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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity is verified at the gene/protein level. The requested target is human MTMR9, myotubularin-related protein 9, an enzymatically inactive member of the myotubularin phosphoinositide-phosphatase family. The literature consistently uses MTMR9 for this human protein and identifies it as a binding partner of MTMR6, MTMR7, and MTMR8; no conflicting same-symbol protein was encountered. The supplied UniProt accession Q96QG7, organism Homo sapiens, and domains—PH-GRAM, myotubularin-like phosphatase, protein-tyrosine-phosphatase-like, and C-terminal interaction/coiled-coil architecture—are concordant with the literature. The accession and aliases C8orf9/MTMR8 were not independently printed in the retrieved papers, so those identifier mappings remain grounded in the supplied UniProt record rather than re-established experimentally here.
MTMR9 is best annotated as a regulatory pseudophosphatase/adaptor, not as an enzyme with its own reaction. Its altered protein-tyrosine-phosphatase signature lacks the essential catalytic cysteine of the C(X)5R motif. It therefore does not directly hydrolyze phosphatidylinositol 3-phosphate [PI3P] or phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]. Instead, heteromerization with active MTMR6/7/8 controls their stability, membrane association, catalytic output, substrate preference, and compartmental targeting. The best-supported cellular functions are regulation of phosphoinositide pools during autophagy, apoptosis/cell survival, macropinocytosis, and ER-to-Golgi secretion. (knop2024nonenzymaticrolesof pages 14-16, zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2009mtmr9increasesmtmr6 pages 1-1)
The human myotubularin family contains catalytically active and inactive members. Active family members remove the D3 phosphate from PI3P and PI(3,5)P2; inactive members lack the catalytic cysteine and commonly regulate active partners through heteromerization. MTMR9 belongs to the inactive class and interacts directly with active MTMR6, MTMR7, and MTMR8. (knop2024nonenzymaticrolesof pages 14-16, zou2012myotubularinrelatedprotein(mtmr) pages 1-1, wang2024recentadvancesof pages 1-2)
The supplied domain calls are functionally coherent:
Accordingly, database descriptions such as “inactive phosphatidylinositol 3-phosphatase 9” should be read as inactive homolog of PI 3-phosphatases, not as evidence that MTMR9 itself catalyzes a measurable reaction.
There is no supported intrinsic MTMR9 substrate or product. Sequence evidence—the disrupted catalytic C(X)5R motif—and biochemical classification identify it as a pseudophosphatase. Any annotation assigning direct PI3P or PI(3,5)P2 hydrolysis to MTMR9 alone would therefore be misleading. (knop2024nonenzymaticrolesof pages 14-16, zou2012myotubularinrelatedprotein(mtmr) pages 1-1)
Human MTMR9 forms an MTMR6–MTMR9 heteromer both in vitro and in cells. It increases MTMR6 phospholipid binding without changing the lipid-binding profile, raises catalytic activity, and stabilizes both subunits, probably by slowing degradation. Initial assays measured up to a sixfold increase in MTMR6 activity from MTMR9; phosphatidylserine liposomes independently produced up to 28-fold stimulation, and their combined effect reached 84-fold. (zou2009mtmr9increasesmtmr6 pages 1-1, zou2009mtmr9increasesmtmr6 pages 8-9)
Substrate-resolved radiolabeled-lipid assays clarified the complex’s preference. MTMR9 enhanced MTMR6 activity by more than 30-fold toward PI(3,5)P2, but only approximately twofold toward PI3P. In cells, coexpression increased PI5P—the product of PI(3,5)P2 D3-dephosphorylation—approximately threefold. Thus, the functional reaction attributable to the complex’s active MTMR6 subunit is:
