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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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. The requested protein is human mitogen-activated protein kinase 8 (MAPK8), conventionally called c-Jun N-terminal kinase 1 (JNK1). It is not MAPK9/JNK2, MAPK10/JNK3, or a MAPK8-interacting scaffold such as MAPK8IP1. Independent literature consistently identifies MAPK8 as JNK1 and places it in the serine/threonine MAP-kinase family, matching the supplied UniProt accession P45983 and its CMGC protein-kinase/MAPK/JNK domain annotations. No gene-symbol or organism conflict was found. (koch2015inhibitorsofcjun pages 1-5, nadel2023jnkcascadeinducedapoptosis—a pages 2-4, nadel2023jnkcascadeinducedapoptosis—a pages 1-2)
Functionally, MAPK8 is an intracellular, ATP-dependent, proline-directed protein kinase. Its core reaction is:
ATP + protein–Ser/Thr–OH → ADP + protein–Ser/Thr–O-phosphate.
JNK1 preferentially phosphorylates serine or threonine followed immediately by proline, but physiological specificity also requires docking interactions and localization within signaling complexes. It is activated principally by dual phosphorylation of Thr183 and Tyr185 in its Thr-Pro-Tyr activation loop. Activated JNK1 phosphorylates transcription factors—notably c-Jun—and numerous cytoplasmic substrates, converting stress, cytokine, immune-receptor, and growth-factor inputs into context-dependent changes in gene expression, survival, apoptosis, metabolism, differentiation, and cytoskeletal behavior. (zeke2016jnksignalingregulation pages 10-10, koch2015inhibitorsofcjun pages 1-5, gehi2022intrinsicdisorderin pages 17-18)
The most important translational development retrieved from 2023–2024 is a 2024 preclinical study identifying MAPK8/JNK1 as a distal B-cell-receptor survival node in chronic lymphocytic leukemia (CLL), including BTK-inhibitor-resistant disease. However, no evidence retrieved establishes an approved MAPK8-selective therapeutic application; commonly used JNK inhibitors have substantial isoform or kinome-selectivity limitations. (saleem2024jnk1inhibitorstarget pages 2-3, saleem2024jnk1inhibitorstarget pages 8-9, saleem2024jnk1inhibitorstarget pages 4-5)
| Topic | Best-supported finding | Evidence type/specificity | Key quantitative detail | Source/date/URL |
|---|---|---|---|---|
| Identity | The supplied UniProt accession P45983 is human MAPK8, encoding JNK1; MAPK9/JNK2, MAPK10/JNK3, and MAPK8IP proteins are distinct targets. | UniProt identity supplied by user; literature independently maps MAPK8 to JNK1. MAPK8-specific. | Three human JNK genes are recognized; JNK1 has multiple approximately 46- and 54/55-kDa splice forms. | Koch et al., Jan. 2015, DOI (koch2015inhibitorsofcjun pages 1-5); Nadel et al., Aug. 2023, DOI (nadel2023jnkcascadeinducedapoptosis—a pages 2-4, nadel2023jnkcascadeinducedapoptosis—a pages 1-2) |
| Catalysis and phosphoacceptor specificity | JNK1 is an ATP-dependent serine/threonine MAP kinase that transfers phosphate to protein Ser/Thr residues, preferentially in S/T-P motifs; docking interactions are also required for physiological specificity. | Biochemical/review synthesis. Primarily pan-JNK, consistent with MAPK8’s kinase-family annotation. | More than 100 JNK substrates, including at least 30 transcription factors, have been reported, but this count is not JNK1-exclusive. | Zeke et al., Sep. 2016, DOI (zeke2016jnksignalingregulation pages 10-10); Gehi et al., Mar. 2022, DOI (gehi2022intrinsicdisorderin pages 17-18) |
| Activation mechanism | Full activity requires dual phosphorylation of the activation-loop Thr183-Pro-Tyr185 motif. MKK7 preferentially phosphorylates Thr183, whereas MKK4 preferentially phosphorylates Tyr185; the kinases can act synergistically. | Established cascade mechanism; mostly pan-JNK, with residue numbering applicable to JNK1. | Two activating phosphosites: Thr183 and Tyr185. | Koch et al., Jan. 2015, DOI (koch2015inhibitorsofcjun pages 1-5); Nadel et al., Aug. 2023, DOI (nadel2023jnkcascadeinducedapoptosis—a pages 2-4, nadel2023jnkcascadeinducedapoptosis—a pages 1-2) |
