| Human Aha1's N-terminal extension confers it holdase activity in vitro. | Human Aha1's N-terminal extension confers it holdase activity in vitro.
Tang J, Hu H, Zhou C, Zhang N., | 09/1/2023 |
| p23 and Aha1: Distinct Functions Promote Client Maturation. | p23 and Aha1: Distinct Functions Promote Client Maturation.
Biebl MM, Buchner J. | 12/31/2022 |
| The Prognostic and Immunotherapeutic Significance of AHSA1 in Pan-Cancer, and Its Relationship With the Proliferation and Metastasis of Hepatocellular Carcinoma. | The Prognostic and Immunotherapeutic Significance of AHSA1 in Pan-Cancer, and Its Relationship With the Proliferation and Metastasis of Hepatocellular Carcinoma.
Li W, Liu J., Free PMC Article | 07/2/2022 |
| Identification of AHSA1 as a Potential Therapeutic Target for Breast Cancer: Bioinformatics Analysis and in vitro Studies. | Identification of AHSA1 as a Potential Therapeutic Target for Breast Cancer: Bioinformatics Analysis and in vitro Studies.
Shi W, Qi L, You XB, Chen YC, Xu YL, Yu WB, Huang MY, Zhao H, Lu JJ. | 06/11/2022 |
| AHA1 upregulates IDH1 and metabolic activity to promote growth and metastasis and predicts prognosis in osteosarcoma. | AHA1 upregulates IDH1 and metabolic activity to promote growth and metastasis and predicts prognosis in osteosarcoma.
Zheng D, Liu W, Xie W, Huang G, Jiang Q, Yang Y, Huang J, Xing Z, Yuan M, Wei M, Li Y, Yin J, Shen J, Shi Z., Free PMC Article | 03/5/2022 |
| Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle? | Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle?
LaPointe P, Mercier R, Wolmarans A. | 06/26/2021 |
| Data support the multi-step nature of the Hsp90/Aha1-interaction, where the N-terminal domain of Aha1 interacts with both Hsp90 M domains upon induction of a partially closed conformation of the Hsp90 dimer. In addition, the data indicate that the C-terminal domain of Aha1 can adopt several conformations leading to a dynamic, polymorphic complex. | Dynamic Aha1 co-chaperone binding to human Hsp90.
Oroz J, Blair LJ, Zweckstetter M., Free PMC Article | 05/9/2020 |
| Aha1 colocalized with tau pathology in brain tissue, and this association positively correlated with Alzheimer disease progression. | Hsp90 activator Aha1 drives production of pathological tau aggregates.
Shelton LB, Baker JD, Zheng D, Sullivan LE, Solanki PK, Webster JM, Sun Z, Sabbagh JJ, Nordhues BA, Koren J 3rd, Ghosh S, Blagg BSJ, Blair LJ, Dickey CA., Free PMC Article | 06/9/2018 |
| These results suggest that differences in the middle domain of Hsp90alpha and Hsp90beta may be responsible for the isoform-specific interactions with selected proteins. | Middle domain of human Hsp90 isoforms differentially binds Aha1 in human cells and alters Hsp90 activity in yeast.
Synoradzki K, Bieganowski P. | 04/25/2015 |
| Aha1 may promote disposal of folding defective proteins by the cellular protein quality control. | Aha1 can act as an autonomous chaperone to prevent aggregation of stressed proteins.
Tripathi V, Darnauer S, Hartwig NR, Obermann WM., Free PMC Article | 04/18/2015 |
| Modulation of Hsp90 activity by AHA1 regulates VEGF signaling to eNOS and angiogenesis. | Modulation of the cochaperone AHA1 regulates heat-shock protein 90 and endothelial NO synthase activation by vascular endothelial growth factor.
Desjardins F, Delisle C, Gratton JP. | 01/12/2013 |
| The interaction of Aha1 with Hsp90 and its co-chaperones in rabbit reticulocyte lysate (RRL) and in HeLa cell extracts, was characterized. | Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins.
Sun L, Prince T, Manjarrez JR, Scroggins BT, Matts RL. | 11/17/2012 |
| Hsp90 phosphorylation on tyrosine313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process. | Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.
Xu W, Mollapour M, Prodromou C, Wang S, Scroggins BT, Palchick Z, Beebe K, Siderius M, Lee MJ, Couvillon A, Trepel JB, Miyata Y, Matts R, Neckers L., Free PMC Article | 10/27/2012 |
| Data propose a model for Aha1 in the Hsp90 ATPase cycle where Aha1 regulates dwell time of Hsp90, and suggest Aha1 activity integrates chaperone function with client folding energetics by modulating ATPase sensitive dimer structural transitions. | Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.
Koulov AV, LaPointe P, Lu B, Razvi A, Coppinger J, Dong MQ, Matteson J, Laister R, Arrowsmith C, Yates JR 3rd, Balch WE., Free PMC Article | 09/13/2010 |
| Hsp90 cochaperones modulate Hsp90-dependent stability of CFTR protein folding in the endoplasmic reticulum | Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis.
Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, Coppinger J, Gurkan C, Kellner W, Matteson J, Plutner H, Riordan JR, Kelly JW, Yates JR 3rd, Balch WE. | 01/21/2010 |
| stimulates the inherent ATPase activity of Hsp90 | Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C. | 01/21/2010 |