The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The supplied record is internally consistent with Rattus norvegicus Ptk7, the rat ortholog of vertebrate protein tyrosine kinase 7, also called PTK7 or CCK4. The protein description, kinase-superfamily assignment, and Ig-like domains match the established PTK7 receptor architecture. No conflicting same-symbol rat protein was identified. However, direct experimental literature on the specific rat accession A0A8I6ALM9 is limited; most mechanistic annotation must therefore be transferred cautiously from conserved human, mouse, Xenopus, zebrafish, and cultured mammalian-cell orthologs.
The best-supported primary function is not enzymatic catalysis. PTK7 is a single-pass cell-surface receptor pseudokinase that acts as a co-receptor and molecular scaffold, organizing Wnt/planar-cell-polarity and other receptor complexes. Its extracellular Ig-like region supports cell-surface interactions, while its intracellular pseudokinase domain recruits signaling proteins such as Dishevelled-associated adaptors, β-catenin, and Src. These complexes regulate polarized migration, cell adhesion, actomyosin organization, convergent extension, and tissue morphogenesis. Because PTK7 neither binds ATP productively nor catalyzes phosphotransfer, it has no kinase reaction, enzymatic substrate, or substrate specificity that should be assigned to it (dessaux2024recentinsightsinto pages 1-2, dessaux2024recentinsightsinto pages 2-4, sheetz2021structuralinsightsinto pages 3-4).
The target is Ptk7 in rat, not another similarly named kinase. The UniProt description “inactive tyrosine-protein kinase 7,” aliases “protein-tyrosine kinase 7,” “pseudo tyrosine kinase receptor 7,” and “tyrosine-protein kinase-like 7,” and the gene links to rat Ensembl/RGD all agree with the vertebrate PTK7/CCK4 literature. Established PTK7 consists of seven extracellular immunoglobulin-like domains, one transmembrane segment, and a cytoplasmic kinase-homology domain. This matches the supplied Ig-like-domain and protein-kinase-family assignments (dessaux2024recentinsightsinto pages 4-5, jin2024ptk7anunderestimated pages 1-2, dessaux2024recentinsightsinto pages 2-4).
The accession nevertheless appears to be chiefly computationally annotated. No biochemical study specifically purifying or manipulating A0A8I6ALM9 was located. Consequently, identity and broad architecture are high-confidence rat annotations, whereas precise binding partners, cleavage positions, and pathway effects are principally orthology-based inferences. Human residue numbers quoted below should not be assumed to be identical in rat without sequence alignment.
| Annotation aspect | Best-supported conclusion | Principal evidence/species | Confidence for rat accession |
|---|---|---|---|
| Identity and architecture | A0A8I6ALM9 is consistent with rat Ptk7, the ortholog of vertebrate PTK7/CCK4: a single-pass receptor-like protein with seven extracellular Ig-like domains and an intracellular kinase-homology domain. | Supplied rat UniProt/Ensembl/RGD annotation; matching human and vertebrate PTK7 architecture and aliases (dessaux2024recentinsightsinto pages 4-5, jin2024ptk7anunderestimated pages 1-2, dessaux2024recentinsightsinto pages 2-4) | High for identity and broad architecture; accession-specific experimental characterization is limited. |
| Enzymatic activity | PTK7 is a pseudokinase, not an active tyrosine kinase: its altered catalytic motifs and sterically occluded ATP pocket prevent ATP/Mg²⁺ binding and phosphotransfer. No catalytic reaction or substrate specificity should be assigned. | Human PTK7-domain crystallography at 1.95 Å, biophysical ATP-binding tests, and lack of autophosphorylation; ATP pocket obstructed by Y877 and L949 in human numbering (dessaux2024recentinsightsinto pages 2-4, andreeva2014ptk7srcsignalingat pages 4-6, sheetz2021structuralinsightsinto pages 3-4) | High by conserved orthology; not directly demonstrated for purified A0A8I6ALM9. |