| Docking and substrates | Substrate selection combines S/T-P recognition with approximately 9–18-residue D-motifs binding JNK’s common-docking region and hydrophobic groove. Canonical substrates include c-Jun and ATF2; c-Jun phosphorylation at Ser63 and Ser73 underlies the “c-Jun N-terminal kinase” name. | Structural, biochemical, and review evidence; docking surface is nearly identical among JNK1–3, so largely pan-JNK, not isoform-selective. | D-motifs are approximately 9–18 residues; canonical c-Jun sites are Ser63 and Ser73. | Zeke et al., Sep. 2016, DOI (zeke2016jnksignalingregulation pages 10-10); Gehi et al., Mar. 2022, DOI (gehi2022intrinsicdisorderin pages 17-18) |
| Localization and trafficking | JNK signaling is organized in cytoplasmic scaffold complexes; after stress activation, JNK can enter the nucleus through importins Imp7, Imp9, and Imp3 and phosphorylate transcription factors. Cytoskeletal or organellar pools are context dependent. | Cell-biological/review evidence, mainly pan-JNK; it should not automatically be assigned exclusively to MAPK8. | Three reported nuclear-import mediators: Imp7, Imp9, and Imp3. | Nadel et al., Aug. 2023, DOI (nadel2023jnkcascadeinducedapoptosis—a pages 2-4); Gehi et al., Mar. 2022, DOI (gehi2022intrinsicdisorderin pages 17-18) |
| HCC research, 2023 | In HepG2 and SMMC7721 hepatoma cells, JNK1 knockdown sensitized cells to TRAIL-induced apoptosis, while neither JNK1 nor JNK2 depletion altered etoposide-induced apoptosis, demonstrating stimulus- and isoform-dependent behavior. | siRNA cell-line experiments. MAPK8/JNK1-specific but preclinical; no human therapeutic efficacy established. | Immunoblot quantification used three experiments (n=3); significance was reported at P<0.05 or P<0.01, without extractable numerical effect sizes. | Yu et al., online Oct. 30, 2023, DOI (yu2023componentsofthe pages 11-13, yu2023componentsofthe pages 6-7, yu2023componentsofthe pages 1-2) |
| CLL target evidence, 2024 | Primary CLL showed MAPK8/JNK1 overexpression and hyperphosphorylation. MAPK8-directed siRNAs reduced viability, while JNK inhibitors induced apoptosis and retained activity in BTK/SYK-inhibitor-resistant CLL. | Human samples, genetic knockdown, pharmacology, and mouse xenografts. Genetic evidence is MAPK8-specific; SP600125, CC-930, and L-JNKi do not establish complete JNK1 or kinome selectivity. Preclinical. | JNK1 mRNA was 3.5-fold higher in 20 CLL samples versus 7 controls; total/phosphorylated JNK1 increased in 20/21 cases. Among 43 primary CLL samples, 49% were responsive and 30% intermediate; normal B cells from five donors showed no survival effect at tested concentrations. | Saleem et al., Nov. 2024, DOI (saleem2024jnk1inhibitorstarget pages 2-3, saleem2024jnk1inhibitorstarget pages 4-5, saleem2024jnk1inhibitorstarget pages 3-4) |
| CLL pathway and in-vivo efficacy, 2024 | JNK1 functions downstream of BCR-associated SYK/PI3K signaling and regulates c-Jun, BCL2, and MCL1. SP600125 reduced CLL burden in xenografts, including BTK-inhibitor-resistant disease, and altered T-cell subsets/functions. | Mechanistic primary-cell and mouse experiments; pharmacological attribution remains limited by inhibitor selectivity. Preclinical. | SYK inhibition reduced p-JNK1 by 30–50%; PI3K inhibition by 45–59%; SYK knockdown reduced it by 42–67%. In one resistant xenograft, splenic CLL fell from 16.8% to 7.21% after 14 days (n=6/group). Tregs declined from 1.38×10⁶ to 0.56×10⁶. | Saleem et al., Nov. 2024, DOI (saleem2024jnk1inhibitorstarget pages 6-7, saleem2024jnk1inhibitorstarget pages 12-13, saleem2024jnk1inhibitorstarget pages 8-9, saleem2024jnk1inhibitorstarget pages 13-13) |
Table: Concise evidence map covering MAPK8 identity, enzymology, activation, substrate recognition, localization, and recent disease studies. It distinguishes MAPK8-specific findings from pan-JNK evidence and flags translational results that remain preclinical.