PI(3,5)P2 + H₂O → PI5P + inorganic phosphate. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2012myotubularinrelatedprotein(mtmr) pages 1-3)
Functionally, MTMR6–MTMR9 coexpression reduced etoposide-induced apoptosis, whereas combined RNAi increased cell death more than MTMR6 depletion alone. This supports an anti-apoptotic, stress-response role, although the evidence comes mainly from cultured-cell perturbation rather than an in-vivo human phenotype. (zou2009mtmr9increasesmtmr6 pages 1-1, zou2009mtmr9increasesmtmr6 pages 8-9)
Human MTMR8 and MTMR9 reciprocally co-immunoprecipitated after expression in HeLa cells. Cycloheximide-chase experiments showed slower MTMR8 degradation in the presence of MTMR9. Unlike the MTMR6 complex, MTMR8–MTMR9 preferentially acts on PI3P: MTMR9 increased MTMR8 activity fourfold toward PI3P but only 1.4-fold toward PI(3,5)P2. The relevant reaction, again catalyzed by MTMR8 rather than MTMR9, is:
PI3P + H₂O → phosphatidylinositol + inorganic phosphate. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2012myotubularinrelatedprotein(mtmr) pages 1-3)
Only MTMR8 plus MTMR9 significantly reduced the measured cellular PI3P pool under the reported conditions. Overexpression of both proteins increased p62, consistent with reduced autophagic degradation, while combined depletion reduced p62 in bafilomycin-treated cells. These findings support inhibition of autophagic flux through depletion of a functionally important PI3P pool. Measurements included 50 cells per coverslip and three coverslips per condition; MTMR8 RNAi reduced its transcript to 0.275 relative to control. (zou2012myotubularinrelatedprotein(mtmr) pages 1-3)
Mass spectrometry and biochemical interaction mapping established MTMR9 as an MTMR7 partner, with binding mediated predominantly by the coiled-coil region. MTMR9 increases MTMR7 phosphatase activity in vitro, but did not detectably alter MTMR7’s cytosolic-versus-membrane distribution in COS-7 cells. The available evidence is less developed than for MTMR6 and MTMR8. (knop2024nonenzymaticrolesof pages 14-16, mochizuki2003characterizationofmyotubularinrelated pages 4-5)
MTMR9 is a soluble intracellular protein with both diffuse cytosolic and membrane-associated vesicular pools. Human-cell imaging places it at the ER-to-Golgi intermediate compartment (ERGIC/IC), cis- and trans-Golgi structures, and dispersed cytoplasmic vesicles. It colocalizes with RAB1 and RAB2; brefeldin A sensitivity of the perinuclear pool supports Golgi association, whereas peripheral brefeldin-resistant vesicles are consistent with an intermediate-compartment pool. MTMR9 recruits MTMR6 and MTMR8 to these locations. (knop2024nonenzymaticrolesof pages 33-34, knop2024nonenzymaticrolesof pages 27-28, knop2024nonenzymaticrolesof pages 91-93, knop2024nonenzymaticrolesof pages 23-27)
MTMR9 loss fragmented the cis-Golgi and redistributed RAB1 and the actin-nucleation/trafficking factor WHAMM. Overexpression also dispersed RAB1-positive vesicles, indicating that secretory-pathway organization requires balanced MTMR9 dosage rather than monotonically increasing with expression. These data place its principal action on cytosolic faces of intracellular membranes, especially the early secretory pathway, rather than extracellularly or as a transmembrane component. (knop2024nonenzymaticrolesof pages 27-28, knop2024nonenzymaticrolesof pages 34-36, knop2024nonenzymaticrolesof pages 93-95)