| Primary molecular function | Functions principally as a cell-surface co-receptor and signaling scaffold, assembling Wnt receptors, adaptors, and active kinases rather than catalyzing phosphorylation. | Human biochemical and structural work; vertebrate developmental models (dessaux2024recentinsightsinto pages 4-5, dessaux2024recentinsightsinto pages 5-6, dessaux2024recentinsightsinto pages 2-4) | High by orthology. |
| Localization | Full-length PTK7 is predominantly at the plasma membrane, with its Ig ectodomain extracellular and pseudokinase domain cytoplasmic; epithelial PTK7 can concentrate at cell–cell contacts. | Human/cancer-cell membrane studies; endogenous PTK7 colocalization with E-cadherin in canine MDCK cells; cytoplasmic domain required for junctional targeting (jin2024ptk7anunderestimated pages 1-2, andreeva2014ptk7srcsignalingat pages 4-6, andreeva2014ptk7srcsignalingat pages 1-2) | Moderate–high by orthology; precise rat tissue and isoform localization remains unverified. |
| Wnt/PCP partners and outputs | Cooperates with FZD7, ROR2, WNT5A, Dishevelled, RACK1, and PKCδ1 to organize β-catenin-independent Wnt/planar-cell-polarity signaling, including JNK, Rho-family GTPases, ROCK, actomyosin remodeling, adhesion, polarized migration, and convergent extension. | Xenopus, mouse, zebrafish, and cultured-cell studies summarized in recent reviews (grund2019ptk7signalingcomplexes pages 25-28, dessaux2024recentinsightsinto pages 4-5, dessaux2024recentinsightsinto pages 5-6) | High for conserved vertebrate function; moderate for exact rat complexes. |
| Canonical Wnt context dependence | PTK7 can bind β-catenin and interact with LRP6/Wnt receptor complexes, but may promote or inhibit Wnt/β-catenin signaling depending on ligand, co-receptor, developmental stage, and disease context. It should not be annotated as an unconditional canonical-Wnt activator or inhibitor. | Human colorectal-cancer cells and Xenopus embryos; conflicting vertebrate results synthesized in 2024 (dessaux2024recentinsightsinto pages 4-5, dessaux2024recentinsightsinto pages 5-6, dessaux2024recentinsightsinto pages 8-10) | Moderate by orthology because directionality is context dependent. |
| Src/ROCK junctional signaling | The cytoplasmic pseudokinase domain binds Src directly and can be phosphorylated by Src; PTK7 promotes active Src and ROCK2 localization at epithelial contacts, thereby spatially organizing myosin-II contractility and planar polarity. | Canine MDCK knockdown/rescue and biochemistry; mouse auditory epithelium in vivo. Ptk7 knockdown reduced ROCK1/2 abundance by about 30% while increasing total ROCK activity (andreeva2014ptk7srcsignalingat pages 4-6, andreeva2014ptk7srcsignalingat pages 1-2) | Moderate–high by mammalian orthology; no direct rat assay located. |
| VEGFR signaling | PTK7 can heteromerize with VEGFR1/FLT1 and VEGFR2/KDR, enhance VEGF-receptor phosphorylation or oligomerization, and support AKT activation, endothelial migration, and angiogenesis. | Human endothelial/cancer-cell studies and blocking-antibody experiments summarized in 2024 (dessaux2024recentinsightsinto pages 4-5, dessaux2024recentinsightsinto pages 5-6) | Moderate by orthology; likely context- and cell-type-dependent. |
| Proteolytic cleavage and fragment localization | MT1-MMP cleaves extracellular PTK7 near L622, releasing soluble PTK7; ADAM17 cleavage near Q689 and γ-secretase cleavage near G721 can release an intracellular fragment that is degraded or enters the nucleus. Soluble and nuclear fragments may signal differently from the intact receptor. | Human fibrosarcoma and colorectal-cancer cells; comparative developmental studies (jin2024ptk7anunderestimated pages 1-2, golubkov2014proteintyrosinepseudokinase7 pages 10-10, dessaux2024recentinsightsinto pages 5-6) | Moderate by orthology; cleavage residues are human numbering and require mapping to the rat sequence. |
