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Research Report: Human JAK1 (UniProt P23458) — Functional Annotation, Mechanism, and Translational Applications

0) Target verification (critical disambiguation)

The literature and evidence summarized here correspond to human Janus kinase 1 (JAK1) with UniProt accession P23458 and kinase EC classification EC 2.7.10.2 (tyrosine-protein kinase). (adeyelu2023kinfamsdenovoclassification pages 10-12, lv2024thejakstatpathway pages 11-12)

1) Key concepts and definitions (current understanding)

1.1 What JAK1 is

JAK1 is an intracellular, non-receptor tyrosine kinase that operates as the receptor-proximal catalytic component of the JAK–STAT signaling pathway, transducing extracellular cytokine signals into transcriptional responses. Mechanistically, activated JAKs phosphorylate (i) themselves, (ii) cytokine receptors, and (iii) STAT transcription factors, which then dimerize and enter the nucleus to regulate gene expression. (jarneborn2025thedualedgedsword pages 2-4)

1.2 Domain architecture (structure → function)

JAK-family kinases (including JAK1) are multi-domain proteins typically described by Janus homology (JH) regions:
- N-terminus: a receptor-binding FERM–SH2 “holodomain” (FERM + SH2-like domains) mediates association to membrane-proximal receptor motifs. (lv2024thejakstatpathway pages 11-12, lv2024thejakstatpathway pages 12-15)
- C-terminus: a tandem pseudokinase domain (JH2) and catalytic tyrosine kinase domain (JH1), where JH2 is regulatory/autoinhibitory and JH1 is the enzymatic kinase. (lv2024thejakstatpathway pages 11-12, lv2024thejakstatpathway pages 12-15)

A kinase-family classification study explicitly annotates human JAK1 (P23458) as EC 2.7.10.2 and delineates two “kinase-like” domains: a non-catalytic/pseudokinase region (residues 583–855) and the active kinase region (residues 875–1153). (adeyelu2023kinfamsdenovoclassification pages 10-12)

1.3 Catalytic activity and substrate specificity (functional core)

JAK1’s JH1 domain is the active tyrosine kinase module. The same kinase-family analysis reports canonical active-site motif residues in JAK1’s catalytic domain, including K908 (N-lobe), D1003 within the HRD motif, and D1022 within the DFG motif—hallmarks of protein kinase catalysis and ATP-dependent phosphotransfer. (adeyelu2023kinfamsdenovoclassification pages 10-12)

Operationally in cells, JAK1 catalyzes phosphorylation events on:
- cytokine receptor cytoplasmic tails (creating phosphotyrosine docking sites), and
- STAT proteins (triggering STAT dimerization and transcriptional activation). (jarneborn2025thedualedgedsword pages 2-4)

2) Cellular localization and where JAK1 acts

JAKs are cytosolic kinases that are anchored near the plasma membrane by binding to cytokine receptor cytoplasmic motifs; this receptor tethering is mediated by the FERM region (and associated SH2-like elements) and positions JAK1 for rapid activation upon receptor engagement/dimerization. (jarneborn2025thedualedgedsword pages 2-4, lv2024thejakstatpathway pages 11-12)

3) Pathways and biological role: JAK1 in cytokine receptor signaling

3.1 Receptor binding mechanism (box 1/box 2 interaction model)

A 2024 structural review provides JAK1-specific receptor binding detail: the intracellular “box 1” motif binds the F2 subdomain of the FERM module, while “box 2” binds the SH2-like domain; the combined box1+box2 epitope spans ~85 Å and buries >1000 Ų of surface area in the receptor–JAK1 interface. (lv2024thejakstatpathway pages 12-15)

A solved complex is described for the human JAK1 FERM–SH2 holodomain bound to IFNλR1 receptor motifs, illustrating this receptor-engagement mode experimentally/structurally. (lv2024thejakstatpathway pages 12-15, lv2024thejakstatpathway pages 11-12)