The identity chain is Homo sapiens MAPK8 → JNK1/SAPK1c → UniProt P45983. The literature recognizes three separate JNK genes: MAPK8/JNK1, MAPK9/JNK2, and MAPK10/JNK3. JNK1 and JNK2 are broadly expressed, whereas JNK3 has a more restricted distribution, especially in nervous tissue. This distinction is important because many papers measure “JNK” collectively or use antibodies and inhibitors that do not separate the three gene products. (koch2015inhibitorsofcjun pages 1-5, gehi2022intrinsicdisorderin pages 17-18, nadel2023jnkcascadeinducedapoptosis—a pages 1-2)
The supplied UniProt annotations—protein-kinase superfamily, CMGC Ser/Thr kinase group, protein-kinase domain, MAPK signature, and JNK-family classification—are fully concordant with the literature. Alternative splicing produces approximately 46- and 54/55-kDa JNK1 forms. Sources differ in how they count transcripts or protein isoforms—one review describes four conventional JNK1 forms, whereas a 2023 review counts eight alternatively spliced forms—probably reflecting different transcript/protein annotation conventions. These counts should therefore not be treated as contradictory biochemical evidence. (koch2015inhibitorsofcjun pages 1-5, nadel2023jnkcascadeinducedapoptosis—a pages 2-4)
MAPK8/JNK1 is a protein serine/threonine kinase. Its kinase domain binds ATP and transfers the terminal phosphate to hydroxyl groups on protein serine or threonine residues. JNKs are proline directed: the minimal phosphoacceptor preference is generally Ser/Thr-Pro. This local motif is insufficient by itself to define a physiological substrate because short S/T-P sequences are abundant. Productive phosphorylation depends heavily on docking motifs, accessibility, subcellular colocalization, scaffold assembly, and signal duration. (zeke2016jnksignalingregulation pages 10-10)
Many substrates, upstream MAP2Ks, phosphatases, and scaffolds recruit JNK through approximately 9–18-residue D-motifs. These bind a negatively charged common-docking region and adjacent hydrophobic groove on the kinase. JIP1-like and NFAT4-like docking motifs represent structurally distinct interaction classes. Because the docking surfaces of JNK1, JNK2, and JNK3 are nearly identical, a demonstrated JNK-binding motif does not by itself establish JNK1 selectivity. (zeke2016jnksignalingregulation pages 10-10)
Canonical substrates include c-Jun and ATF2. JNK was originally defined through phosphorylation of the c-Jun N-terminal sites Ser63 and Ser73, which enhances AP-1-associated transcriptional responses. Reviews report more than 100 JNK substrates and at least 30 transcription factors, but those totals describe the JNK family rather than a rigorously validated JNK1-only substrate set. (koch2015inhibitorsofcjun pages 1-5, gehi2022intrinsicdisorderin pages 17-18)
Full activation requires phosphorylation of the JNK1 activation-loop sequence Thr183-Pro-Tyr185. MKK7 preferentially phosphorylates the threonine, whereas MKK4 preferentially phosphorylates the tyrosine; their combined action can produce synergistic activation. This dual-input mechanism connects JNK1 to MAP3K-driven responses initiated by oxidative stress, inflammatory cytokines, ribotoxic or genotoxic stress, small GTPases, and receptor-associated signaling systems. (koch2015inhibitorsofcjun pages 1-5, nadel2023jnkcascadeinducedapoptosis—a pages 2-4, nadel2023jnkcascadeinducedapoptosis—a pages 1-2)
The pathway is therefore commonly represented as:
stress/receptor → MAP3K → MKK4/MKK7 → MAPK8/JNK1 → substrates such as c-Jun/ATF2.
