in the Proximal Region of Respiratory Ci... | ACCEPT | Summary: DNAH9 detected in human respiratory cilia, distally, opposite to the proximal DNAH11. Reason: Correct. The cached abstract of PMID:26909801 does not mention DNAH9, but the curator had the full text, which immunostains DNAH9 in respiratory cilia opposite the proximal DNAH11; the localization is independently established by PMID:30471717 and by the UniProt record, which are quoted here. Supporting Evidence: PMID:30471717 DNAH9 and its partner heavy chain DNAH5 localize to type 2 ODAs of the distal cilium file:human/DNAH9/DNAH9-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme |
| GO:0097729 9+2 motile cilium | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer of 9+2 motile cilium. Reason: Correct. Supporting Evidence: PMID:18950741 Respiratory cilia contain at least two distinct ODA types: type 1, DNAH9 negative and DNAH5 positive (proximal ciliary axoneme); and type 2, DNAH9 and DNAH5 positive (distal ciliary axoneme). |
| GO:0120135 distal portion of axoneme | IDA PMID:26909801 DNAH11 Localization in the Proximal Region of Respiratory Ci... | ACCEPT | Summary: DNAH9 occupies the distal ciliary axoneme, while DNAH11 occupies the proximal region. Reason: Core location: defines the distal type 2 ODA. The cached abstract of PMID:26909801 does not mention DNAH9; the curator had the full text, and the distal localization is independently established by PMID:30471717 and the UniProt record, quoted here. Supporting Evidence: PMID:30471717 DNAH9 and its partner heavy chain DNAH5 localize to type 2 ODAs of the distal cilium file:human/DNAH9/DNAH9-uniprot.txt Note=Found in the distal portion of ciliary axoneme. |
| GO:0120135 distal portion of axoneme | IDA PMID:30471717 Mutations in Outer Dynein Arm Heavy Chain DNAH9 Cause Motile... | ACCEPT | Summary: DNAH9 localizes to type 2 ODAs of the distal cilium. Reason: Core location. Supporting Evidence: PMID:30471717 DNAH9 and its partner heavy chain DNAH5 localize to type 2 ODAs of the distal cilium |
| GO:0120135 distal portion of axoneme | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfer of distal portion of axoneme. Reason: Agrees with the experimental data. Supporting Evidence: PMID:30471717 DNAH9 and its partner heavy chain DNAH5 localize to type 2 ODAs of the distal cilium |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Is DNAH9 present in human sperm? PMID:31178125 reports DNAH9 absent from the sperm axoneme, while HPA immunofluorescence and a DNAH3 study were curated as sperm end piece/sperm flagellum. Could the antibodies cross-react with DNAH17?
Q: Should GO have a molecular function term for binding the outer dynein arm docking complex, to replace the protein binding annotation for the DNAH9-ODAD1 interaction?
Q: Why do the outer-arm beta heavy chains (DNAH9, DNAH11, DNAH17) receive only the generic dynein complex IBA, while the gamma chain DNAH5 inherits outer dynein arm and outer dynein arm assembly from node PTN002472868? Could an equivalent beta-chain node carry these terms?
Experiment: Map the DNAH9-ODAD1 interface by crosslinking mass spectrometry or structure of the distal ODA-docking complex, and test docking-deficient DNAH9 mutants in airway cell rescue.
Type: structural biology and rescue
Experiment: Immunostain human sperm with several independent DNAH9 antibodies and DNAH9-null controls to settle whether DNAH9 is present in the sperm flagellum.
Type: immunofluorescence with genetic controls
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)