3.2 Cytokine/JAK pairing logic (functional wiring)

JAK1 participates in multiple cytokine receptor complexes and commonly signals as heterodimers (or coordinated pairs) with other JAKs. Reported examples of JAK1-containing receptor/JAK pairs include:
- IFN-γ receptor signaling: JAK1 + JAK2 leading to STAT1 recruitment/activation (representative example in immunology/cancer context). (liu2026jakinhibitionin pages 2-3)
- Type I interferons (IFN-α/β): JAK1 + TYK2. (djidjik2025jakstatinhuman pages 2-3)
- IL-10 family signaling: JAK1 + TYK2. (djidjik2025jakstatinhuman pages 2-3)
- Common γ-chain cytokines (e.g., IL‑2, IL‑4, IL‑7, IL‑21): JAK1 + JAK3. (djidjik2025jakstatinhuman pages 2-3, jarneborn2025thedualedgedsword pages 2-4)
- IL‑6/gp130 signaling: JAK1 is described as associating with the gp130 receptor system (a major pro-inflammatory axis). (jarneborn2025thedualedgedsword pages 2-4)

These pairings help explain why JAK1-selective inhibition can broadly dampen inflammatory signaling: JAK1 sits at key junctions for interferon, IL‑6 family, and multiple lymphocyte cytokine pathways. (jarneborn2025thedualedgedsword pages 4-6, jarneborn2025thedualedgedsword pages 2-4)

4) Mechanistic regulation: autoinhibition, activation, and regulatory phosphorylation

4.1 Pseudokinase (JH2) regulation and autoinhibition

A central regulatory concept is that the JH2 pseudokinase domain restrains JAK activity at baseline and is required for proper control of the catalytic JH1 kinase domain. A 2024 structural synthesis notes that deletion of the pseudokinase domain can increase basal kinase activity, supporting an autoinhibitory role for JH2. (lv2024thejakstatpathway pages 12-15)

4.2 Activation model: receptor-driven rearrangements and TK release

Cytokine binding induces receptor dimerization/oligomerization that repositions receptor-bound JAKs, shifting JAK1 from an inhibited state to an active configuration (including changes in relative placement/orientation of the JH1 kinase domains). (lv2024thejakstatpathway pages 12-15, sun2024anovelapproach pages 1-2)

A 2024 computational study of full-length JAK1 activation proposes that activation is thermodynamically favorable but faces an initial energy barrier associated with releasing the tyrosine kinase domain from an inhibited “FERM–PK cavity” state. (sun2024anovelapproach pages 1-2)

4.3 Activation loop phosphorylation sites (JAK1-specific)

A clinical-immunology-focused review lists JAK1 activation-loop tyrosines Y1022/Y1023 as phosphorylation sites, with Y1023 reported to be more highly phosphorylated than Y1022—supporting an activation-loop phosphorylation mechanism typical of kinases. (djidjik2025jakstatinhuman pages 2-3)

5) Recent developments (prioritizing 2023–2024) and latest research directions

5.1 2024 structural biology consolidation

A high-impact 2024 review integrates structural biology of the JAK–STAT pathway and provides JAK1-specific receptor engagement (IFNλR1 complex) and domain-organization schematics, helping refine mechanistic understanding of how receptor motifs organize the JAK1 FERM–SH2 interface and how JH2 regulates JH1 activation. (lv2024thejakstatpathway pages 12-15, lv2024thejakstatpathway pages 11-12)

5.2 2024 systems/biophysical modeling of JAK1 activation transitions

The 2024 Briefings in Bioinformatics study models inhibited vs activated JAK1 full-length conformations and analyzes energetically plausible activation paths; it also uses pathogenic/regulatory mutations (e.g., in the pseudokinase region) to rationalize negative vs positive regulatory effects on activation dynamics. (sun2024anovelapproach pages 1-2)

6) Current applications and real-world implementations (JAK1-selective inhibitors)

6.1 Therapeutic rationale: why JAK1 selectivity matters

In clinical inflammatory disease contexts (e.g., ulcerative colitis), JAK1 is described as mediating inflammatory cytokine signals, motivating JAK1-selective inhibitors to preferentially suppress pro-inflammatory pathways while attempting to spare JAK2-driven hematopoietic functions. (caballeromateos2024gamechangerhow pages 2-4)