This simple cascade is an abstraction. In cells, scaffold proteins—including JIP-family proteins, POSH and β-arrestin-associated complexes—organize selected upstream kinases, JNK, and substrates. AKT-mediated phosphorylation of cascade components or scaffolds can inhibit signaling. (nadel2023jnkcascadeinducedapoptosis—a pages 13-14, nadel2023jnkcascadeinducedapoptosis—a pages 2-4)
JNK output is restrained by phosphatases, including dual-specificity MAPK phosphatases and serine/threonine phosphatases. Reported regulators include MKP1/DUSP1, MKP5, PPM1H, PPM1J, PP2A, and PP5. Dephosphorylation, protein degradation, feedback regulation, and relocalization collectively control the amplitude and duration of the response. Much of this evidence is pan-JNK; individual phosphatases should not automatically be assigned as uniquely regulating MAPK8. (nadel2023jnkcascadeinducedapoptosis—a pages 13-14, nadel2023jnkcascadeinducedapoptosis—a pages 2-4)
MAPK8/JNK1 is an intracellular, non-receptor kinase, not a secreted or transmembrane protein. In unstimulated cells, JNK signaling is commonly organized in cytoplasmic complexes associated with scaffolds and regulatory proteins. Following activation, JNK can translocate into the nucleus through importin-dependent mechanisms involving Imp7, Imp9, and Imp3, where it phosphorylates c-Jun, ATF2, and other transcriptional regulators. (gehi2022intrinsicdisorderin pages 17-18, nadel2023jnkcascadeinducedapoptosis—a pages 2-4)
JNK activity is also reported in cytoskeletal and organelle-associated signaling contexts. These pools provide routes for regulating microtubules, actin-associated structures, trafficking, mitochondrial apoptosis, and localized stress responses. Nevertheless, the strongest retrieved localization evidence is family-level rather than MAPK8-exclusive. A conservative annotation is therefore: predominantly cytoplasmic and nuclear, with stimulus-dependent nuclear accumulation and context-dependent association with scaffolds, cytoskeleton, and organelles.
MAPK8’s primary role is to act as a regulated phosphorylation switch in the JNK stress-activated MAPK pathway. It integrates upstream kinase activity and redistributes that information to transcriptional and cytoplasmic substrates. Its output is determined by stimulus identity, signal strength and duration, cell type, scaffold composition, localization, splice isoform, and the concurrent activity of JNK2/JNK3 and other MAPKs. (zeke2016jnksignalingregulation pages 10-10, nadel2023jnkcascadeinducedapoptosis—a pages 2-4)
Principal pathway contexts include:
Yu and colleagues, published online 30 October 2023, used RNA interference in HepG2 and SMMC7721 hepatoma cells. JNK1 depletion sensitized cells to TRAIL-induced apoptosis, whereas depletion of either JNK1 or JNK2 did not materially alter etoposide-induced apoptosis. In contrast, JNK2 depletion reduced early apoptosis after TNF-α/cycloheximide or anisomycin in the reported experiments. Immunoblot quantification used three experiments and reported P<0.05 or P<0.01, but numerical effect sizes were not available in the extracted text. DOI URL. (yu2023componentsofthe pages 11-13, yu2023componentsofthe pages 6-7, yu2023componentsofthe pages 1-2)
