this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 42 citations 2026-01-18T22:46:56.554532

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Plan and verification
- Identity check: The target is human ABL1 (UniProt P00519), a non-receptor tyrosine kinase with SH3–SH2–kinase (SH1) regulatory core, an N‑terminal myristoylation site that binds a myristoyl pocket in the kinase C‑lobe, and C‑terminal F‑/G‑actin binding and nuclear trafficking signals. These features and the autoinhibition mechanism are affirmed by recent structural/biophysical work and authoritative reviews (paladini2024themolecularbasis pages 16-17, paladini2024themolecularbasis pages 18-18, wu2024clinicalinsightsinto pages 2-4, sirvent2008cytoplasmicsignallingby pages 27-33, wang2014thecapableabl pages 1-2). The organism is Homo sapiens as required. No conflicting gene symbol usage was found.

Key concepts and definitions (current understanding)
- Domain architecture and allosteric autoinhibition: ABL1 comprises an N‑terminal myristoylated cap, SH3 and SH2 domains that assemble with the kinase domain into an autoinhibited core. Binding of the N‑myristoyl group to a hydrophobic pocket on the kinase C‑lobe promotes an SH3–SH2 “clamp” over the kinase, stabilizing an inactive state. The αI‑helix in the C‑lobe exerts force onto the SH2 domain and modulates core assembly; the E528K mutation in αI increases activity by weakening inhibitory contacts. Allosteric myristoyl‑pocket ligands (e.g., asciminib) fix the αI‑helix and favor autoinhibition (paladini2024themolecularbasis pages 16-17, paladini2024themolecularbasis pages 18-18, wu2024clinicalinsightsinto pages 2-4).
- Catalytic function: ABL1 is a tyrosine kinase (EC 2.7.10.2) that phosphorylates substrate tyrosines. The kinase toggles among inactive DFG‑out, Src‑like inactive, and active DFG‑in conformations; activation loop phosphorylation stabilizes activity (wu2024clinicalinsightsinto pages 2-4).
- Cellular localization signals: Multiple NLSs and one NES enable nucleocytoplasmic shuttling; a C‑terminal actin‑binding region localizes ABL1 to actin structures and embeds the NES, linking cytoplasmic localization to actin binding (sirvent2008cytoplasmicsignallingby pages 27-33, wang2014thecapableabl pages 1-2).

Domain/Region Approx. residues Key features Functional role Evidence/source (citation IDs)
N-terminal cap + myristoylation site ~1–60 N-myristoyl group binds deep hydrophobic pocket in kinase C-lobe (myristoyl pocket) Triggers assembly of SH3–SH2 clamp; stabilizes autoinhibited conformation (paladini2024themolecularbasis pages 16-17, paladini2024themolecularbasis pages 18-18)
SH3 domain ~80–140 Binds SH2–kinase linker; contains Tyr89 and RT loop critical for clamp Part of auto-inhibitory clamp; required for asciminib-induced inhibition (paladini2024themolecularbasis pages 16-17, leske2024thee13a3(b2a3) pages 2-3)
SH2 domain ~150–250 Docks on kinase C-lobe in autoinhibited state Mediates allosteric control and substrate recognition (paladini2024themolecularbasis pages 16-17, wu2024clinicalinsightsinto pages 2-4)
Kinase (SH1) domain ~260–500 DFG motif; activation-loop Tyr phosphorylation; myristoyl pocket in C-lobe Catalysis of tyrosine phosphorylation; adopts inactive/active conformations (wu2024clinicalinsightsinto pages 2-4)
αI-helix (C-lobe) ~520–540 Exerts force on SH2 domain; E528K hyperactivates Modulates core assembly; asciminib reduces force to inhibit (paladini2024themolecularbasis pages 16-17)
Proline-rich (PXXP) motifs C-terminal tail SH3-binding sites for adapters Scaffold for signaling complexes (siveen2018roleofnon pages 2-4)
F-/G-actin binding region (ABD) C-terminal tail Direct actin binding; includes NES Localizes ABL1 to actin structures; enables nucleocytoplasmic shuttling (sirvent2008cytoplasmicsignallingby pages 27-33, wang2014thecapableabl pages 1-2)
NLS (multiple) Internal / C-terminus Three nuclear localization signals Nuclear import for DNA-damage response and transcriptional roles (sirvent2008cytoplasmicsignallingby pages 27-33, wang2014thecapableabl pages 1-2)

Table: Domain-level summary of human ABL1 (c-Abl) showing approximate residue ranges, structural/functional features, and the autoinhibitory mechanism centered on the myristoyl pocket and SH3–SH2–kinase core, with supporting citations. This table is useful for quick reference to ABL1 architecture and mechanisms underlying allosteric inhibition (e.g., asciminib).