6.2 Ulcerative colitis (UC)

A 2024 clinical review of UC management reports rapid onset of JAK inhibitors (days 1–3) and provides remission percentages at specific timepoints. Reported values include:
- Upadacitinib: remission up to 80% at 8 weeks and 38% at 52 weeks (as summarized in that review). (caballeromateos2024gamechangerhow pages 2-4)
- Filgotinib: remission 71.9% at week 12 and 76.4% at week 24 (as summarized in that review). (caballeromateos2024gamechangerhow pages 2-4)

Clinical trial implementation example (registry):
- SELECTION trial (NCT02914522): Phase 2b/3, completed, n=1351, evaluating filgotinib 100/200 mg for induction and maintenance of remission in moderately-to-severely active UC. (NCT02914522 chunk 1)

6.3 Atopic dermatitis (AD)

A 2024 umbrella review of meta-analyses quantifies efficacy of JAK inhibitors (including JAK1-selective agents) in AD:
- IGA response: pooled RR 2.83 (95% CI 2.25–3.56). (he2024januskinaseinhibitors pages 1-2)
- EASI75: pooled RR 2.84 (95% CI 2.2–3.67). (he2024januskinaseinhibitors pages 1-2)
- Pruritus (PP‑NRS): pooled SMD −0.49 (95% CI −0.67 to −0.32). (he2024januskinaseinhibitors pages 1-2)
Drug/dose-specific quantitative signals include:
- Upadacitinib: rapid IGA effect RR 5.3 (95% CI 4.19–6.71). (he2024januskinaseinhibitors pages 8-11)
- Abrocitinib: overall IGA response RR 3.02 (95% CI 2.26–4.02); 200 mg vs 100 mg IGA response RR 2.52 (95% CI 1.92–3.3). (he2024januskinaseinhibitors pages 8-11)

Real-world and Phase 4 implementation examples (registry):
- NCT05507580 (upadacitinib): Phase 4, completed, n=461, treat-to-target and dosing flexibility design (15/30 mg), primary endpoint EASI90 at week 24. (NCT05507580 chunk 1)
- NCT05602207 (abrocitinib): Phase 4, completed, n=24, abrocitinib 100 mg QD for 12 weeks in dupilumab inadequate responders; includes skin biomarker assessment (e.g., CCL18, MMP12, K16, S100A7/A8/A9). (NCT05602207 chunk 1)
- NCT05391061 (abrocitinib): recruiting observational post-marketing study in Korea; primary outcomes emphasize AE/ADR surveillance up to 52 weeks and effectiveness endpoints (e.g., IGA, EASI-75, itch improvement). (NCT05391061 chunk 1)

7) Safety, risk–benefit, and expert synthesis (2023–2024 prioritized)

7.1 Quantitative safety signals in AD meta-evidence (2024)

The 2024 umbrella review reports no overall increase in discontinuations or serious adverse events across meta-analyses, but highlights drug- and dose-specific adverse-event risk ratios:
- Abrocitinib 200 mg: acne RR 4.34, headache RR 1.76, nausea RR 7.81. (he2024januskinaseinhibitors pages 1-2)
- Upadacitinib: acne RR 6.23, nasopharyngitis RR 1.36, elevated blood CPK RR 2.41. (he2024januskinaseinhibitors pages 1-2)
- Systemic JAK inhibitors: TEAEs increased vs placebo RR 1.23 (95% CI 1.11–1.36). (he2024januskinaseinhibitors pages 8-11)

The same umbrella review qualitatively reiterates regulatory concern (FDA boxed warnings as of July 2022) for major adverse cardiovascular events, malignancy, thrombosis, and death risks for certain JAK inhibitors, motivating patient selection and risk stratification. (he2024januskinaseinhibitors pages 13-15)

7.2 Upadacitinib safety synthesis across indications (2024 systematic review)

A 2024 systematic literature review of indirect/direct treatment comparisons of RCTs summarizes upadacitinib safety across RA, PsA, AS, AD, UC, Crohn’s disease, and nr-axSpA, covering publications from 2018 to Aug 3, 2022:
- 16/25 studies (64%) reported no statistically significant difference in studied safety outcomes between upadacitinib and comparators/placebo; 9/25 (36%) had mixed results, with 8/25 (32%) reporting higher event rates and 1/25 (4%) lower rates. (mysler2024safetyofupadacitinib pages 1-2, mysler2024safetyofupadacitinib pages 2-5)
The review also reports that in the subset of analyses available in the excerpt, MACE, VTE, and malignancy comparisons were often not statistically different (with sparse reporting by outcome), reinforcing that safety interpretation depends on indication, comparator, and follow-up. (mysler2024safetyofupadacitinib pages 22-24)