| Developmental roles | Conserved PTK7 signaling regulates convergent extension, neural-tube closure, neural-crest migration, auditory planar polarity, axial/spinal morphology, and aspects of heart and lung morphogenesis. | Loss-of-function studies in mouse, Xenopus, zebrafish, and other vertebrates; human variant associations (grund2019ptk7signalingcomplexes pages 25-28, dessaux2024recentinsightsinto pages 4-5, tan2024thewntcoreceptor pages 16-17, andreeva2014ptk7srcsignalingat pages 1-2) | Moderate–high for rat biological inference, but not accession-specific direct evidence. |
| Cancer targeting and applications | Cell-surface PTK7 is being exploited for ADCs, CAR-T cells, aptamers, imaging, and experimental PTK7–β-catenin inhibitors. Cofetuzumab pelidotin produced a 19.6% objective response rate in 56 patients with recurrent PTK7-positive NSCLC and 30% in the non-squamous, EGFR-wild-type subgroup, but development was terminated; no PTK7-targeted drug was approved as of October 2024. | Human trials and preclinical human-tumor/mouse-xenograft studies; 2024 reviews and aptamer studies (jin2024ptk7anunderestimated pages 15-17, jin2024ptk7anunderestimated pages 14-15, jin2024ptk7anunderestimated pages 13-14, dessaux2024recentinsightsinto pages 8-10) | High for human translational status; low relevance to normal rat function. Most such evidence does not characterize A0A8I6ALM9 directly. |
Table: Evidence-graded functional annotation of rat UniProt A0A8I6ALM9, distinguishing the limited accession-specific evidence from mechanistic findings in human and other vertebrate orthologs.
PTK7 resembles a receptor tyrosine kinase topologically but is a genuine class-1 pseudokinase. In the human domain, seven of forty kinase-consensus residues are unconventional. The glycine-rich loop is altered, the catalytic and DFG motifs are degenerate, and the canonical DFG sequence is replaced by ALG. The ATP pocket is additionally obstructed by Y877 in the β5/αD hinge and L949 in the ALG motif. The activation loop resembles the autoinhibited insulin-receptor kinase conformation, although the αC helix has an unusual active-like position (dessaux2024recentinsightsinto pages 2-4, andreeva2014ptk7srcsignalingat pages 1-2, sheetz2021structuralinsightsinto pages 3-4).
The strongest evidence is structural and biophysical. The human PTK7 pseudokinase crystal structure was determined at 1.95 Å, and purified PTK7 showed no significant stability change after addition of 5 mM Mg²⁺–ATP, consistent with failure to bind nucleotide. In biochemical experiments, the isolated PTK7 domain did not autophosphorylate, although active Src could phosphorylate it (andreeva2014ptk7srcsignalingat pages 4-6, sheetz2021structuralinsightsinto pages 3-4). Thus:
This distinction is central: phosphorylation detected on PTK7 can be generated by another kinase, such as Src, and must not be interpreted as PTK7 autophosphorylation.
Full-length PTK7 is predominantly a plasma-membrane protein, oriented with seven Ig-like domains outside the cell and the pseudokinase domain in the cytoplasm. It assembles ligand–receptor–adaptor complexes and spatially constrains active enzymes and cytoskeletal regulators. This explains how an inactive kinase-domain protein can transmit extracellular or cell-contact information (dessaux2024recentinsightsinto pages 4-5, jin2024ptk7anunderestimated pages 1-2, dessaux2024recentinsightsinto pages 2-4).
The most reproducible pathway assignment is β-catenin-independent Wnt/planar cell polarity (PCP) signaling. PTK7 participates in complexes containing WNT5A, ROR2, Frizzled-7, Dishevelled, RACK1, and PKCδ1. Its intracellular domain helps recruit Dishevelled to the plasma membrane through RACK1/PKCδ1, thereby linking receptor organization to JNK, Rho-family GTPases, ROCK, myosin-II, cytoskeletal remodeling, adhesion, and directional migration (grund2019ptk7signalingcomplexes pages 25-28, dessaux2024recentinsightsinto pages 4-5, dessaux2024recentinsightsinto pages 5-6).