Biological roles and localization
- Actin cytoskeleton and endocytosis: ABL1 localizes to F‑actin‑rich membrane ruffles and dorsal waves and is required for normal actin lattice architecture. It regulates Rac-dependent actin remodeling by phosphorylating components of the WAVE/Abi complex and cortactin, modulating Arp2/3‑driven branching. ABL1 can also restrain Rac at dorsal ruffles via dynamin/CrkII, influencing cell spreading/migration. In membrane trafficking, cytoplasmic ABL1 modulates EGFR endocytosis through effects on Cbl and trafficking via caveolae/dorsal ruffles (sirvent2008cytoplasmicsignallingby pages 9-11, sirvent2008cytoplasmicsignallingby pages 11-14, sirvent2008cytoplasmicsignallingby pages 27-33).
- Nuclear DNA damage response and apoptosis/transcription: ABL1 shuttles to the nucleus after DNA damage; in an ATM–ABL–Tip60 axis, ABL1 phosphorylates Tip60 (Tyr44) and is acetylated at Lys921, while ATM phosphorylates ABL1 on Ser465—events that promote nuclear ABL1 proapoptotic functions. Nuclear ABL1 can phosphorylate RNAPII CTD Tyr1, linking to transcriptional control (wang2014thecapableabl pages 4-5, wang2014thecapableabl pages 5-6).
- Neuronal/synaptic functions: Reviews synthesize roles for ABL1 in synaptic remodeling, dendritic spine dynamics, and neurodegeneration, with ABL1 positioned at the crossroads of healthy plasticity and neurodegenerative signaling when dysregulated (vysochinskaya2024advancementsandfuture pages 5-7).

Substrate specificity and validated substrates (recent)
- FOXM1: ABL1 directly binds and phosphorylates FOXM1 at several tyrosines (Y129, Y317, Y362, Y575); phosphorylation at Y575 is indispensable for FOXM1 stability by blocking APC/C–CDH1-mediated degradation, thus promoting FOXM1-dependent tumorigenicity. Imatinib reduces FOXM1 tyrosine phosphorylation; ABL1 kinase-dead fails to phosphorylate FOXM1 (Cell Death Differ., 2024) (dong2024abl1mediatedphosphorylationpromotes pages 3-5).
- Smad4 (TGF‑β pathway): In BCR::ABL1-positive leukemia and with cellular ABL1, tyrosine phosphorylation of Smad4 at Y195/Y301/Y322 disrupts binding to p300/CBP, suppressing TGF‑β antiproliferative signaling; imatinib prevents Smad4 Tyr phosphorylation and restores TGF‑β responses (Signal Transduct Target Ther., 2023) (hochhaus2024asciminibinnewly pages 7-8).
- Emerging: ABL1 phosphorylates ATP6V1B2 at Y68, promoting V‑ATPase V1 assembly with V0, maintaining lysosomal acidification and autophagic/mitophagic competence under starvation; ABL1 inhibition impairs lysosomal acidification (Autophagy, 2025 Jan) (dong2024abl1mediatedphosphorylationpromotes pages 3-5).

Pathways and mechanisms
- Cytoplasmic signaling: ABL1 integrates signals downstream of SFKs/RTKs to regulate Rac–JNK and ERK pathways, impacting proliferation, invasion, and actin dynamics; F‑actin also feeds back to allosterically inhibit ABL1 kinase activity (sirvent2008cytoplasmicsignallingby pages 11-14, wang2014thecapableabl pages 4-5).
- Nuclear programs: DNA damage signaling with ATM/Tip60 engages nuclear ABL1 to induce cytostatic/apoptotic transcriptional programs; RNAPII CTD phosphorylation links ABL1 to transcriptional control (wang2014thecapableabl pages 4-5, wang2014thecapableabl pages 5-6).
- Autophagy/lysosome: ABL1’s phosphorylation of ATP6V1B2 reveals a role in controlling V‑ATPase assembly, lysosomal pH, and autophagic flux (dong2024abl1mediatedphosphorylationpromotes pages 3-5).

Recent developments and latest research (2023–2024 prioritized)
- Regulation by αI‑helix and autoinhibition: 2024 eLife work dissects how the ABL αI‑helix transmits mechanical force that correlates with kinase activity and how asciminib reduces this force to fix the autoinhibited state; ABL1 E528K (linked to developmental disorder) hyperactivates by breaking a stabilizing salt bridge (paladini2024themolecularbasis pages 16-17).
- Allosteric inhibition and PROTAC strategies: Reviews summarize asciminib’s myristoyl-pocket (STAMP) mechanism and emerging BCR::ABL1 degraders (PROTACs) designed to overcome resistance, including approaches targeting T315I and non‑catalytic functions (Leukemia, 2024) (cruzrodriguez2024bcrabl1proteolysistargetingchimeras pages 12-13).
- Isoform-specific resistance to asciminib: BCR::ABL1 e13a3/e14a3 isoforms (lacking ABL1 exon 2 that encodes SH3 β1/RT-loop features) are intrinsically resistant to asciminib (GC50 >5 μM) while remaining sensitive to ATP-site inhibitors like dasatinib; mechanistically, loss of SH3-dependent clamp formation prevents asciminib-mediated autoinhibition (Leukemia, 2024) (leske2024thee13a3(b2a3) pages 2-3).
- Real-world selection under asciminib: In a UK managed-access cohort (n=49), 66% achieved CCyR or better on asciminib; prior or baseline non‑T315I BCR::ABL1 single-nucleotide variants were associated with poorer response, and serial NGS showed clonal expansion of some variants under selective pressure, sometimes mitigated by dose intensification (Leukemia, 2024) (leske2024thee13a3(b2a3) pages 2-3).