8) Disease/target association landscape (database triangulation)

Open Targets lists JAK1 among top associated targets for immune-mediated inflammatory diseases such as atopic eczema and rheumatoid arthritis, with evidence including approved clinical-stage associations (e.g., therapeutics targeting the pathway). (OpenTargets Search: -JAK1)

9) Visual evidence (domain and receptor-binding schematic)

Key structural schematics and the receptor-binding example for human JAK1 are available in Lv et al. 2024 Figure 7, including the JAK domain organization and a JAK1 FERM–SH2 complex with IFNλR1 box1/box2 motifs. (lv2024thejakstatpathway media 48c6cfbc, lv2024thejakstatpathway media 2685a077, lv2024thejakstatpathway media 299b38a0)

10) Evidence summary table

Table: This table compacts the most actionable functional-annotation facts for human JAK1 (UniProt P23458), including identity, mechanism, pathway pairings, therapeutic applications, safety signals, and trial metadata. It is useful as a citation-ready summary for downstream narrative reporting.

11) Practical functional annotation (concise, actionable)

• Molecular function: ATP-dependent protein tyrosine kinase (EC 2.7.10.2) that phosphorylates cytokine receptors and STATs downstream of cytokine receptor engagement. (adeyelu2023kinfamsdenovoclassification pages 10-12, jarneborn2025thedualedgedsword pages 2-4)
• Substrate/context specificity: functions in receptor-proximal complexes, commonly pairing with JAK2, JAK3, or TYK2 depending on receptor (e.g., IFN-γ: JAK1/JAK2; IFN-α/β and IL‑10: JAK1/TYK2; IL‑2/4/7/21: JAK1/JAK3). (djidjik2025jakstatinhuman pages 2-3, jarneborn2025thedualedgedsword pages 2-4)
• Localization: intracellular, enriched at plasma membrane-proximal receptor complexes via FERM–SH2 binding to receptor box motifs. (jarneborn2025thedualedgedsword pages 2-4, lv2024thejakstatpathway pages 12-15)
• Regulation: autoinhibition via JH2 pseudokinase, activation-loop phosphorylation at Y1022/Y1023, and negative feedback via SOCS/PIAS/phosphatases in the broader pathway. (lv2024thejakstatpathway pages 12-15, djidjik2025jakstatinhuman pages 2-3, jarneborn2025thedualedgedsword pages 2-4)

Limitations of this report (transparency)

Some highly detailed biochemical specifics (e.g., direct in vitro substrate panels, catalytic kcat/Km values for particular peptide substrates, or exhaustive residue-level mapping of receptor preferences across all cytokine receptors) were not available within the retrieved excerpts. The report therefore emphasizes well-supported pathway-level substrate classes (receptor tails and STATs) and mechanistic structural evidence from recent reviews and synthesis studies.

References

1. (adeyelu2023kinfamsdenovoclassification pages 10-12): Tolulope Adeyelu, Nicola Bordin, Vaishali P. Waman, Marta Sadlej, Ian Sillitoe, Aurelio A. Moya-Garcia, and Christine A. Orengo. Kinfams: de-novo classification of protein kinases using cath functional units. Biomolecules, 13:277, Feb 2023. URL: https://doi.org/10.3390/biom13020277, doi:10.3390/biom13020277. This article has 12 citations.

2. (lv2024thejakstatpathway pages 11-12): You Lv, Jianxun Qi, Jeff J. Babon, Longxing Cao, Guohuang Fan, Jiajia Lang, Jin Zhang, Pengbing Mi, B. Kobe, and Faming Wang. The jak-stat pathway: from structural biology to cytokine engineering. Signal Transduction and Targeted Therapy, Aug 2024. URL: https://doi.org/10.1038/s41392-024-01934-w, doi:10.1038/s41392-024-01934-w. This article has 122 citations and is from a peer-reviewed journal.

