The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The UniProt accession P47196 corresponds to RAC-alpha serine/threonine-protein kinase (Akt-1 / PKBα) in Rattus norvegicus (rat). A rat in vivo study explicitly states that the 3D structure of rat Akt-1 was retrieved from UniProt as “UniProt ID: P47196”, which directly validates the accession→protein→organism mapping for this report. Publication: Alwaili et al., 2024-12 (Frontiers in Molecular Biosciences), https://doi.org/10.3389/fmolb.2024.1507786 (alwaili2024avenanthramidecamelioratedoxorubicininduced pages 2-3).
AKT1 (Protein kinase B alpha; PKBα) is a serine/threonine protein kinase in the AGC kinase family that functions as a central signaling node downstream of growth factor/insulin pathways, regulating survival, growth, metabolism, and cytoskeletal programs by phosphorylating protein substrates. (hassan2024aktkinasesas pages 2-3).
Canonical AKT proteins (including AKT1) share:
- an N-terminal pleckstrin homology (PH) domain that binds phosphoinositides,
- a central protein kinase catalytic domain, and
- a C-terminal regulatory tail containing a hydrophobic motif (HM) with a key regulatory serine. (chu2018aktkinaseactivation pages 1-3, yudushkin2020controlofakt pages 1-2, hassan2024aktkinasesas pages 2-3).
AKT1 catalyzes ATP-dependent phosphorylation of serine/threonine residues in protein substrates (EC 2.7.11.1, protein-serine/threonine kinase). Functional substrate examples frequently used for mechanistic assays include GSK3 and FOXO transcription factors. (chu2018aktkinaseactivation pages 1-3, hassan2024aktkinasesas pages 2-3).
A widely supported mechanistic model is that AKT1 activity is controlled by:
- membrane recruitment via the PH domain binding PI(3,4,5)P3 (PIP3) and/or PI(3,4)P2, generated downstream of PI3K, and
- multisite phosphorylation, especially:
- Thr308 in the activation loop phosphorylated by PDK1, and
- Ser473 in the hydrophobic motif phosphorylated largely by mTORC2.
This dual control produces strong spatiotemporal gating (activity restricted to appropriate lipid membranes) and high pathway specificity. (hassan2024aktkinasesas pages 2-3, chu2018aktkinaseactivation pages 1-3, shaw2025molecularinsighton pages 4-5).
A key concept for functional annotation is that AKT1 is autoinhibited in unstimulated conditions by an intramolecular PH–kinase domain interface that buries the PH domain lipid-binding site and masks the kinase domain in a way that is incompatible with full activation. Structural work shows that phosphorylation alone does not fully override this autoinhibition; productive activation requires membrane phosphoinositide engagement. (truebestein2021structureofautoinhibited pages 1-2, truebestein2021structureofautoinhibited pages 3-4).
Figure evidence: Cropped figures from the PNAS structural paper illustrate the autoinhibited AKT1 structure and an activation schematic linking lipid binding and phosphorylation events. (truebestein2021structureofautoinhibited media b1c9177b, truebestein2021structureofautoinhibited media 8a846e33).
AKT1 sits in the canonical PI3K→AKT→mTOR axis. PI3K generates PIP3 from PI(4,5)P2, recruiting AKT to membranes; PDK1 and mTORC2 then phosphorylate AKT at Thr308 and Ser473, respectively, to yield full catalytic competence. (hassan2024aktkinasesas pages 2-3, chu2026structuralandmechanistic pages 6-7).
At the biochemical level, activated AKT1 phosphorylates multiple substrates to bias cells toward anabolic/survival states; mechanistic studies specifically cite increased phosphorylation activity toward substrates such as GSK3 and FOXO1/3a upon Thr308/Ser473 phosphorylation and membrane engagement. (chu2018aktkinaseactivation pages 1-3, chu2026structuralandmechanistic pages 3-4).
AKT signaling is terminated by:
- PTEN, which removes the membrane recruitment signal by converting PIP3 back to PI(4,5)P2, preventing AKT membrane recruitment; and
- protein phosphatases such as PP2A and PHLPP, which dephosphorylate AKT regulatory sites. Because phosphorylation state is stabilized by membrane association, AKT membrane dissociation is tightly coupled to dephosphorylation and inactivation. (chu2026structuralandmechanistic pages 3-4, yudushkin2020controlofakt pages 5-7, chu2026structuralandmechanistic pages 4-5).