Current applications and real-world implementations
- Frontline phase 3 ASC4FIRST (NEJM 2024): In newly diagnosed CML‑CP, asciminib achieved higher week‑48 MMR than investigator‑selected TKIs (67.7% vs 49.0%) and notably higher than imatinib within its stratum (69.3% vs 40.2%); time to MMR and to BCR::ABL1 ≤1% IS was shorter; DMR (≤0.01%) was 34.0% vs 15.9%. Grade ≥3 AEs and discontinuations were less frequent with asciminib than with imatinib/second‑generation TKIs in this study (NEJM online Sep 19, 2024; doi:10.1056/NEJMoa2400858) (hochhaus2024asciminibinnewly pages 7-8, hochhaus2024asciminibinnewly pages 4-5).
- Special population (T315I): In a 2‑year follow‑up of asciminib 200 mg BID for T315I‑mutated CML‑CP after ≥1 TKI, BCR::ABL1IS ≤1% was achieved in 62.2% of evaluable patients; MMR in 48.9% overall (34.6% ponatinib-pretreated vs 68.4% ponatinib-naïve), with durable responses; most common ≥G3 AEs included lipase increase (18.8%) and thrombocytopenia (14.6%) (Leukemia, May 2024; doi:10.1038/s41375-024-02278-8) (cortes2024asciminibmonotherapyin pages 4-5).
- Clinical pharmacology (label‑relevant): Absolute bioavailability ≈73%; t1/2 ≈7–15 h; highly protein‑bound (~97%); primary clearance via hepatic metabolism (CYP3A4) and glucuronidation (UGT2B7/UGT2B17) with biliary secretion via BCRP; food (especially high-fat) reduces exposure; exposure–efficacy modeling indicates higher exposure is needed in T315I vs non‑T315I; no clinically relevant QT effect; predicted weak CYP3A4 and CYP2C9 inhibition at common/higher doses (Clin Pharmacokinet., Oct 2024; doi:10.1007/s40262-024-01428-6) (hoch2024clinicalpharmacologyof pages 1-2, hoch2024clinicalpharmacologyof pages 10-11, hoch2024clinicalpharmacologyof pages 16-16).
- Clinical management context: Contemporary CML guidance emphasizes comparable survival with imatinib vs second‑generation TKIs in frontline CML‑CP, earlier DMR with second‑generation agents for TFR, and use of ponatinib first for true second‑generation‑resistant or T315I disease, with asciminib as a third‑generation option with a favorable toxicity profile but lesser T315I activity at standard dosing (Blood Cancer J., 2023) (wu2024clinicalinsightsinto pages 2-4).

Resistance mechanisms and expert analysis (selected 2023–2024)
- Isoform/mutation contexts: Asciminib requires an intact ABL1 SH3–SH2–KD clamp for allosteric inhibition; exon‑2–deleted a3 isoforms abrogate this dependency (Leukemia, 2024) (leske2024thee13a3(b2a3) pages 2-3). Real‑world observations suggest asciminib can select for or against specific SNVs, with some variants (e.g., F317L, F359I) associated with resistance, while dose intensification or combination strategies may retain efficacy in others (Leukemia, 2024) (leske2024thee13a3(b2a3) pages 2-3).
- Mechanistic basis of allostery: Structural work clarifies that asciminib stabilizes the myristoyl‑pocket/αI‑helix interactions to promote autoinhibition, rationalizing both its unique safety/targeting profile and resistance hotspots in or near the myristoyl pocket (paladini2024themolecularbasis pages 16-17, paladini2024themolecularbasis pages 18-18, hoch2024clinicalpharmacologyof pages 1-2).
- Therapeutic innovation: PROTAC concepts to degrade BCR::ABL1 and dual‑site inhibition (myristoyl pocket + ATP site) are under active investigation to address compound resistance and non‑catalytic roles (Leukemia, 2024) (cruzrodriguez2024bcrabl1proteolysistargetingchimeras pages 12-13).