3. (jarneborn2025thedualedgedsword pages 2-4): Anders Jarneborn, Pradeep Kumar Kopparapu, and Tao Jin. The dual-edged sword: risks and benefits of jak inhibitors in infections. Pathogens, 14:324, Mar 2025. URL: https://doi.org/10.3390/pathogens14040324, doi:10.3390/pathogens14040324. This article has 9 citations.

4. (lv2024thejakstatpathway pages 12-15): You Lv, Jianxun Qi, Jeff J. Babon, Longxing Cao, Guohuang Fan, Jiajia Lang, Jin Zhang, Pengbing Mi, B. Kobe, and Faming Wang. The jak-stat pathway: from structural biology to cytokine engineering. Signal Transduction and Targeted Therapy, Aug 2024. URL: https://doi.org/10.1038/s41392-024-01934-w, doi:10.1038/s41392-024-01934-w. This article has 122 citations and is from a peer-reviewed journal.

5. (liu2026jakinhibitionin pages 2-3): Ziyuan Liu, Jiaqi Liu, Hongyu Chu, Zhuming Lu, Shengshan Xu, Yanguo Qin, Lianfang Zhao, and Chi Zhang. Jak inhibition in pd-1 immunotherapy and tumor microenvironment. Frontiers in Immunology, Apr 2026. URL: https://doi.org/10.3389/fimmu.2026.1790936, doi:10.3389/fimmu.2026.1790936. This article has 0 citations and is from a peer-reviewed journal.

6. (djidjik2025jakstatinhuman pages 2-3): Reda Djidjik, Lydia Lamara Mahammed, Lilya Meriem Berkani, Ines Allam, Alaa Hamidou Benmoussa, Merzak Gharnaout, and Brahim Belaid. Jak/stat in human diseases: a common axis in immunodeficiencies and hematological disorders. Frontiers in Immunology, Dec 2025. URL: https://doi.org/10.3389/fimmu.2025.1669688, doi:10.3389/fimmu.2025.1669688. This article has 3 citations and is from a peer-reviewed journal.

7. (jarneborn2025thedualedgedsword pages 4-6): Anders Jarneborn, Pradeep Kumar Kopparapu, and Tao Jin. The dual-edged sword: risks and benefits of jak inhibitors in infections. Pathogens, 14:324, Mar 2025. URL: https://doi.org/10.3390/pathogens14040324, doi:10.3390/pathogens14040324. This article has 9 citations.

8. (sun2024anovelapproach pages 1-2): Shengjie Sun, Georgialina Rodriguez, Gaoshu Zhao, Jason E Sanchez, Wenhan Guo, Dan Du, Omar J Rodriguez Moncivais, Dehua Hu, Jing Liu, Robert Arthur Kirken, and Lin Li. A novel approach to study multi-domain motions in jak1’s activation mechanism based on energy landscape. Briefings in Bioinformatics, Jan 2024. URL: https://doi.org/10.1093/bib/bbae079, doi:10.1093/bib/bbae079. This article has 13 citations and is from a domain leading peer-reviewed journal.

9. (caballeromateos2024gamechangerhow pages 2-4): Antonio M Caballero-Mateos and Guillermo Arturo Cañadas-de la Fuente. Game changer: how janus kinase inhibitors are reshaping the landscape of ulcerative colitis management. World Journal of Gastroenterology, 30:3942-3953, Sep 2024. URL: https://doi.org/10.3748/wjg.v30.i35.3942, doi:10.3748/wjg.v30.i35.3942. This article has 18 citations.

10. (NCT02914522 chunk 1): Study to Evaluate the Efficacy and Safety of Filgotinib in the Induction and Maintenance of Remission in Adults With Moderately to Severely Active Ulcerative Colitis. Gilead Sciences. 2016. ClinicalTrials.gov Identifier: NCT02914522

11. (he2024januskinaseinhibitors pages 1-2): Qingying He, Xin Xie, Qian Chen, Wenquan Li, Zongzhou Song, Xurui Wang, Xiao Ma, Jinhao Zeng, and Jing Guo. Janus kinase inhibitors in atopic dermatitis: an umbrella review of meta-analyses. Frontiers in Immunology, Feb 2024. URL: https://doi.org/10.3389/fimmu.2024.1342810, doi:10.3389/fimmu.2024.1342810. This article has 19 citations and is from a peer-reviewed journal.