The resulting biological role is spatial rather than simply “on/off” pathway activation: PTK7 helps cells orient contractile forces and protrusions relative to neighboring cells and tissue axes. Vertebrate loss-of-function studies consequently implicate Ptk7 in convergent extension, neural-tube closure, neural-crest migration, auditory epithelial polarity, axial/spinal morphology, and heart and lung morphogenesis (grund2019ptk7signalingcomplexes pages 25-28, tan2024thewntcoreceptor pages 16-17, andreeva2014ptk7srcsignalingat pages 1-2).
PTK7 also binds β-catenin and can interact with LRP6-containing receptor complexes, but its effect on canonical Wnt signaling is context dependent. In some colorectal-cancer systems, PTK7–β-catenin association supports Wnt target-gene expression. In Xenopus, interaction through the transmembrane region with LRP6 was reported to promote Wnt/β-catenin signaling while repressing PCP signaling. Other contexts show inhibition of canonical signaling. The direction likely depends on the available Wnt ligands, Frizzled/LRP/ROR co-receptors, cell state, and receptor processing; PTK7 should therefore not be annotated as an unconditional canonical-Wnt activator or inhibitor (dessaux2024recentinsightsinto pages 4-5, dessaux2024recentinsightsinto pages 5-6, dessaux2024recentinsightsinto pages 8-10).
In epithelial cells, PTK7 can concentrate at cell–cell junctions. Endogenous PTK7 colocalized with E-cadherin at contacts in MDCK epithelial monolayers. Full-length murine PTK7 rescued Ptk7-knockdown phenotypes and localized to contacts, whereas a cytoplasmic-domain deletion accumulated aberrantly at apical membranes. Thus, the cytoplasmic domain contributes both to junctional targeting and function (andreeva2014ptk7srcsignalingat pages 4-6, andreeva2014ptk7srcsignalingat pages 1-2).
At contacts, PTK7 directly binds the Src SH3-containing region through its pseudokinase domain. Src then phosphorylates PTK7, and phosphorylated PTK7 can engage Src's SH2 domain. Ptk7 knockdown reduced active Src at junctions, displaced ROCK2, weakened junctional contractility, and increased basal actomyosin. Although total ROCK1 and ROCK2 abundance fell by approximately 30%, overall ROCK activity increased, illustrating that PTK7 controls the spatial distribution, not merely the bulk quantity, of signaling activity (andreeva2014ptk7srcsignalingat pages 4-6).
Accordingly, the principal working locations are:
The latter two locations concern processed PTK7 species and should not be treated as the default localization of intact rat PTK7.
PTK7 can also modulate active receptor tyrosine kinases. In human endothelial systems it associates with FLT1/VEGFR1 and KDR/VEGFR2, promoting VEGF-receptor phosphorylation or oligomerization, AKT activity, migration, and angiogenesis. Anti-PTK7 antibodies can inhibit VEGF-induced angiogenesis by disrupting PTK7–KDR association (dessaux2024recentinsightsinto pages 5-6). PTK7 therefore behaves as a noncatalytic amplifier or organizer of an active kinase rather than phosphorylating VEGFR substrates itself.
Additional reported interactions include Plexin-family guidance receptors and, in cancer-specific settings, NDRG1 and AMIGO2. These are credible examples of PTK7's broader scaffold capacity but are less suitable as universal annotations for normal rat tissues because they are highly cell-state dependent (dessaux2024recentinsightsinto pages 10-11, dessaux2024recentinsightsinto pages 6-8).
PTK7 function is regulated by sequential proteolysis. In human numbering, MT1-MMP cleaves near L622 in the seventh Ig-like domain, releasing a soluble ectodomain. ADAM17 can cleave near Q689, close to the transmembrane region, and γ-secretase cleavage near G721 can release an intracellular fragment. The latter may undergo proteasomal degradation or enter the nucleus; in colorectal-cancer and fibrosarcoma cells, nuclear intracellular fragments promoted migration- and proliferation-associated programs (jin2024ptk7anunderestimated pages 1-2, golubkov2014proteintyrosinepseudokinase7 pages 10-10, dessaux2024recentinsightsinto pages 5-6).