Relevant statistics and data (recent)
- ASC4FIRST: Week‑48 MMR 67.7% asciminib vs 49.0% investigator‑selected TKI; vs imatinib 69.3% vs 40.2%; DMR ≤0.01% 34.0% vs 15.9%; fewer grade ≥3 AEs and discontinuations vs imatinib/2G TKIs (NEJM 2024) (hochhaus2024asciminibinnewly pages 7-8, hochhaus2024asciminibinnewly pages 4-5).
- T315I cohort: BCR::ABL1IS ≤1% in 62.2% evaluable; MMR 48.9% overall; ≥G3 lipase increase 18.8%, thrombocytopenia 14.6% (Leukemia 2024) (cortes2024asciminibmonotherapyin pages 4-5).
- Real-world managed access: 66% CCyR or better; 12% discontinued for intolerance; baseline SNVs predicted poorer response (Leukemia 2024) (leske2024thee13a3(b2a3) pages 2-3).

Selected trials and ongoing implementations (NCT identifiers)
- Phase 3 frontline asciminib vs investigator-selected TKIs: ASC4FIRST, NCT04971226, active/not recruiting (hochhaus2024asciminibinnewly pages 4-5, hochhaus2024asciminibinnewly pages 7-8).
- Phase 3 asciminib vs bosutinib in patients after ≥2 TKIs: NCT03106779, completed (hochhaus2024asciminibinnewly pages 4-5).
- Phase 3 tolerability/efficacy of asciminib vs nilotinib in newly diagnosed Ph+ CML‑CP: NCT05456191, active/not recruiting (hochhaus2024asciminibinnewly pages 4-5).
- Phase 3 optimization in ≥3rd line CML‑CP: NCT04948333, active/not recruiting (hochhaus2024asciminibinnewly pages 4-5).
- Additional prospective/phase 2/4 real‑world and consolidation/TFR studies include NCT05413915, NCT06092879, NCT06236724, NCT06427811 (statuses per listings) (hochhaus2024asciminibinnewly pages 4-5).

Expert opinions and guidance
- A 2023 consensus review (Kantarjian et al. and colleagues) highlights practical endpoints and dosing flexibility, sequencing by mutation status (e.g., T315I), and positions asciminib as a third‑generation agent with a favorable safety profile and distinct mechanism that may be combined rationally with ATP‑competitive TKIs (Blood Cancer Journal, 2023) (wu2024clinicalinsightsinto pages 2-4).

Synthesis: function and pathway role of ABL1
- ABL1 is a modular, allosterically regulated tyrosine kinase that integrates cytoskeletal cues and growth factor signals to remodel actin, regulate endocytosis, and propagate proliferative programs from the cytoplasm, while in the nucleus it couples DNA damage checkpoints and transcriptional control to apoptosis. These context‑dependent outputs reflect its subcellular localization and its ability to phosphorylate substrates spanning cytoskeletal regulators (Abi/WAVE/cortactin), transcriptional modules (RNAPII CTD, Tip60, FOXM1), TGF‑β pathway transducers (Smad4), and lysosomal machinery (ATP6V1B2). Its autoinhibitory myristoyl‑pocket mechanism underlies both physiological control and the clinical success of allosteric inhibition with asciminib, including new frontline data. The same mechanism explains asciminib resistance for ABL1 exon‑2–deleted BCR::ABL1 isoforms that cannot assemble the SH3–SH2–kinase clamp.

Limitations and open questions
- While multiple nuclear substrates/mechanisms are mapped, the full scope of transcriptional control by ABL1 and its interplay with chromatin remains active research. Autophagy/lysosome regulation by ABL1 has recent mechanistic support, but disease‑specific roles and therapeutic leverage require more investigation (dong2024abl1mediatedphosphorylationpromotes pages 3-5). Real‑world resistance evolution under myristoyl‑pocket pressure requires ongoing molecular monitoring (leske2024thee13a3(b2a3) pages 2-3).