The unifying mechanism is spatial regulation of PI3P and PI(3,5)P2 turnover through active MTMR partners. These low-abundance signaling lipids define membrane identity and regulate recruitment of trafficking and autophagy machinery. MTMR9 changes partner activity, stability, and localization, thereby controlling selected lipid pools rather than globally dephosphorylating all cellular PI3P or PI(3,5)P2. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2009mtmr9increasesmtmr6 pages 1-1, zou2012myotubularinrelatedprotein(mtmr) pages 1-3)
The strongest direct model is that MTMR8–MTMR9 reduces PI3P needed for autophagosome formation/maturation, thereby suppressing autophagic flux. Overexpression increased p62; combined depletion produced a reciprocal effect. Later knockout work reported increased basal autophagy, broadly consistent with loss of a negative regulator, although MTMR9-only RNAi did not always reproduce the phenotype. This discrepancy may reflect incomplete depletion, adaptation after knockout, cell-line differences, or compensation among MTMR partners. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, knop2024nonenzymaticrolesof pages 34-36, knop2024nonenzymaticrolesof pages 93-95, zou2012myotubularinrelatedprotein(mtmr) pages 1-3)
A 2020 human-cell study localized MTMR9 to ERGIC/Golgi membranes and demonstrated effects on secretory cargo. In a temperature-sensitive VSVG assay, only approximately 30% of MTMR9-overexpressing cells showed cargo reaching the Golgi at the scored time, although VSVG ultimately reached the plasma membrane, indicating delay rather than complete blockade. Super-resolution imaging detected VSVG in MTMR9-positive vesicles. (knop2024nonenzymaticrolesof pages 33-34)
In HEK293T producer/STF reporter cocultures, MTMR9 overexpression reduced paracrine WNT3A reporter activity approximately fourfold. Conditioned medium from control and MTMR9-overexpressing cultures retained similar reporter activity, suggesting preferential impairment of a cell-surface-associated WNT3A pool rather than all released ligand. RUSH-WNT3A experiments scored more than 100 cells per condition and found delayed ER-to-Golgi progression after MTMR9 loss. These results support a cargo-trafficking/secretion role upstream of Wnt-receptor signal transduction, not direct action by MTMR9 in recipient-cell β-catenin signaling. (knop2024nonenzymaticrolesof pages 33-34, knop2024nonenzymaticrolesof pages 34-36)
Evolutionary evidence from C. elegans links MTM-6/MTM-9 to recycling of the Wnt cargo receptor MIG-14/Wls, but this should be regarded as supportive conservation evidence, not direct proof of the identical mechanism in humans. (knop2024nonenzymaticrolesof pages 23-27)
In EGF-stimulated A431 cells, siRNA against MTMR9 or MTMR6 significantly reduced dextran uptake, while transferrin uptake through clathrin-mediated endocytosis was unaffected. This argues for selective participation in macropinocytosis rather than a general block of endocytosis. Exact effect sizes and replication statistics were unavailable in the retrieved passage, so the precise step and lipid pool remain uncertain. (knop2024nonenzymaticrolesof pages 14-16)
MTMR6–MTMR9 promotes resistance to etoposide-induced apoptosis, plausibly through regulation of PI(3,5)P2/PI5P and stabilization/activation of MTMR6. This is experimentally supported but remains a cultured-cell pathway annotation rather than an established physiological or clinical indication. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2009mtmr9increasesmtmr6 pages 1-1, zou2009mtmr9increasesmtmr6 pages 8-9)
The central annotation and the distinction between mechanistic and association evidence are summarized below.