Shedding is not merely receptor disposal. Soluble PTK7 released by senescent fibroblasts was reported to signal paracrinally through Wnt/Ca²⁺ and alter intestinal stem-cell differentiation. Comparative Drosophila work similarly supports non-cell-autonomous actions of soluble PTK7-family proteins (dessaux2024recentinsightsinto pages 5-6, dessaux2024recentinsightsinto pages 6-8). Nevertheless, direct demonstration of these exact cleavage events in rat A0A8I6ALM9 is lacking, and cleavage-site conservation should be verified experimentally.
The most defensible functional annotation for rat Ptk7 is:
A catalytically inactive, single-pass receptor-like scaffold that organizes Wnt/PCP and junctional cytoskeletal signaling to control cell polarity, adhesion, directional migration, and tissue morphogenesis.
Mechanistically informative biological processes include:
These processes are supported strongly across vertebrates, but most have not been directly tested with the named rat accession.
A May 2024 authoritative review emphasized that PTK7's inactive domain remains conformationally useful and pharmacologically targetable. In-cell NanoBRET assays reconstituted the PTK7–β-catenin interaction and identified small molecules that disrupt the complex, suppress Wnt signaling, and inhibit colorectal-cancer proliferation and anchorage-independent growth at micromolar potency. These remain early discovery compounds requiring optimization and patient-derived-model testing (dessaux2024recentinsightsinto pages 1-2, dessaux2024recentinsightsinto pages 5-6, dessaux2024recentinsightsinto pages 8-10).
Recent work has also shifted attention from PTK7 abundance alone to receptor state: full-length surface PTK7, soluble ectodomain, and nuclear intracellular fragments can have different or opposing effects. The 2024 expert analysis argues that the ratio of intact to cleaved PTK7 may be more informative than total expression and warns that MT1-MMP/ADAM17 shedding could permit escape from surface-directed ADC, CAR-T, or aptamer therapy (dessaux2024recentinsightsinto pages 8-8, dessaux2024recentinsightsinto pages 6-8).
Human cancer associations remain context dependent. A 2024 breast-cancer analysis included 1,136 tumors assessed for protein, METABRIC data from 1,980 cases, and TCGA data from 1,082 cases. PTK7 mRNA—but not overall protein expression—was associated with breast-cancer-specific survival in METABRIC; reported subgroup associations included ER-positive tumors (p=0.020), PgR-negative tumors (p=0.002), and HER2-negative tumors (p<0.001), while TCGA did not reproduce the survival association. This reinforces expert caution against treating PTK7 expression as a universal prognostic marker (lacey2024proteintyrosinekinase pages 9-11).
PTK7's accessible extracellular domains and frequent tumor-surface expression have made it a target for ADCs, CAR-T cells, aptamers, molecular imaging, and targeted drug delivery. Cofetuzumab pelidotin combines a humanized anti-PTK7 antibody with an auristatin payload through a cleavable valine–citrulline linker. Preclinical studies showed sustained regression in patient-derived models of triple-negative breast, ovarian, and non-small-cell lung cancer (dessaux2024recentinsightsinto pages 6-8).
In a Phase Ib study of 56 patients with recurrent PTK7-positive NSCLC, cofetuzumab pelidotin produced an objective response rate of 19.6%. The non-squamous, EGFR-wild-type subgroup had a 30% response rate and median progression-free survival of 5.5 months. Development was subsequently terminated after weak responses in other molecular/histological subgroups; no PTK7-targeted drug had received marketing approval as of October 2024 (jin2024ptk7anunderestimated pages 14-15, jin2024ptk7anunderestimated pages 13-14).
Other modalities remain mainly experimental. PTK7 CAR-T cells have shown antigen-specific cytotoxicity and tumor control in mouse xenografts. The 42-nucleotide DNA aptamer Sgc8c has been used for selective imaging and delivery of doxorubicin and other payloads to PTK7-positive cells. Small-molecule PTK7–β-catenin inhibitors, bispecific ADCs, and newer PTK7 ADCs are preclinical or in early clinical development (jin2024ptk7anunderestimated pages 15-17, dessaux2024recentinsightsinto pages 6-8, dessaux2024recentinsightsinto pages 8-8). These applications validate surface accessibility but do not themselves establish normal rat physiology.