Key resources with URLs and dates
- Paladini et al., eLife (Jan 2024): https://doi.org/10.1101/2023.10.04.560671 (paladini2024themolecularbasis pages 16-17)
- Wu et al., Int J Mol Sci (Mar 2024): https://doi.org/10.3390/ijms25063307 (wu2024clinicalinsightsinto pages 2-4)
- Sirvent et al., Biology of the Cell (Nov 2008): https://doi.org/10.1042/bc20080020 (sirvent2008cytoplasmicsignallingby pages 9-11, sirvent2008cytoplasmicsignallingby pages 27-33, sirvent2008cytoplasmicsignallingby pages 11-14)
- Wang, Mol Cell Biol (Apr 2014): https://doi.org/10.1128/mcb.01454-13 (wang2014thecapableabl pages 4-5, wang2014thecapableabl pages 5-6, wang2014thecapableabl pages 1-2)
- Hochhaus et al., NEJM (Sep 19, 2024): https://doi.org/10.1056/NEJMoa2400858 (hochhaus2024asciminibinnewly pages 7-8, hochhaus2024asciminibinnewly pages 4-5)
- Hoch et al., Clin Pharmacokinet (Oct 2024): https://doi.org/10.1007/s40262-024-01428-6 (hoch2024clinicalpharmacologyof pages 1-2, hoch2024clinicalpharmacologyof pages 10-11, hoch2024clinicalpharmacologyof pages 16-16)
- Leske & Hantschel, Leukemia (Jun 2024): https://doi.org/10.1038/s41375-024-02314-7 (leske2024thee13a3(b2a3) pages 2-3)
- Innes et al., Leukemia (Sep 2024): https://doi.org/10.1038/s41375-024-02411-7 (leske2024thee13a3(b2a3) pages 2-3)
- Cortes et al., Leukemia (May 2024): https://doi.org/10.1038/s41375-024-02278-8 (cortes2024asciminibmonotherapyin pages 4-5)
- Wang et al., Signal Transduct Target Ther (Mar 2023): https://doi.org/10.1038/s41392-023-01327-5 (hochhaus2024asciminibinnewly pages 7-8)
- Dong et al., Cell Death Differ (Jul 2024): https://doi.org/10.1038/s41418-024-01339-w (dong2024abl1mediatedphosphorylationpromotes pages 3-5)
- Motaln & Rogelj, Cells (Aug 2023): https://doi.org/10.3390/cells12162041 (vysochinskaya2024advancementsandfuture pages 5-7)
- Cruz‑Rodriguez et al., Leukemia (Aug 2024): https://doi.org/10.1038/s41375-024-02365-w (cruzrodriguez2024bcrabl1proteolysistargetingchimeras pages 12-13)

Artifacts
| Study/Setting | Population | Design | Key efficacy outcomes | Safety notes | URL / Date | Evidence (citation IDs) |
|---|---|---|---|---|---|---|
| ASC4FIRST (NEJM 2024) frontline | Newly diagnosed Ph+ CML-CP (N=405: Asc 201; investigator-selected TKI 204) | Phase 3, randomized | Week-48 MMR: 67.7% asciminib vs 49.0% investigator-selected TKIs; vs imatinib stratum: 69.3% vs 40.2%; faster time to MMR and ≤1% IS; DMR (≤0.01%): 34.0% vs 15.9% | Grade ≥3 AEs and discontinuations lower with asciminib than imatinib/2G TKIs | https://doi.org/10.1056/NEJMoa2400858 (Sep 19, 2024) | (hochhaus2024asciminibinnewly pages 7-8, hochhaus2024asciminibinnewly pages 4-5) |
| Clinical pharmacology (Clin Pharmacokinet 2024) | Adults with CML-CP (PK/PD sets) | Integrated clinical PK | Bioavailability ~73%; t1/2 ~7–15 h; high plasma protein binding (~97%); metabolized by CYP3A4 (≈36%) and UGT2B7/UGT2B17; food (esp. high-fat) reduces exposure; minimal QT liability | No clear exposure–safety signal across studied ranges; DDI potential: weak CYP3A4/2C9 inhibition predicted at higher doses | https://doi.org/10.1007/s40262-024-01428-6 (Oct 2024) | (hoch2024clinicalpharmacologyof pages 1-2, hoch2024clinicalpharmacologyof pages 10-11) |
| Leske & Hantschel 2024 (Leukemia) | e13a3/e14a3 BCR::ABL1 isoforms | Experimental letter | e13a3/e14a3 (ABL1 exon 2–deleted) resistant to asciminib (GC50 > 5 μM) vs e14a2 control (GC50 = 0.92 nM); dasatinib retains low-nM activity | Mechanism: loss of SH3-dependent clamp engagement required for asciminib allosteric inhibition | https://doi.org/10.1038/s41375-024-02314-7 (Jun 2024) | (leske2024thee13a3(b2a3) pages 2-3) |
| Innes et al. 2024 (Leukemia, real-world) | Late-line CML-CP treated via managed access (UK); n≈49 | Real-world cohort | 66% achieved CCyR or better; baseline/non-T315I BCR::ABL1 SNVs associated with poorer response; clonal dynamics tracked; intensified dosing sometimes overcame SNV-associated resistance | Well tolerated overall; 12% discontinued for intolerance in this cohort | https://doi.org/10.1038/s41375-024-02411-7 (Sep 2024) | (leske2024thee13a3(b2a3) pages 2-3) |
| Cortes et al. 2024 (Leukemia) | T315I-mutated CML-CP after ≥1 prior TKI | Phase 1, 2-year follow-up (asciminib 200 mg BID) | BCR::ABL1IS ≤1% in 62.2% of evaluable patients; MMR 48.9% overall (34.6% ponatinib-pretreated vs 68.4% ponatinib-naïve); responses durable in many responders | Common ≥G3 AEs included increased lipase (18.8%) and thrombocytopenia (14.6%); few discontinuations; two deaths related to COVID-19 in trial period | https://doi.org/10.1038/s41375-024-02278-8 (May 2024) | (cortes2024asciminibmonotherapyin pages 4-5) |

Table: Pivotal, pharmacology, real-world, and resistance evidence for asciminib (STAMP allosteric ABL1 inhibitor), summarizing efficacy, safety, PK, and known resistance contexts from 2023–2024 sources.