| Claim/domain | Strongest evidence | Experimental system | Quantitative result | Confidence/limitations |
|---|---|---|---|---|
| Catalytic inactivity / pseudophosphatase | Direct sequence-based inference: MTMR9 is an inactive myotubularin because its catalytic C(X)5R protein-tyrosine-phosphatase motif lacks the essential cysteine; it therefore regulates active MTMRs rather than directly dephosphorylating phosphoinositides. (knop2024nonenzymaticrolesof pages 14-16, zou2012myotubularinrelatedprotein(mtmr) pages 1-1) |
Human MTMR9 sequence/family comparison; biochemical studies of recombinant heteromeric complexes | No intrinsic MTMR9 phosphatase activity demonstrated; quantitative activity belongs to its active partners | High confidence. Strong sequence and family evidence, consistent with biochemical characterization; MTMR9 should not be annotated as directly catalyzing PI3P or PI(3,5)P2 hydrolysis. |
| MTMR6 activation, stability, and apoptosis | Direct mechanistic evidence: MTMR9 heteromerizes with MTMR6 in vitro and in cells, increases phospholipid binding and catalytic activity, and mutually stabilizes both proteins; coexpression protects against etoposide-induced apoptosis. (zou2009mtmr9increasesmtmr6 pages 1-1, zou2009mtmr9increasesmtmr6 pages 8-9) | Recombinant proteins and phosphatidylserine liposomes; transfected human cells; immunoprecipitation, RNAi, protein-level and apoptosis assays | MTMR9 increased MTMR6 activity up to 6-fold; phosphatidylserine liposomes stimulated it up to 28-fold; combined stimulation reached 84-fold. Later substrate-resolved assays found >30-fold activation toward PI(3,5)P2 versus about 2-fold toward PI3P. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2009mtmr9increasesmtmr6 pages 1-1) | High confidence for complex formation and enzymatic regulation; moderate for physiological anti-apoptotic role. Mostly overexpression/RNAi cell-culture evidence; no established human phenotype or in-vivo disease mechanism. |
| MTMR8 substrate specificity and autophagy | Direct mechanistic evidence: MTMR9 binds and stabilizes MTMR8, preferentially enhances its PI3P 3-phosphatase activity, lowers cellular PI3P, and suppresses autophagic flux; dual depletion produces the reciprocal phenotype. (zou2012myotubularinrelatedprotein(mtmr) pages 1-1, zou2012myotubularinrelatedprotein(mtmr) pages 1-3) | Recombinant radiolabeled-lipid assays; co-immunoprecipitation, cycloheximide chase, PI3P imaging, p62 and bafilomycin assays in HeLa cells | MTMR9 increased MTMR8 activity 4-fold toward PI3P but only 1.4-fold toward PI(3,5)P2. MTMR8 RNAi reduced its transcript to 0.275 relative to control; PI3P imaging counted 50 cells per coverslip on three coverslips per condition. (zou2012myotubularinrelatedprotein(mtmr) pages 1-3) | High confidence for altered substrate preference and stabilization; moderate for autophagy annotation. Results rely on cultured cells and perturbation of both proteins; MTMR9-only RNAi and knockout studies have not always yielded identical autophagy phenotypes. |
| ERGIC/Golgi/RAB1 localization and VSVG/WNT3A trafficking | Direct cell-biological evidence: MTMR9 localizes to ER–Golgi intermediate-compartment and Golgi membranes, recruits MTMR6/MTMR8, colocalizes with RAB1/RAB2, and is required at balanced levels for Golgi integrity and early secretory trafficking. (knop2024nonenzymaticrolesof pages 33-34, knop2024nonenzymaticrolesof pages 27-28, knop2024nonenzymaticrolesof pages 34-36) | Human RPE-1, HeLa, HEK293T and STF reporter cells; tagged proteins, CRISPR knockout, brefeldin A, ts045-VSVG and RUSH-WNT3A trafficking, reporter and conditioned-medium assays | After temperature shift, only ~30% of MTMR9-overexpressing cells showed VSVG reaching the Golgi. MTMR9 reduced paracrine WNT3A reporter activity about 4-fold, while released conditioned-medium activity was similar, implicating the cell-surface-associated WNT3A pool. More than 100 cells per condition were scored in a WNT3A trafficking assay. (knop2024nonenzymaticrolesof pages 33-34, knop2024nonenzymaticrolesof pages 34-36) | Moderate-to-high confidence for cultured-cell trafficking function. Both loss and overexpression perturb trafficking, implying dosage sensitivity. Tagged-protein localization and cell-line assays may not reproduce endogenous behavior in tissues; no in-vivo human validation. |