In quiescent cells, AKT is described as present in cytosol and nucleus, while growth factor stimulation triggers PH-domain-dependent recruitment to membranes enriched for PIP3/PI(3,4)P2. A key modern view is an “allosteric lipid switch” in which catalysis in cells is strongly constrained to phosphoinositide-containing membranes, even when phosphorylation is present. (yudushkin2020controlofakt pages 5-7, yudushkin2020controlofakt pages 2-4).
Compartmental signaling can be shaped by lipid identity and lifetime:
- PIP3 is associated with acute recruitment of Akt1/3 to plasma membrane,
- PI(3,4)P2 can support sustained signaling at plasma membrane and early endosomes in some models.
Additionally, phosphatase access and membrane dissociation kinetics govern how long AKT remains active. (yudushkin2020controlofakt pages 5-7).
A 2024 expert review emphasizes that AKT inhibitors fall into multiple mechanistic classes (ATP-competitive, allosteric/PH-domain, PIP3 analogues, covalent-allosteric concepts), and highlights increasing interest in isoform-centric and allele-selective strategies (e.g., AKT1 E17K and other activating variants) to improve therapeutic index compared with pan-AKT blockade. Publication: Hassan et al., 2024-11, https://doi.org/10.1186/s13046-024-03207-4 (hassan2024aktkinasesas pages 13-14, hassan2024aktkinasesas pages 14-16).
A 2024 resistance-focused review underscores that many AKT inhibitors faced limitations from dose-limiting toxicity and adaptive resistance, reinforcing biomarker selection and combination regimens as key design features in current practice. Publication: Browne & Okines, 2024-06, https://doi.org/10.3390/cancers16122259 (browne2024resistancetotargeted pages 4-6).
In a 2023 TNBC brain-metastasis model, CRISPR AKT1 knockout produced mixed phenotypes (reduced viability in one clone, but increased migration/clonogenic survival and decreased radiosensitivity in both KO clones), illustrating that AKT1’s role can be context-specific and that isoform-specific perturbation does not necessarily phenocopy pharmacologic pan-AKT inhibition. Publication: Kempska et al., 2023-07, https://doi.org/10.3389/fonc.2023.1129682 (kempska2023impactofakt1 pages 1-2).
Clinical translation of AKT inhibition is exemplified by capivasertib (ATP-competitive pan-AKT inhibitor) combined with endocrine therapy.
These outcomes are widely cited as pivotal for the clinical role of AKT inhibitors in biomarker-defined HR+/HER2− breast cancer. (browne2024resistancetotargeted pages 4-6, alves2023druggingthepi3kaktmtor pages 1-2).
CAPItello-291 registry record:
- Trial: NCT04305496 (AstraZeneca), phase 3, randomized, double-blind capivasertib + fulvestrant vs placebo + fulvestrant; enrollment 818.
- Dosing in the registry: capivasertib 400 mg BID on intermittent schedule (Days 1–4 weekly in 28-day cycle) + fulvestrant 500 mg IM with loading then q28 days.
- Primary endpoint includes PFS (RECIST 1.1) in overall and “Altered Population”.
URL: https://clinicaltrials.gov/study/NCT04305496 (NCT04305496 chunk 1).
Implementation-oriented phase III study using historical control:
- Trial: NCT07281833 (CAPIcorn, West German Study Group), phase 3, open-label; plans to screen ~600 and enroll 250 enriched for PIK3CA/AKT1/PTEN alterations.
- Includes patient-reported outcome (PRO) adherence endpoints (digital monitoring) in addition to clinical outcomes.
URL: https://clinicaltrials.gov/study/NCT07281833 (NCT07281833 chunk 1).
A 2024 rat hepatotoxicity study used the rat AKT1 (P47196) structure as an explicit computational target for docking analyses in a therapeutic modulation context (doxorubicin hepatotoxicity; AKT/GSK-3β axis). While not definitive mechanistic biology for AKT1 function per se, it is a concrete example of real-world use of the specific rat protein identifier in applied research workflows. (alwaili2024avenanthramidecamelioratedoxorubicininduced pages 2-3).