The expert interpretation is not that JNK1 has a single oncogenic or tumor-suppressive role. Rather, the results demonstrate stimulus-specific division of labor between JNK1 and JNK2. The authors suggested that selective JNK1 targeting could have value in HCC, but this remains cell-line evidence; ATP-site inhibitor SP600125 cannot reliably distinguish JNK1 from JNK2. (yu2023componentsofthe pages 11-13)
Saleem and colleagues, published November 2024, identified MAPK8/JNK1 as overexpressed and hyperactivated in CLL. JNK1 mRNA was 3.5-fold higher in primary CLL samples (n=20) than in healthy CD19+ B cells (n=7), and increased total and phosphorylated JNK1 was detected in 20 of 21 CLL samples. The investigators also analyzed public datasets, lymph-node tissue, and IGHV-defined subgroups. DOI URL. (saleem2024jnk1inhibitorstarget pages 2-3, saleem2024jnk1inhibitorstarget pages 3-4)
Four MAPK8/JNK1-directed siRNAs reduced CLL-cell viability, supplying target-specific genetic evidence. Pharmacologically, SP600125, CC-930, and the substrate-binding inhibitory peptide L-JNKi produced more than 30% apoptosis after 24 hours in most of 43 primary samples. Under the study’s classification criteria, 49% were responsive and 30% intermediate. Normal B cells from five donors showed no survival effect at the highest tested concentrations. The pharmacology should nevertheless be interpreted more cautiously than the siRNA experiments because these compounds do not establish complete JNK1 or kinome selectivity. (saleem2024jnk1inhibitorstarget pages 2-3, saleem2024jnk1inhibitorstarget pages 4-5)
Mechanistically, SYK inhibition lowered phospho-JNK1 by 30–50%, PI3K inhibition by 45–59%, and SYK knockdown by 42–67%. JNK1 inhibition decreased phosphorylation or expression of c-Jun and the survival proteins BCL2 and MCL1, supporting placement of JNK1 downstream of proximal B-cell-receptor kinases. (saleem2024jnk1inhibitorstarget pages 6-7)
Activity extended to three primary CLL samples resistant to BTK- or combined BTK/SYK-directed treatment, including cases with BTK or PLCγ2 alterations. In one resistant patient-derived NOG-mouse xenograft, two weeks of SP600125 reduced splenic CLL representation from 16.8% to 7.21%, with n=6 per group. In TCL1-transgenic mice, treatment reduced leukemia-associated organ enlargement and signaling, lowered regulatory T cells from 1.38×10⁶ to 0.56×10⁶, and increased CD4+ effector-cell degranulation/cytotoxic function without significantly reducing total CD4+ or CD8+ cell numbers. (saleem2024jnk1inhibitorstarget pages 12-13, saleem2024jnk1inhibitorstarget pages 8-9, saleem2024jnk1inhibitorstarget pages 13-13)
These results constitute a credible preclinical application—using JNK1-directed intervention to bypass proximal BCR-inhibitor resistance—but not a demonstrated clinical treatment. The model systems, small resistant-case series, and imperfect inhibitor selectivity are material limitations.
MAPK8 activity is routinely used as a readout of cellular stress and MAPK signaling, generally through phospho-Thr183/Tyr185 immunoblotting, immunohistochemistry, flow-based assays, or measurement of phosphorylated c-Jun. A 2024 study demonstrated monitoring of endogenous MAPK8 phosphorylation using a CRISPR-inserted, 1.3-kDa HiBiT tag and a homogeneous BRET immunoassay, illustrating a practical platform for drug screening and stimulus-response profiling while preserving endogenous gene regulation. The retrieved text did not provide assay-performance statistics sufficient for quantitative comparison with conventional methods.