| Macropinocytosis | Direct functional screening evidence: MTMR9 or MTMR6 knockdown reduced EGF-stimulated dextran uptake, whereas clathrin-mediated transferrin uptake was unaffected, suggesting selective participation in macropinocytosis. (knop2024nonenzymaticrolesof pages 14-16) | Serum-starved human A431 cells stimulated with EGF; siRNA knockdown; dextran and transferrin internalization assays | Reported as a statistically significant reduction in dextran uptake, but no effect size, replicate number, or exact p-value was available in the retrieved evidence | Moderate-to-low confidence. Selectivity control is useful, but quantitative details and independent replication are limited; the precise MTMR9-dependent lipid pool or trafficking step remains unresolved. |
| 2024 methotrexate pharmacogenomics | Human association: Germline MTMR9 missense candidate rs200687372 (A>G; predicted Ile/Val) was associated with delayed high-dose methotrexate clearance in Korean children with acute lymphoblastic leukemia. (choi2024novelgenomicvariants pages 1-2, choi2024novelgenomicvariants pages 5-7) | Whole-exome sequencing of 51 patients and longitudinal analysis of 341 infusions; 25 delayed-clearance cases and 26 controls | Two heterozygotes occurred among cases and none among controls; longitudinal Bonferroni-corrected p<0.0001. Binary Fisher test was nonsignificant (p=0.24) despite reported RR 2.13, 95% CI 1.58–2.87. Overall, 80/341 infusions (23.5%) had delayed clearance. (choi2024novelgenomicvariants pages 5-7) | Low confidence; association only. Very rare variant, small ancestry-specific cohort, inconsistent significance across analyses, no functional experiment, and no external replication for MTMR9—the replicated signal was PKD1L2, not MTMR9. It is not evidence that MTMR9 controls methotrexate transport directly. |
| 2024 breast-cancer association | Exploratory association: Transcriptomic/machine-learning analysis linked higher MTMR9 expression with a lipid-metabolism prognostic signature and poorer breast-cancer outcomes; docking nominated niclosamide as a possible MTMR9-binding compound. (chen2024integrationoftranscriptomics pages 21-22, chen2024integrationoftranscriptomics pages 19-21) | Public breast-cancer transcriptomes, machine-learning survival model, molecular docking, and preliminary breast-cancer cell experiments | Retrieved evidence did not provide an MTMR9-specific hazard ratio, confidence interval, cohort size, exact p-value, binding affinity, or validated target-engagement measurement | Low confidence; hypothesis-generating association. No MTMR9 knockout/overexpression study established effects on tumor growth, migration, apoptosis, or drug response; docking is not proof of binding, mechanism, or therapeutic action. |
Table: Evidence hierarchy separating direct biochemical and cell-biological findings for human MTMR9/Q96QG7 from preliminary clinical associations. Quantitative results and major experimental limitations are shown to support cautious functional annotation.
Recent literature has not replaced the core biochemical model established in 2009–2012. Rather, it extends MTMR9 toward trafficking and exploratory disease associations.
A 2024 synthesis of MTMR9’s non-enzymatic biology emphasized its vesicular, Golgi, and RAB1-associated localization and proposed that MTMR9 regulates active phosphatases and trafficking machinery as a scaffold/pseudophosphatase. Because this source is a thesis rather than a peer-reviewed primary article, its original observations should be weighted below the underlying 2020 Experimental Cell Research study. (knop2024nonenzymaticrolesof pages 91-93, knop2024nonenzymaticrolesof pages 33-34, knop2024nonenzymaticrolesof pages 23-27)
A peer-reviewed cardiovascular review published March 2024 summarized older human associations between the intronic variant rs2293855 and BMI, HbA1c, insulin secretion/sensitivity, prediabetes, and metabolic syndrome. The review did not supply cohort sizes or effect estimates in the retrieved pages and acknowledged that these associations do not establish a direct molecular mechanism. Proposed links to obesity, hypertension, or cardiovascular disease therefore remain hypothesis-generating. URL: https://doi.org/10.3389/fcvm.2024.1364604. (wang2024recentadvancesof pages 4-5, wang2024recentadvancesof pages 3-4, wang2024recentadvancesof pages 9-9)