The following table provides a compact functional-annotation summary for rat AKT1 (P47196) with citations.
| Annotation topic | Summary for rat AKT1 (UniProt P47196) | Key evidence |
|---|---|---|
| Identity verification | The target matches Rattus norvegicus Akt1, encoding RAC-alpha serine/threonine-protein kinase / PKBα. A 2024 rat study explicitly states that the Rattus norvegicus Akt-1 structure used for docking was retrieved from UniProt as P47196, confirming the accession-gene-organism mapping. Core AKT1 architecture and regulation are consistent with canonical mammalian AKT1/PKBα literature. | (alwaili2024avenanthramidecamelioratedoxorubicininduced pages 2-3, hassan2024aktkinasesas pages 2-3) |
| Domains | AKT1 has the canonical AKT layout: N-terminal PH domain, central bilobal kinase domain, and C-terminal hydrophobic/regulatory tail (hydrophobic motif). This organization underlies phosphoinositide sensing, catalytic phosphorylation, and C-tail-dependent regulation. | (chu2018aktkinaseactivation pages 1-3, yudushkin2020controlofakt pages 1-2, hassan2024aktkinasesas pages 2-3) |
| Catalytic activity (EC 2.7.11.1) | AKT1 is an AGC-family serine/threonine protein kinase that transfers phosphate from ATP to Ser/Thr residues on protein substrates. Its kinase activity is central to growth, survival, metabolism, and anabolic signaling. Representative downstream substrates include GSK3 and FOXO proteins. | (hassan2024aktkinasesas pages 2-3, chu2018aktkinaseactivation pages 1-3, yudushkin2020controlofakt pages 2-4) |
| Activation mechanism | Activation is membrane- and phosphorylation-coupled. The PH domain binds PI(3,4,5)P3 (PIP3) and PI(3,4)P2, recruiting AKT1 to phosphoinositide-enriched membranes. PDK1 phosphorylates Thr308 in the activation loop for partial activation; mTORC2 phosphorylates Ser473 in the hydrophobic motif for full activation/substrate tuning. Thr450 turn-motif phosphorylation contributes to folding/stability. | (hassan2024aktkinasesas pages 2-3, chu2026structuralandmechanistic pages 6-7, shaw2025molecularinsighton pages 4-5) |
| Autoinhibition | In unstimulated cells, AKT1 adopts a PH-in autoinhibited conformation in which a PH–kinase domain interface masks the active state and sequesters the lipid-binding site. Structural work showed that phosphorylation alone does not fully relieve this state; productive activation requires both phosphoinositide binding and regulatory phosphorylation. | (truebestein2021structureofautoinhibited pages 1-2, truebestein2021structureofautoinhibited pages 3-4, yudushkin2020controlofakt pages 1-2) |
| Localization / compartments | AKT1 is largely cytosolic (and can be nuclear) in quiescent cells, but active signaling is concentrated at membrane-associated compartments, especially the plasma membrane and, in some models, endosomal membranes. Lipid identity helps specify compartmental signaling, and dissociation from membranes promotes rapid inactivation. | (yudushkin2020controlofakt pages 5-7, chu2026structuralandmechanistic pages 4-5, truebestein2021structureofautoinhibited pages 1-2) |
| Termination / negative regulation | AKT signaling is terminated at two levels: PTEN removes the lipid signal by dephosphorylating PIP3 to PI(4,5)P2, preventing membrane recruitment; PP2A and PHLPP dephosphorylate AKT at key regulatory residues, especially after membrane dissociation. This couples localization, phosphorylation state, and signaling duration. | (chu2026structuralandmechanistic pages 3-4, yudushkin2020controlofakt pages 5-7, chu2026structuralandmechanistic pages 4-5) |