12. (he2024januskinaseinhibitors pages 8-11): Qingying He, Xin Xie, Qian Chen, Wenquan Li, Zongzhou Song, Xurui Wang, Xiao Ma, Jinhao Zeng, and Jing Guo. Janus kinase inhibitors in atopic dermatitis: an umbrella review of meta-analyses. Frontiers in Immunology, Feb 2024. URL: https://doi.org/10.3389/fimmu.2024.1342810, doi:10.3389/fimmu.2024.1342810. This article has 19 citations and is from a peer-reviewed journal.

13. (NCT05507580 chunk 1): A Study to Assess Treat-to-Target and Dosing Flexibility of Oral Upadacitinib Tablets in Adult Participants With Moderate to Severe Atopic Dermatitis. AbbVie. 2023. ClinicalTrials.gov Identifier: NCT05507580

14. (NCT05602207 chunk 1): Effects of Abrocitinib in Subjects With Atopic Dermatitis With an Unsatisfactory Response After Treatment With Dupilumab. Innovaderm Research Inc.. 2022. ClinicalTrials.gov Identifier: NCT05602207

15. (NCT05391061 chunk 1): A Study to Learn About the Study Medicine (Called Cibinqo) in People With Atopic Dermatitis. Pfizer. 2023. ClinicalTrials.gov Identifier: NCT05391061

16. (he2024januskinaseinhibitors pages 13-15): Qingying He, Xin Xie, Qian Chen, Wenquan Li, Zongzhou Song, Xurui Wang, Xiao Ma, Jinhao Zeng, and Jing Guo. Janus kinase inhibitors in atopic dermatitis: an umbrella review of meta-analyses. Frontiers in Immunology, Feb 2024. URL: https://doi.org/10.3389/fimmu.2024.1342810, doi:10.3389/fimmu.2024.1342810. This article has 19 citations and is from a peer-reviewed journal.

17. (mysler2024safetyofupadacitinib pages 1-2): Eduardo Mysler, Gerd R. Burmester, Christopher D. Saffore, John Liu, Lani Wegrzyn, Chelsey Yang, Keith A. Betts, Yan Wang, Alan D. Irvine, and Remo Panaccione. Safety of upadacitinib in immune-mediated inflammatory diseases: systematic literature review of indirect and direct treatment comparisons of randomized controlled trials. Advances in Therapy, 41:567-597, Jan 2024. URL: https://doi.org/10.1007/s12325-023-02732-6, doi:10.1007/s12325-023-02732-6. This article has 22 citations and is from a peer-reviewed journal.

18. (mysler2024safetyofupadacitinib pages 2-5): Eduardo Mysler, Gerd R. Burmester, Christopher D. Saffore, John Liu, Lani Wegrzyn, Chelsey Yang, Keith A. Betts, Yan Wang, Alan D. Irvine, and Remo Panaccione. Safety of upadacitinib in immune-mediated inflammatory diseases: systematic literature review of indirect and direct treatment comparisons of randomized controlled trials. Advances in Therapy, 41:567-597, Jan 2024. URL: https://doi.org/10.1007/s12325-023-02732-6, doi:10.1007/s12325-023-02732-6. This article has 22 citations and is from a peer-reviewed journal.

19. (mysler2024safetyofupadacitinib pages 22-24): Eduardo Mysler, Gerd R. Burmester, Christopher D. Saffore, John Liu, Lani Wegrzyn, Chelsey Yang, Keith A. Betts, Yan Wang, Alan D. Irvine, and Remo Panaccione. Safety of upadacitinib in immune-mediated inflammatory diseases: systematic literature review of indirect and direct treatment comparisons of randomized controlled trials. Advances in Therapy, 41:567-597, Jan 2024. URL: https://doi.org/10.1007/s12325-023-02732-6, doi:10.1007/s12325-023-02732-6. This article has 22 citations and is from a peer-reviewed journal.

20. (OpenTargets Search: -JAK1): Open Targets Query (-JAK1, 19 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

21. (lv2024thejakstatpathway media 48c6cfbc): You Lv, Jianxun Qi, Jeff J. Babon, Longxing Cao, Guohuang Fan, Jiajia Lang, Jin Zhang, Pengbing Mi, B. Kobe, and Faming Wang. The jak-stat pathway: from structural biology to cytokine engineering. Signal Transduction and Targeted Therapy, Aug 2024. URL: https://doi.org/10.1038/s41392-024-01934-w, doi:10.1038/s41392-024-01934-w. This article has 122 citations and is from a peer-reviewed journal.