A pharmacogenomic study published 14 November 2024 performed germline whole-exome sequencing in 51 Korean children with acute lymphoblastic leukemia, covering 341 high-dose methotrexate infusions. MTMR9 rs200687372 (A>G; predicted Ile/Val) occurred in two of 25 delayed-clearance cases and none of 26 controls. It passed the longitudinal screen with Bonferroni-corrected p<0.0001, but its binary Fisher test was nonsignificant (p=0.24); the reported relative risk was 2.13, 95% CI 1.58–2.87. Overall, 80/341 infusions (23.5%) met delayed-clearance criteria. Crucially, MTMR9 was not externally replicated—the replicated locus was PKD1L2—so rs200687372 is a rare candidate association, not an actionable pharmacogenetic marker or evidence that MTMR9 transports methotrexate. URL: https://doi.org/10.3389/fphar.2024.1480657. (choi2024novelgenomicvariants pages 1-2, choi2024novelgenomicvariants pages 5-7)
A breast-cancer transcriptomic/machine-learning study published October 2024 associated elevated MTMR9 expression with a lipid-metabolism signature and worse prognosis, and molecular docking nominated niclosamide as a possible MTMR9-binding compound. The retrieved evidence provided no MTMR9-specific hazard ratio, confidence interval, exact p-value, target-engagement measurement, or causal perturbation. The authors explicitly called for knockout/overexpression experiments and in-vivo validation. Consequently, this is biomarker-generation and virtual-screening evidence, not proof that MTMR9 drives breast cancer or is a niclosamide target. URL: https://doi.org/10.3389/fimmu.2024.1470167. (chen2024integrationoftranscriptomics pages 21-22, chen2024integrationoftranscriptomics pages 19-21)
Open Targets lists MTMR9 associations with lysosomal-storage, Alzheimer, Parkinson, multiple-sclerosis, and broader neurodegenerative phenotypes, largely from CRISPR-based cellular screens. Such aggregated scores are useful for prioritization but do not establish Mendelian causality, clinical validity, or a disease-specific MTMR9 mechanism. (OpenTargets Search: -MTMR9)
There is currently no established MTMR9-specific diagnostic test, approved drug, targeted therapy, or clinically validated biomarker supported by the retrieved evidence. The most realistic present applications are research uses:
The most defensible concise functional annotation is:
MTMR9 is a catalytically inactive myotubularin-family pseudophosphatase that forms regulatory complexes with active MTMR6, MTMR7, and MTMR8. It promotes partner stability and can alter membrane recruitment, catalytic output, and preference for PI(3,5)P2 versus PI3P. Through these complexes it regulates compartment-specific phosphoinositide pools involved in autophagy, apoptosis, macropinocytosis, and ER-to-Golgi/Golgi trafficking, including WNT3A secretion.
Confidence is high for catalytic inactivity, heteromerization, partner activation/stabilization, and differential lipid-substrate regulation; moderate for specific roles in autophagy, apoptosis, and early secretion because evidence is primarily from cultured cells; and low for current disease causality or clinical utility. The major unresolved questions are the endogenous stoichiometry and structure of each complex, tissue-specific partners, precise lipid pools at ERGIC/Golgi membranes, and whether recent human genetic/expression associations are causal.
References
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(zou2009mtmr9increasesmtmr6 pages 8-9): Jun Zou, Shao-Chun Chang, Jasna Marjanovic, and Philip W. Majerus. Mtmr9 increases mtmr6 enzyme activity, stability, and role in apoptosis*. Journal of Biological Chemistry, 284:2064-2071, Jan 2009. URL: https://doi.org/10.1074/jbc.m804292200, doi:10.1074/jbc.m804292200. This article has 69 citations and is from a domain leading peer-reviewed journal.
(zou2012myotubularinrelatedprotein(mtmr) pages 1-3): Jun Zou, Chunfen Zhang, Jasna Marjanovic, Marina V. Kisseleva, Philip W. Majerus, and Monita P. Wilson. Myotubularin-related protein (mtmr) 9 determines the enzymatic activity, substrate specificity, and role in autophagy of mtmr8. Proceedings of the National Academy of Sciences, 109:9539-9544, May 2012. URL: https://doi.org/10.1073/pnas.1207021109, doi:10.1073/pnas.1207021109. This article has 79 citations and is from a highest quality peer-reviewed journal.