| Representative substrates / pathway effects | Activated AKT1 phosphorylates substrates including GSK3 and FOXO1/3a, thereby promoting cell survival, proliferation, metabolism, and anabolic growth programs. Phosphorylation state, especially the Thr308/Ser473 balance, can influence substrate preference and signaling output. | (chu2018aktkinaseactivation pages 1-3, chu2026structuralandmechanistic pages 3-4, hassan2024aktkinasesas pages 2-3) |
| 2023–2024 clinical translation | A major recent milestone was capivasertib clinical translation. In CAPItello-291, capivasertib + fulvestrant improved median PFS from 3.6 to 7.2 months overall (HR 0.60) and from 3.1 to 7.3 months in pathway-altered tumors; reviews note FDA approval in HR+/HER2− advanced breast cancer with PIK3CA/AKT/PTEN alterations. Earlier supportive phase II data (FAKTION) showed PFS 10.3 vs 4.8 months and OS 29.3 vs 23.4 months. | (browne2024resistancetotargeted pages 4-6, alves2023druggingthepi3kaktmtor pages 1-2) |
| Clinical trial registry implementation | NCT04305496 (CAPItello-291): phase III, randomized, double-blind capivasertib + fulvestrant vs placebo + fulvestrant; enrollment 818; capivasertib 400 mg BID, 4 days on/3 days off; primary endpoint PFS in overall and altered populations. NCT07281833 (CAPIcorn): phase III implementation-oriented study; plans to screen ~600 and enroll 250, enriching for PIK3CA/AKT1/PTEN alterations; evaluates treatment plus patient-reported-outcome adherence metrics. | (NCT04305496 chunk 1, NCT07281833 chunk 1, NCT04305496 chunk 6) |
| 2023 AKT1-specific experimental study | In a 2023 TNBC brain-metastasis model, ipatasertib reduced viability and radiosensitized MDA-MB-231BR cells, but AKT1 knockout showed mixed/complex isoform-specific biology: reduced viability in one clone yet increased migration and clonogenic survival in both KO clones with decreased radiosensitivity, highlighting that AKT1 loss is not functionally equivalent to pan-AKT inhibition. The paper notes PI3K/AKT pathway activation in 43–70% of breast cancers. | (kempska2023impactofakt1 pages 1-2) |
Table: This table summarizes verified identity, molecular function, regulation, localization, and recent translational evidence for rat AKT1/PKBα (UniProt P47196). It is designed as a compact functional-annotation reference with citations to the available evidence contexts.
References
(alwaili2024avenanthramidecamelioratedoxorubicininduced pages 2-3): Maha Abdullah Alwaili, Amal S. Abu-Almakarem, Salwa Aljohani, Sahar Abdulrahman Alkhodair, Maha M. Al-Bazi, Thamir M. Eid, Jehan Alamri, Maysa A. Mobasher, Norah K. Algarza, Arwa Ishaq A. Khayyat, Luluah Saleh Alshaygy, and Karim Samy El-Said. Avenanthramide-c ameliorate doxorubicin-induced hepatotoxicity via modulating akt/gsk-3β and wnt-4/β-catenin pathways in male rats. Frontiers in Molecular Biosciences, Dec 2024. URL: https://doi.org/10.3389/fmolb.2024.1507786, doi:10.3389/fmolb.2024.1507786. This article has 9 citations.
(hassan2024aktkinasesas pages 2-3): Dalal Hassan, Craig W. Menges, Joseph R Testa, and Alfonso Bellacosa. Akt kinases as therapeutic targets. Journal of Experimental & Clinical Cancer Research : CR, Nov 2024. URL: https://doi.org/10.1186/s13046-024-03207-4, doi:10.1186/s13046-024-03207-4. This article has 62 citations.
(chu2018aktkinaseactivation pages 1-3): Nam Chu, Nam Chu, Nam Chu, Antonieta L. Salguero, Antonieta L. Salguero, Antonieta L. Salguero, Albert Z. Liu, Zan Chen, Daniel R. Dempsey, Daniel R. Dempsey, Daniel R. Dempsey, S. Ficarro, William M. Alexander, J. Marto, J. Marto, Yana Li, L. Amzel, S. Gabelli, and P. Cole. Akt kinase activation mechanisms revealed using protein semisynthesis. Cell, 174:897-907.e14, Aug 2018. URL: https://doi.org/10.1016/j.cell.2018.07.003, doi:10.1016/j.cell.2018.07.003. This article has 173 citations and is from a highest quality peer-reviewed journal.