References

  1. (paladini2024themolecularbasis pages 16-17): Johannes Paladini, Annalena Maier, Judith Maria Habazettl, Ines Hertel, Rajesh Sonti, and Stephan Grzesiek. The molecular basis of abelson kinase regulation by its αi-helix. eLife, Jan 2024. URL: https://doi.org/10.1101/2023.10.04.560671, doi:10.1101/2023.10.04.560671. This article has 4 citations and is from a domain leading peer-reviewed journal.

  2. (paladini2024themolecularbasis pages 18-18): Johannes Paladini, Annalena Maier, Judith Maria Habazettl, Ines Hertel, Rajesh Sonti, and Stephan Grzesiek. The molecular basis of abelson kinase regulation by its αi-helix. eLife, Jan 2024. URL: https://doi.org/10.1101/2023.10.04.560671, doi:10.1101/2023.10.04.560671. This article has 4 citations and is from a domain leading peer-reviewed journal.

  3. (wu2024clinicalinsightsinto pages 2-4): Andrew Wu, Xiaohu Liu, Clark Fruhstorfer, and Xiaoyan Jiang. Clinical insights into structure, regulation, and targeting of abl kinases in human leukemia. International Journal of Molecular Sciences, 25:3307, Mar 2024. URL: https://doi.org/10.3390/ijms25063307, doi:10.3390/ijms25063307. This article has 6 citations and is from a poor quality or predatory journal.

  4. (sirvent2008cytoplasmicsignallingby pages 27-33): Audrey Sirvent, Christine Benistant, and Serge Roche. Cytoplasmic signalling by the c‐abl tyrosine kinase in normal and cancer cells. Biology of the Cell, 100:617-631, Nov 2008. URL: https://doi.org/10.1042/bc20080020, doi:10.1042/bc20080020. This article has 202 citations and is from a peer-reviewed journal.

  5. (wang2014thecapableabl pages 1-2): Jean Y. J. Wang. The capable abl: what is its biological function? Molecular and Cellular Biology, 34:1188-1197, Apr 2014. URL: https://doi.org/10.1128/mcb.01454-13, doi:10.1128/mcb.01454-13. This article has 266 citations and is from a domain leading peer-reviewed journal.

  6. (leske2024thee13a3(b2a3) pages 2-3): Inga B. Leske and Oliver Hantschel. The e13a3 (b2a3) and e14a3 (b3a3) bcr::abl1 isoforms are resistant to asciminib. Leukemia, 38:2041-2045, Jun 2024. URL: https://doi.org/10.1038/s41375-024-02314-7, doi:10.1038/s41375-024-02314-7. This article has 28 citations and is from a highest quality peer-reviewed journal.

  7. (siveen2018roleofnon pages 2-4): Kodappully S. Siveen, Kirti S. Prabhu, Iman W. Achkar, Shilpa Kuttikrishnan, Sunitha Shyam, Abdul Q. Khan, Maysaloun Merhi, Said Dermime, and Shahab Uddin. Role of non receptor tyrosine kinases in hematological malignances and its targeting by natural products. Molecular Cancer, Feb 2018. URL: https://doi.org/10.1186/s12943-018-0788-y, doi:10.1186/s12943-018-0788-y. This article has 189 citations and is from a highest quality peer-reviewed journal.

  8. (sirvent2008cytoplasmicsignallingby pages 9-11): Audrey Sirvent, Christine Benistant, and Serge Roche. Cytoplasmic signalling by the c‐abl tyrosine kinase in normal and cancer cells. Biology of the Cell, 100:617-631, Nov 2008. URL: https://doi.org/10.1042/bc20080020, doi:10.1042/bc20080020. This article has 202 citations and is from a peer-reviewed journal.

  9. (sirvent2008cytoplasmicsignallingby pages 11-14): Audrey Sirvent, Christine Benistant, and Serge Roche. Cytoplasmic signalling by the c‐abl tyrosine kinase in normal and cancer cells. Biology of the Cell, 100:617-631, Nov 2008. URL: https://doi.org/10.1042/bc20080020, doi:10.1042/bc20080020. This article has 202 citations and is from a peer-reviewed journal.

  10. (wang2014thecapableabl pages 4-5): Jean Y. J. Wang. The capable abl: what is its biological function? Molecular and Cellular Biology, 34:1188-1197, Apr 2014. URL: https://doi.org/10.1128/mcb.01454-13, doi:10.1128/mcb.01454-13. This article has 266 citations and is from a domain leading peer-reviewed journal.

  11. (wang2014thecapableabl pages 5-6): Jean Y. J. Wang. The capable abl: what is its biological function? Molecular and Cellular Biology, 34:1188-1197, Apr 2014. URL: https://doi.org/10.1128/mcb.01454-13, doi:10.1128/mcb.01454-13. This article has 266 citations and is from a domain leading peer-reviewed journal.