(knop2024nonenzymaticrolesof pages 33-34): F Knop. Non-enzymatic roles of kinases and phosphatases-the case of mtmr9 and aak1. Unknown journal, 2024.
(knop2024nonenzymaticrolesof pages 27-28): F Knop. Non-enzymatic roles of kinases and phosphatases-the case of mtmr9 and aak1. Unknown journal, 2024.
(knop2024nonenzymaticrolesof pages 91-93): F Knop. Non-enzymatic roles of kinases and phosphatases-the case of mtmr9 and aak1. Unknown journal, 2024.
(knop2024nonenzymaticrolesof pages 23-27): F Knop. Non-enzymatic roles of kinases and phosphatases-the case of mtmr9 and aak1. Unknown journal, 2024.
(knop2024nonenzymaticrolesof pages 34-36): F Knop. Non-enzymatic roles of kinases and phosphatases-the case of mtmr9 and aak1. Unknown journal, 2024.
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(choi2024novelgenomicvariants pages 1-2): Jung Yoon Choi, Hoshik Kwon, Hyery Kim, Kyung Taek Hong, Youngeun Ma, Kyung-Nam Koh, Sunmin Yun, Keon Hee Yoo, Sang Hoon Song, Ho Joon Im, Ju Han Kim, and Hyoung Jin Kang. Novel genomic variants influencing methotrexate delayed clearance in pediatric patients with acute lymphoblastic leukemia. Frontiers in Pharmacology, Nov 2024. URL: https://doi.org/10.3389/fphar.2024.1480657, doi:10.3389/fphar.2024.1480657. This article has 4 citations.
(choi2024novelgenomicvariants pages 5-7): Jung Yoon Choi, Hoshik Kwon, Hyery Kim, Kyung Taek Hong, Youngeun Ma, Kyung-Nam Koh, Sunmin Yun, Keon Hee Yoo, Sang Hoon Song, Ho Joon Im, Ju Han Kim, and Hyoung Jin Kang. Novel genomic variants influencing methotrexate delayed clearance in pediatric patients with acute lymphoblastic leukemia. Frontiers in Pharmacology, Nov 2024. URL: https://doi.org/10.3389/fphar.2024.1480657, doi:10.3389/fphar.2024.1480657. This article has 4 citations.
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(chen2024integrationoftranscriptomics pages 19-21): Xiaohan Chen, Jinfeng Yi, Lili Xie, Tong Liu, Baogang Liu, and Meisi Yan. Integration of transcriptomics and machine learning for insights into breast cancer: exploring lipid metabolism and immune interactions. Frontiers in Immunology, Oct 2024. URL: https://doi.org/10.3389/fimmu.2024.1470167, doi:10.3389/fimmu.2024.1470167. This article has 6 citations and is from a peer-reviewed journal.
(wang2024recentadvancesof pages 4-5): Jia Wang, Wei Guo, Qiang Wang, Yongjian Yang, and Xiongshan Sun. Recent advances of myotubularin-related (mtmr) protein family in cardiovascular diseases. Frontiers in Cardiovascular Medicine, Mar 2024. URL: https://doi.org/10.3389/fcvm.2024.1364604, doi:10.3389/fcvm.2024.1364604. This article has 16 citations and is from a peer-reviewed journal.
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(wang2024recentadvancesof pages 9-9): Jia Wang, Wei Guo, Qiang Wang, Yongjian Yang, and Xiongshan Sun. Recent advances of myotubularin-related (mtmr) protein family in cardiovascular diseases. Frontiers in Cardiovascular Medicine, Mar 2024. URL: https://doi.org/10.3389/fcvm.2024.1364604, doi:10.3389/fcvm.2024.1364604. This article has 16 citations and is from a peer-reviewed journal.
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