22. (lv2024thejakstatpathway media 2685a077): You Lv, Jianxun Qi, Jeff J. Babon, Longxing Cao, Guohuang Fan, Jiajia Lang, Jin Zhang, Pengbing Mi, B. Kobe, and Faming Wang. The jak-stat pathway: from structural biology to cytokine engineering. Signal Transduction and Targeted Therapy, Aug 2024. URL: https://doi.org/10.1038/s41392-024-01934-w, doi:10.1038/s41392-024-01934-w. This article has 122 citations and is from a peer-reviewed journal.

23. (lv2024thejakstatpathway media 299b38a0): You Lv, Jianxun Qi, Jeff J. Babon, Longxing Cao, Guohuang Fan, Jiajia Lang, Jin Zhang, Pengbing Mi, B. Kobe, and Faming Wang. The jak-stat pathway: from structural biology to cytokine engineering. Signal Transduction and Targeted Therapy, Aug 2024. URL: https://doi.org/10.1038/s41392-024-01934-w, doi:10.1038/s41392-024-01934-w. This article has 122 citations and is from a peer-reviewed journal.

24. (kwon2026revisitingjanuskinases pages 1-2): Sunghark Kwon. Revisiting janus kinases as molecular drug targets for rheumatic diseases. Frontiers in Medicine, Jan 2026. URL: https://doi.org/10.3389/fmed.2026.1716179, doi:10.3389/fmed.2026.1716179. This article has 1 citations.

25. (he2024januskinaseinhibitors pages 11-13): Qingying He, Xin Xie, Qian Chen, Wenquan Li, Zongzhou Song, Xurui Wang, Xiao Ma, Jinhao Zeng, and Jing Guo. Janus kinase inhibitors in atopic dermatitis: an umbrella review of meta-analyses. Frontiers in Immunology, Feb 2024. URL: https://doi.org/10.3389/fimmu.2024.1342810, doi:10.3389/fimmu.2024.1342810. This article has 19 citations and is from a peer-reviewed journal.

26. (mysler2024safetyofupadacitinib pages 24-26): Eduardo Mysler, Gerd R. Burmester, Christopher D. Saffore, John Liu, Lani Wegrzyn, Chelsey Yang, Keith A. Betts, Yan Wang, Alan D. Irvine, and Remo Panaccione. Safety of upadacitinib in immune-mediated inflammatory diseases: systematic literature review of indirect and direct treatment comparisons of randomized controlled trials. Advances in Therapy, 41:567-597, Jan 2024. URL: https://doi.org/10.1007/s12325-023-02732-6, doi:10.1007/s12325-023-02732-6. This article has 22 citations and is from a peer-reviewed journal.

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Citations

1. jarneborn2025thedualedgedsword pages 2-4
2. adeyelu2023kinfamsdenovoclassification pages 10-12
3. lv2024thejakstatpathway pages 12-15
4. liu2026jakinhibitionin pages 2-3
5. djidjik2025jakstatinhuman pages 2-3
6. sun2024anovelapproach pages 1-2
7. caballeromateos2024gamechangerhow pages 2-4
8. he2024januskinaseinhibitors pages 1-2
9. he2024januskinaseinhibitors pages 8-11
10. he2024januskinaseinhibitors pages 13-15
11. mysler2024safetyofupadacitinib pages 22-24
12. lv2024thejakstatpathway pages 11-12
13. jarneborn2025thedualedgedsword pages 4-6
14. mysler2024safetyofupadacitinib pages 1-2
15. mysler2024safetyofupadacitinib pages 2-5
16. kwon2026revisitingjanuskinases pages 1-2
17. he2024januskinaseinhibitors pages 11-13
18. mysler2024safetyofupadacitinib pages 24-26
19. https://doi.org/10.3390/biom13020277
20. https://doi.org/10.1038/s41392-024-01934-w
21. https://doi.org/10.3389/fmed.2026.1716179
22. https://doi.org/10.3390/pathogens14040324
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