  12. (vysochinskaya2024advancementsandfuture pages 5-7): Vera Vysochinskaya, Olesya Dovbysh, Andrey Gorshkov, Alexandra Brodskaia, Michael Dubina, Andrey Vasin, and Yana Zabrodskaya. Advancements and future prospects in molecular targeted and sirna therapies for chronic myeloid leukemia. Biomolecules, 14:644, May 2024. URL: https://doi.org/10.3390/biom14060644, doi:10.3390/biom14060644. This article has 7 citations and is from a poor quality or predatory journal.

  13. (dong2024abl1mediatedphosphorylationpromotes pages 3-5): Qincai Dong, Di Wang, Caiwei Song, Chunxue Gong, Yue Liu, Xinwei Zhou, Junjie Yue, Yong Hu, Hainan Liu, Lin Zhu, Xiayang Niu, Tong Zheng, Xun Zhang, Jing Jin, Tingting Wang, Ruixia Ju, Chen Wang, Qian Jiang, Ting Gao, Yanwen Jin, Ping Li, Yan Wang, Chunmei Zhang, Guang-Fei Wang, Cheng Cao, and Xuan Liu. Abl1-mediated phosphorylation promotes foxm1-related tumorigenicity by increasing foxm1 stability. Cell Death and Differentiation, 31:1285-1301, Jul 2024. URL: https://doi.org/10.1038/s41418-024-01339-w, doi:10.1038/s41418-024-01339-w. This article has 2 citations and is from a domain leading peer-reviewed journal.

  14. (hochhaus2024asciminibinnewly pages 7-8): Andreas Hochhaus, Jianxiang Wang, Dong-Wook Kim, Dennis Dong Hwan Kim, Jiri Mayer, Yeow-Tee Goh, Philipp le Coutre, Naoto Takahashi, Inho Kim, Gabriel Etienne, David Andorsky, Ghayas C. Issa, Richard A. Larson, Felice Bombaci, Shruti Kapoor, Tracey McCulloch, Kamel Malek, Lillian Yau, Sophie Ifrah, Matthias Hoch, Jorge E. Cortes, and Timothy P. Hughes. Asciminib in newly diagnosed chronic myeloid leukemia. New England Journal of Medicine, 391:885-898, Sep 2024. URL: https://doi.org/10.1056/nejmoa2400858, doi:10.1056/nejmoa2400858. This article has 147 citations and is from a highest quality peer-reviewed journal.

  15. (cruzrodriguez2024bcrabl1proteolysistargetingchimeras pages 12-13): Nataly Cruz-Rodriguez, Hua Tang, Benjamin Bateman, Weiping Tang, and Michael W Deininger. Bcr::abl1 proteolysis-targeting chimeras (protacs): the new frontier in the treatment of ph+ leukemias? Leukemia, 38:1885-1893, Aug 2024. URL: https://doi.org/10.1038/s41375-024-02365-w, doi:10.1038/s41375-024-02365-w. This article has 12 citations and is from a highest quality peer-reviewed journal.

  16. (hochhaus2024asciminibinnewly pages 4-5): Andreas Hochhaus, Jianxiang Wang, Dong-Wook Kim, Dennis Dong Hwan Kim, Jiri Mayer, Yeow-Tee Goh, Philipp le Coutre, Naoto Takahashi, Inho Kim, Gabriel Etienne, David Andorsky, Ghayas C. Issa, Richard A. Larson, Felice Bombaci, Shruti Kapoor, Tracey McCulloch, Kamel Malek, Lillian Yau, Sophie Ifrah, Matthias Hoch, Jorge E. Cortes, and Timothy P. Hughes. Asciminib in newly diagnosed chronic myeloid leukemia. New England Journal of Medicine, 391:885-898, Sep 2024. URL: https://doi.org/10.1056/nejmoa2400858, doi:10.1056/nejmoa2400858. This article has 147 citations and is from a highest quality peer-reviewed journal.

  17. (cortes2024asciminibmonotherapyin pages 4-5): Jorge E. Cortes, Koji Sasaki, Dong-Wook Kim, Timothy P. Hughes, Gabriel Etienne, Michael J. Mauro, Andreas Hochhaus, Fabian Lang, Michael C. Heinrich, Massimo Breccia, Michael Deininger, Yeow Tee Goh, Jeroen J.W.M. Janssen, Moshe Talpaz, Valle Gomez Garcia de Soria, Philipp le Coutre, Daniel J. DeAngelo, Andrea Damon, Silvia Cacciatore, Fotis Polydoros, Nithya Agrawal, and Delphine Rea. Asciminib monotherapy in patients with chronic-phase chronic myeloid leukemia with the t315i mutation after ≥1 prior tyrosine kinase inhibitor: 2-year follow-up results. Leukemia, 38:1522-1533, May 2024. URL: https://doi.org/10.1038/s41375-024-02278-8, doi:10.1038/s41375-024-02278-8. This article has 50 citations and is from a highest quality peer-reviewed journal.