(yudushkin2020controlofakt pages 1-2): Ivan Yudushkin. Control of akt activity and substrate phosphorylation in cells. Iubmb Life, 72:1115-1125, Mar 2020. URL: https://doi.org/10.1002/iub.2264, doi:10.1002/iub.2264. This article has 64 citations and is from a peer-reviewed journal.
(shaw2025molecularinsighton pages 4-5): Alexandria L. Shaw and John E. Burke. Molecular insight on the role of the phosphoinositide pip3 in regulating the protein kinases akt, pdk1, and btk. Biochemical Society Transactions, Jul 2025. URL: https://doi.org/10.1042/bst20253059, doi:10.1042/bst20253059. This article has 17 citations and is from a peer-reviewed journal.
(truebestein2021structureofautoinhibited pages 1-2): Linda Truebestein, Harald Hornegger, Dorothea Anrather, Markus Hartl, Kaelin D. Fleming, Jordan T. B. Stariha, Els Pardon, Jan Steyaert, John E. Burke, and Thomas A. Leonard. Structure of autoinhibited akt1 reveals mechanism of pip3-mediated activation. Proceedings of the National Academy of Sciences of the United States of America, Aug 2021. URL: https://doi.org/10.1073/pnas.2101496118, doi:10.1073/pnas.2101496118. This article has 106 citations and is from a highest quality peer-reviewed journal.
(truebestein2021structureofautoinhibited pages 3-4): Linda Truebestein, Harald Hornegger, Dorothea Anrather, Markus Hartl, Kaelin D. Fleming, Jordan T. B. Stariha, Els Pardon, Jan Steyaert, John E. Burke, and Thomas A. Leonard. Structure of autoinhibited akt1 reveals mechanism of pip3-mediated activation. Proceedings of the National Academy of Sciences of the United States of America, Aug 2021. URL: https://doi.org/10.1073/pnas.2101496118, doi:10.1073/pnas.2101496118. This article has 106 citations and is from a highest quality peer-reviewed journal.
(truebestein2021structureofautoinhibited media b1c9177b): Linda Truebestein, Harald Hornegger, Dorothea Anrather, Markus Hartl, Kaelin D. Fleming, Jordan T. B. Stariha, Els Pardon, Jan Steyaert, John E. Burke, and Thomas A. Leonard. Structure of autoinhibited akt1 reveals mechanism of pip3-mediated activation. Proceedings of the National Academy of Sciences of the United States of America, Aug 2021. URL: https://doi.org/10.1073/pnas.2101496118, doi:10.1073/pnas.2101496118. This article has 106 citations and is from a highest quality peer-reviewed journal.
(truebestein2021structureofautoinhibited media 8a846e33): Linda Truebestein, Harald Hornegger, Dorothea Anrather, Markus Hartl, Kaelin D. Fleming, Jordan T. B. Stariha, Els Pardon, Jan Steyaert, John E. Burke, and Thomas A. Leonard. Structure of autoinhibited akt1 reveals mechanism of pip3-mediated activation. Proceedings of the National Academy of Sciences of the United States of America, Aug 2021. URL: https://doi.org/10.1073/pnas.2101496118, doi:10.1073/pnas.2101496118. This article has 106 citations and is from a highest quality peer-reviewed journal.
(chu2026structuralandmechanistic pages 6-7): Nam Chu, Nhat Le, Ouada Nebie, and Sammi Yang. Structural and mechanistic basis of mtorc2 activation of protein kinase akt/pkb. Biochemical Journal, 483:375-389, Mar 2026. URL: https://doi.org/10.1042/bcj20253108, doi:10.1042/bcj20253108. This article has 1 citations and is from a domain leading peer-reviewed journal.
(chu2026structuralandmechanistic pages 3-4): Nam Chu, Nhat Le, Ouada Nebie, and Sammi Yang. Structural and mechanistic basis of mtorc2 activation of protein kinase akt/pkb. Biochemical Journal, 483:375-389, Mar 2026. URL: https://doi.org/10.1042/bcj20253108, doi:10.1042/bcj20253108. This article has 1 citations and is from a domain leading peer-reviewed journal.
(yudushkin2020controlofakt pages 5-7): Ivan Yudushkin. Control of akt activity and substrate phosphorylation in cells. Iubmb Life, 72:1115-1125, Mar 2020. URL: https://doi.org/10.1002/iub.2264, doi:10.1002/iub.2264. This article has 64 citations and is from a peer-reviewed journal.