JNK-directed medicinal chemistry has explored ATP-competitive, covalent, allosteric, and substrate-docking inhibitors. The central expert concern is selectivity: ATP-binding sites are highly conserved across JNK paralogs and the broader kinome, while JNK1–3 also have nearly identical docking surfaces. Consequently, apparent “JNK1 inhibitor” phenotypes require genetic corroboration, paralog profiling, and broad kinase-selectivity measurements. (zeke2016jnksignalingregulation pages 10-10, koch2015inhibitorsofcjun pages 1-5)
CC-90001, derived from CC-930, has undergone phase I/II testing in pulmonary fibrosis, demonstrating clinical implementation of JNK-pathway pharmacology rather than validated MAPK8-specific therapy. The cited discussion reported respiratory infections in 21% of participants, while erythrocytes, platelets, granulocytes, and T cells were reportedly unaffected. These data should not be interpreted as proof that selectively inhibiting MAPK8 is safe or effective because the compound and clinical context are not strictly JNK1-specific. (saleem2024jnk1inhibitorstarget pages 13-13)
Open Targets aggregates MAPK8 associations with cancer, neurodegenerative disease, xenobiotic responses, poisoning, and muscle cramps. These associations support biological and translational relevance but are heterogeneous database-level evidence, not proof that MAPK8 is causal or clinically actionable in every listed condition. (OpenTargets Search: -MAPK8)
High-confidence annotation: MAPK8/P45983 is human JNK1, an intracellular CMGC-family MAP kinase that catalyzes ATP-dependent phosphorylation of proline-directed serine/threonine sites. It is activated by MKK4/MKK7-mediated phosphorylation of Thr183/Tyr185 and transmits stress and receptor signals to c-Jun, ATF2, and other substrates. Its function is executed in scaffolded cytoplasmic complexes and, following activation, in the nucleus. (zeke2016jnksignalingregulation pages 10-10, koch2015inhibitorsofcjun pages 1-5, gehi2022intrinsicdisorderin pages 17-18)
Moderate-confidence, context-dependent annotation: JNK1 participates in apoptosis, survival, inflammation, metabolism, cytoskeletal regulation, and oncogenic signaling. The direction of effect cannot be inferred from activation alone; it depends on cell type, stimulus, localization, signal duration, and paralog compensation. (zeke2016jnksignalingregulation pages 10-10, yu2023componentsofthe pages 11-13, yu2023componentsofthe pages 6-7)
Promising but preclinical application: MAPK8/JNK1 inhibition in CLL, especially BTK-inhibitor-resistant disease, is supported by patient-sample, RNAi, and mouse-model evidence with substantial quantitative effects. Clinical efficacy and therapeutic index remain unproven. (saleem2024jnk1inhibitorstarget pages 2-3, saleem2024jnk1inhibitorstarget pages 12-13, saleem2024jnk1inhibitorstarget pages 8-9)
Principal evidence gap: Much of the established JNK literature is family-level. Claims about mitochondrial localization, individual substrates, disease causality, or inhibitor efficacy should be labeled pan-JNK unless MAPK8-specific genetics, isoform-resolved biochemistry, or selective pharmacology is available.
References
(koch2015inhibitorsofcjun pages 1-5): Pierre Koch, Matthias Gehringer, and Stefan A. Laufer. Inhibitors of c-jun n-terminal kinases: an update. Journal of medicinal chemistry, 58 1:72-95, Jan 2015. URL: https://doi.org/10.1021/jm501212r, doi:10.1021/jm501212r. This article has 134 citations and is from a highest quality peer-reviewed journal.
(nadel2023jnkcascadeinducedapoptosis—a pages 2-4): Guy Nadel, Galia Maik-Rachline, and Rony Seger. Jnk cascade-induced apoptosis—a unique role in gqpcr signaling. International Journal of Molecular Sciences, 24:13527, Aug 2023. URL: https://doi.org/10.3390/ijms241713527, doi:10.3390/ijms241713527. This article has 44 citations.
(nadel2023jnkcascadeinducedapoptosis—a pages 1-2): Guy Nadel, Galia Maik-Rachline, and Rony Seger. Jnk cascade-induced apoptosis—a unique role in gqpcr signaling. International Journal of Molecular Sciences, 24:13527, Aug 2023. URL: https://doi.org/10.3390/ijms241713527, doi:10.3390/ijms241713527. This article has 44 citations.
(zeke2016jnksignalingregulation pages 10-10): András Zeke, Mariya Misheva, Attila Reményi, and Marie A. Bogoyevitch. Jnk signaling: regulation and functions based on complex protein-protein partnerships. Microbiology and Molecular Biology Reviews, 80:793-835, Sep 2016. URL: https://doi.org/10.1128/mmbr.00043-14, doi:10.1128/mmbr.00043-14. This article has 666 citations and is from a domain leading peer-reviewed journal.