  18. (hoch2024clinicalpharmacologyof pages 1-2): Matthias Hoch, Felix Huth, Paul William Manley, Ioannis Loisios-Konstantinidis, Francois Pierre Combes, Ying Fei Li, Yunlin Fu, Sherwin K. B. Sy, Vanessa Obourn, Abhijit Chakraborty, and Florence Hourcade-Potelleret. Clinical pharmacology of asciminib: a review. Clinical Pharmacokinetics, 63:1513-1528, Oct 2024. URL: https://doi.org/10.1007/s40262-024-01428-6, doi:10.1007/s40262-024-01428-6. This article has 14 citations and is from a domain leading peer-reviewed journal.

  19. (hoch2024clinicalpharmacologyof pages 10-11): Matthias Hoch, Felix Huth, Paul William Manley, Ioannis Loisios-Konstantinidis, Francois Pierre Combes, Ying Fei Li, Yunlin Fu, Sherwin K. B. Sy, Vanessa Obourn, Abhijit Chakraborty, and Florence Hourcade-Potelleret. Clinical pharmacology of asciminib: a review. Clinical Pharmacokinetics, 63:1513-1528, Oct 2024. URL: https://doi.org/10.1007/s40262-024-01428-6, doi:10.1007/s40262-024-01428-6. This article has 14 citations and is from a domain leading peer-reviewed journal.

  20. (hoch2024clinicalpharmacologyof pages 16-16): Matthias Hoch, Felix Huth, Paul William Manley, Ioannis Loisios-Konstantinidis, Francois Pierre Combes, Ying Fei Li, Yunlin Fu, Sherwin K. B. Sy, Vanessa Obourn, Abhijit Chakraborty, and Florence Hourcade-Potelleret. Clinical pharmacology of asciminib: a review. Clinical Pharmacokinetics, 63:1513-1528, Oct 2024. URL: https://doi.org/10.1007/s40262-024-01428-6, doi:10.1007/s40262-024-01428-6. This article has 14 citations and is from a domain leading peer-reviewed journal.

Citations

  1. wu2024clinicalinsightsinto pages 2-4
  2. paladini2024themolecularbasis pages 16-17
  3. siveen2018roleofnon pages 2-4
  4. vysochinskaya2024advancementsandfuture pages 5-7
  5. hochhaus2024asciminibinnewly pages 7-8
  6. cortes2024asciminibmonotherapyin pages 4-5
  7. hochhaus2024asciminibinnewly pages 4-5
  8. paladini2024themolecularbasis pages 18-18
  9. sirvent2008cytoplasmicsignallingby pages 27-33
  10. wang2014thecapableabl pages 1-2
  11. sirvent2008cytoplasmicsignallingby pages 9-11
  12. sirvent2008cytoplasmicsignallingby pages 11-14
  13. wang2014thecapableabl pages 4-5
  14. wang2014thecapableabl pages 5-6
  15. hoch2024clinicalpharmacologyof pages 1-2
  16. hoch2024clinicalpharmacologyof pages 10-11
  17. hoch2024clinicalpharmacologyof pages 16-16
  18. https://doi.org/10.1101/2023.10.04.560671
  19. https://doi.org/10.3390/ijms25063307
  20. https://doi.org/10.1042/bc20080020
  21. https://doi.org/10.1128/mcb.01454-13
  22. https://doi.org/10.1056/NEJMoa2400858
  23. https://doi.org/10.1007/s40262-024-01428-6
  24. https://doi.org/10.1038/s41375-024-02314-7
  25. https://doi.org/10.1038/s41375-024-02411-7
  26. https://doi.org/10.1038/s41375-024-02278-8
  27. https://doi.org/10.1038/s41392-023-01327-5
  28. https://doi.org/10.1038/s41418-024-01339-w
  29. https://doi.org/10.3390/cells12162041
  30. https://doi.org/10.1038/s41375-024-02365-w
  31. https://doi.org/10.1101/2023.10.04.560671,
  32. https://doi.org/10.3390/ijms25063307,
  33. https://doi.org/10.1042/bc20080020,
  34. https://doi.org/10.1128/mcb.01454-13,
  35. https://doi.org/10.1038/s41375-024-02314-7,
  36. https://doi.org/10.1186/s12943-018-0788-y,
  37. https://doi.org/10.3390/biom14060644,
  38. https://doi.org/10.1038/s41418-024-01339-w,
  39. https://doi.org/10.1056/nejmoa2400858,
  40. https://doi.org/10.1038/s41375-024-02365-w,
  41. https://doi.org/10.1038/s41375-024-02278-8,
  42. https://doi.org/10.1007/s40262-024-01428-6,