For rat Ptk7/A0A8I6ALM9, the highest-confidence annotation is a plasma-membrane pseudokinase receptor/co-receptor and scaffold. It has no demonstrated catalytic reaction. Its extracellular Ig-like domains support receptor, ligand, and cell-surface interactions, while its intracellular kinase-like domain recruits signaling proteins and organizes active kinases. Its central conserved role is to spatially coordinate Wnt/PCP, Src–ROCK, and actomyosin signaling during polarized migration and morphogenesis.
The largest uncertainty is not protein identity but accession-specific validation: direct rat experiments, tissue-resolved localization, isoform usage, ligand affinities, and rat cleavage-site mapping remain sparse. Consequently, detailed molecular claims should be labeled as conserved vertebrate inference until A0A8I6ALM9 is directly tested. The most useful future experiments would be rat-sequence confirmation, surface-proteomics and junctional imaging, ATP-binding/autophosphorylation controls, interactome analysis under defined Wnt ligands, and mapping of endogenous rat proteolytic fragments.
References
(dessaux2024recentinsightsinto pages 1-2): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(dessaux2024recentinsightsinto pages 2-4): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(sheetz2021structuralinsightsinto pages 3-4): Joshua B. Sheetz, Sebastian Mathea, Hanna Karvonen, Ketan Malhotra, Deep Chatterjee, Wilhelmiina Niininen, Robert Perttilä, Franziska Preuss, Krishna Suresh, Steven E. Stayrook, Yuko Tsutsui, Ravi Radhakrishnan, Daniela Ungureanu, Stefan Knapp, and Mark A. Lemmon. Structural insights into pseudokinase domains of receptor tyrosine kinases. The FASEB Journal, 35:390-405.e7, May 2021. URL: https://doi.org/10.1096/fasebj.2021.35.s1.02446, doi:10.1096/fasebj.2021.35.s1.02446. This article has 108 citations.
(dessaux2024recentinsightsinto pages 4-5): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(jin2024ptk7anunderestimated pages 1-2): Zhipeng Jin, Tianyu Guo, Xue Zhang, Xin Wang, and Yefu Liu. Ptk7: an underestimated contributor to human cancer. Frontiers in Oncology, Oct 2024. URL: https://doi.org/10.3389/fonc.2024.1448695, doi:10.3389/fonc.2024.1448695. This article has 19 citations.
(andreeva2014ptk7srcsignalingat pages 4-6): Anna Andreeva, Jianyi Lee, Madhura Lohia, Xiaoji Wu, Ian G. Macara, and Xiaowei Lu. Ptk7-src signaling at epithelial cell contacts mediates spatial organization of actomyosin and planar cell polarity. Developmental cell, 29 1:20-33, Apr 2014. URL: https://doi.org/10.1016/j.devcel.2014.02.008, doi:10.1016/j.devcel.2014.02.008. This article has 68 citations and is from a highest quality peer-reviewed journal.
(dessaux2024recentinsightsinto pages 5-6): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(andreeva2014ptk7srcsignalingat pages 1-2): Anna Andreeva, Jianyi Lee, Madhura Lohia, Xiaoji Wu, Ian G. Macara, and Xiaowei Lu. Ptk7-src signaling at epithelial cell contacts mediates spatial organization of actomyosin and planar cell polarity. Developmental cell, 29 1:20-33, Apr 2014. URL: https://doi.org/10.1016/j.devcel.2014.02.008, doi:10.1016/j.devcel.2014.02.008. This article has 68 citations and is from a highest quality peer-reviewed journal.
(grund2019ptk7signalingcomplexes pages 25-28): A Grund. Ptk7 signaling complexes in neural crest cell migration. Unknown journal, 2019.