(gehi2022intrinsicdisorderin pages 17-18): Bhuvaneshwari R. Gehi, Kundlik Gadhave, Vladimir N. Uversky, and Rajanish Giri. Intrinsic disorder in proteins associated with oxidative stress-induced jnk signaling. Cellular and Molecular Life Sciences, Mar 2022. URL: https://doi.org/10.1007/s00018-022-04230-4, doi:10.1007/s00018-022-04230-4. This article has 23 citations and is from a domain leading peer-reviewed journal.
(saleem2024jnk1inhibitorstarget pages 2-3): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(saleem2024jnk1inhibitorstarget pages 8-9): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(saleem2024jnk1inhibitorstarget pages 4-5): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(yu2023componentsofthe pages 11-13): Jijun Yu, Xinying Li, Junxia Cao, Ting Zhu, Shuifeng Liang, Le Du, Meng Cao, Haitao Wang, Yaolin Zhang, Yinxi Zhou, Beifen Shen, Jiannan Feng, Jiyan Zhang, Jing Wang, and Jianfeng Jin. Components of the jnk–mapk pathway play distinct roles in hepatocellular carcinoma. Journal of Cancer Research and Clinical Oncology, 149:17495-17509, Oct 2023. URL: https://doi.org/10.1007/s00432-023-05473-9, doi:10.1007/s00432-023-05473-9. This article has 25 citations and is from a peer-reviewed journal.
(yu2023componentsofthe pages 6-7): Jijun Yu, Xinying Li, Junxia Cao, Ting Zhu, Shuifeng Liang, Le Du, Meng Cao, Haitao Wang, Yaolin Zhang, Yinxi Zhou, Beifen Shen, Jiannan Feng, Jiyan Zhang, Jing Wang, and Jianfeng Jin. Components of the jnk–mapk pathway play distinct roles in hepatocellular carcinoma. Journal of Cancer Research and Clinical Oncology, 149:17495-17509, Oct 2023. URL: https://doi.org/10.1007/s00432-023-05473-9, doi:10.1007/s00432-023-05473-9. This article has 25 citations and is from a peer-reviewed journal.
(yu2023componentsofthe pages 1-2): Jijun Yu, Xinying Li, Junxia Cao, Ting Zhu, Shuifeng Liang, Le Du, Meng Cao, Haitao Wang, Yaolin Zhang, Yinxi Zhou, Beifen Shen, Jiannan Feng, Jiyan Zhang, Jing Wang, and Jianfeng Jin. Components of the jnk–mapk pathway play distinct roles in hepatocellular carcinoma. Journal of Cancer Research and Clinical Oncology, 149:17495-17509, Oct 2023. URL: https://doi.org/10.1007/s00432-023-05473-9, doi:10.1007/s00432-023-05473-9. This article has 25 citations and is from a peer-reviewed journal.
(saleem2024jnk1inhibitorstarget pages 3-4): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(saleem2024jnk1inhibitorstarget pages 6-7): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(saleem2024jnk1inhibitorstarget pages 12-13): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(saleem2024jnk1inhibitorstarget pages 13-13): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(nadel2023jnkcascadeinducedapoptosis—a pages 13-14): Guy Nadel, Galia Maik-Rachline, and Rony Seger. Jnk cascade-induced apoptosis—a unique role in gqpcr signaling. International Journal of Molecular Sciences, 24:13527, Aug 2023. URL: https://doi.org/10.3390/ijms241713527, doi:10.3390/ijms241713527. This article has 44 citations.
(saleem2024jnk1inhibitorstarget pages 9-10): Shifa Khaja Saleem, Sarah Decker, Sandra Kissel, Marcus Bauer, Dmitry Chernyakov, Daniela Bräuer-Hartmann, Konrad Aumann, Claudia Wickenhauser, Marco Herling, Oleksandra Skorobohatko, Nimitha Mathew, Cornelius Schmidt, Claudius Klein, Marie Follo, and Christine Dierks. Jnk1 inhibitors target distal b cell receptor signaling and overcome btk-inhibitor resistance in cll. The Journal of Experimental Medicine, Nov 2024. URL: https://doi.org/10.1084/jem.20230681, doi:10.1084/jem.20230681. This article has 3 citations.
(OpenTargets Search: -MAPK8): Open Targets Query (-MAPK8, 15 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.