(chu2026structuralandmechanistic pages 4-5): Nam Chu, Nhat Le, Ouada Nebie, and Sammi Yang. Structural and mechanistic basis of mtorc2 activation of protein kinase akt/pkb. Biochemical Journal, 483:375-389, Mar 2026. URL: https://doi.org/10.1042/bcj20253108, doi:10.1042/bcj20253108. This article has 1 citations and is from a domain leading peer-reviewed journal.
(yudushkin2020controlofakt pages 2-4): Ivan Yudushkin. Control of akt activity and substrate phosphorylation in cells. Iubmb Life, 72:1115-1125, Mar 2020. URL: https://doi.org/10.1002/iub.2264, doi:10.1002/iub.2264. This article has 64 citations and is from a peer-reviewed journal.
(hassan2024aktkinasesas pages 13-14): Dalal Hassan, Craig W. Menges, Joseph R Testa, and Alfonso Bellacosa. Akt kinases as therapeutic targets. Journal of Experimental & Clinical Cancer Research : CR, Nov 2024. URL: https://doi.org/10.1186/s13046-024-03207-4, doi:10.1186/s13046-024-03207-4. This article has 62 citations.
(hassan2024aktkinasesas pages 14-16): Dalal Hassan, Craig W. Menges, Joseph R Testa, and Alfonso Bellacosa. Akt kinases as therapeutic targets. Journal of Experimental & Clinical Cancer Research : CR, Nov 2024. URL: https://doi.org/10.1186/s13046-024-03207-4, doi:10.1186/s13046-024-03207-4. This article has 62 citations.
(browne2024resistancetotargeted pages 4-6): Iseult M. Browne and Alicia F. C. Okines. Resistance to targeted inhibitors of the pi3k/akt/mtor pathway in advanced oestrogen-receptor-positive breast cancer. Cancers, 16:2259, Jun 2024. URL: https://doi.org/10.3390/cancers16122259, doi:10.3390/cancers16122259. This article has 44 citations.
(kempska2023impactofakt1 pages 1-2): Joanna Kempska, Leticia Oliveira-Ferrer, Astrid Grottke, Minyue Qi, Malik Alawi, Felix Meyer, Kerstin Borgmann, Fabienne Hamester, Kathrin Eylmann, Maila Rossberg, Daniel J. Smit, Manfred Jücker, Elena Laakmann, Isabell Witzel, Barbara Schmalfeldt, Volkmar Müller, and Karen Legler. Impact of akt1 on cell invasion and radiosensitivity in a triple negative breast cancer cell line developing brain metastasis. Frontiers in Oncology, Jul 2023. URL: https://doi.org/10.3389/fonc.2023.1129682, doi:10.3389/fonc.2023.1129682. This article has 13 citations.
(alves2023druggingthepi3kaktmtor pages 1-2): Carla L. Alves and Henrik J. Ditzel. Drugging the pi3k/akt/mtor pathway in er+ breast cancer. International Journal of Molecular Sciences, 24:4522, Feb 2023. URL: https://doi.org/10.3390/ijms24054522, doi:10.3390/ijms24054522. This article has 127 citations.
(NCT04305496 chunk 1): Capivasertib+Fulvestrant vs Placebo+Fulvestrant as Treatment for Locally Advanced (Inoperable) or Metastatic HR+/HER2- Breast Cancer. AstraZeneca. 2020. ClinicalTrials.gov Identifier: NCT04305496
(NCT07281833 chunk 1): Phase III Study to Evaluate the Safety, Efficacy, and Impact on Quality of Life of Capivasertib Alongside Standard-of-care Endocrine Treatment in Patients With HR+/HER2- Advanced Breast Cancer and Progression on Prior Endocrine-based Treatment. West German Study Group. 2025. ClinicalTrials.gov Identifier: NCT07281833
(NCT04305496 chunk 6): Capivasertib+Fulvestrant vs Placebo+Fulvestrant as Treatment for Locally Advanced (Inoperable) or Metastatic HR+/HER2- Breast Cancer. AstraZeneca. 2020. ClinicalTrials.gov Identifier: NCT04305496