(dessaux2024recentinsightsinto pages 8-10): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(golubkov2014proteintyrosinepseudokinase7 pages 10-10): Vladislav S. Golubkov, Natalie L. Prigozhina, Yong Zhang, Konstantin Stoletov, John D. Lewis, Phillip E. Schwartz, Robert M. Hoffman, and Alex Y. Strongin. Protein-tyrosine pseudokinase 7 (ptk7) directs cancer cell motility and metastasis. Aug 2014. URL: https://doi.org/10.1074/jbc.m114.574459, doi:10.1074/jbc.m114.574459. This article has 81 citations and is from a domain leading peer-reviewed journal.
(tan2024thewntcoreceptor pages 16-17): Qian Hui Tan, Agimaa Otgonbaatar, Prameet Kaur, Angelica Faye Ga, Nathan P. Harmston, and Nicholas S. Tolwinski. The wnt co-receptor ptk7/otk and its homolog otk-2 in neurogenesis and patterning. Cells, 13:365, Feb 2024. URL: https://doi.org/10.3390/cells13050365, doi:10.3390/cells13050365. This article has 4 citations.
(jin2024ptk7anunderestimated pages 15-17): Zhipeng Jin, Tianyu Guo, Xue Zhang, Xin Wang, and Yefu Liu. Ptk7: an underestimated contributor to human cancer. Frontiers in Oncology, Oct 2024. URL: https://doi.org/10.3389/fonc.2024.1448695, doi:10.3389/fonc.2024.1448695. This article has 19 citations.
(jin2024ptk7anunderestimated pages 14-15): Zhipeng Jin, Tianyu Guo, Xue Zhang, Xin Wang, and Yefu Liu. Ptk7: an underestimated contributor to human cancer. Frontiers in Oncology, Oct 2024. URL: https://doi.org/10.3389/fonc.2024.1448695, doi:10.3389/fonc.2024.1448695. This article has 19 citations.
(jin2024ptk7anunderestimated pages 13-14): Zhipeng Jin, Tianyu Guo, Xue Zhang, Xin Wang, and Yefu Liu. Ptk7: an underestimated contributor to human cancer. Frontiers in Oncology, Oct 2024. URL: https://doi.org/10.3389/fonc.2024.1448695, doi:10.3389/fonc.2024.1448695. This article has 19 citations.
(sheetz2021structuralinsightsinto pages 7-8): Joshua B. Sheetz, Sebastian Mathea, Hanna Karvonen, Ketan Malhotra, Deep Chatterjee, Wilhelmiina Niininen, Robert Perttilä, Franziska Preuss, Krishna Suresh, Steven E. Stayrook, Yuko Tsutsui, Ravi Radhakrishnan, Daniela Ungureanu, Stefan Knapp, and Mark A. Lemmon. Structural insights into pseudokinase domains of receptor tyrosine kinases. The FASEB Journal, 35:390-405.e7, May 2021. URL: https://doi.org/10.1096/fasebj.2021.35.s1.02446, doi:10.1096/fasebj.2021.35.s1.02446. This article has 108 citations.
(dessaux2024recentinsightsinto pages 10-11): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(dessaux2024recentinsightsinto pages 6-8): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(dessaux2024recentinsightsinto pages 8-8): Charlotte Dessaux, Laetitia Ganier, Louis Guiraud, and Jean-Paul Borg. Recent insights into the therapeutic strategies targeting the pseudokinase ptk7 in cancer. Oncogene, 43:1973-1984, May 2024. URL: https://doi.org/10.1038/s41388-024-03060-x, doi:10.1038/s41388-024-03060-x. This article has 36 citations and is from a domain leading peer-reviewed journal.
(lacey2024proteintyrosinekinase pages 9-11): Kate Lacey, Megan R. Greener, Tangkam R. Marak, Emad A. Rakha, Andrew R. Green, Ian O. Ellis, Stewart G. Martin, and Sarah J. Storr. Protein tyrosine kinase 7 (ptk7) in breast cancer: a retrospective analysis of tumour expression and association with clinical outcome. Sep 2024. URL: https://doi.org/10.3390/cancers16183206, doi:10.3390/cancers16183206. This article has 3 citations.