HAX-1 regulates cyclophilin-D levels and mitochondria permeability transition pore in the heart

Heart Disease and Stroke Statistics—2015 Update: A Report From the American Heart Association

Mozaffarian, D., Benjamin, E. J., Go, A. S., Arnett, D. K., Blaha, M. J., Cushman, M., de Ferranti, S., Després, J.-P., Fullerton, H. J., Howard, V. J., et al. (2015) · Circulation · doi:10.1161/cir.0000000000000152 · Cited by 5,797 · see citing works

Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+

Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · see citing works

Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works

Mechanisms Underlying Acute Protection From Cardiac Ischemia-Reperfusion Injury

Murphy, E., & Steenbergen, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00024.2007 · Cited by 1,472 · see citing works

Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death

Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971 · see citing works

Bortezomib as the First Proteasome Inhibitor Anticancer Drug: Current Status and Future Perspectives

Chen, D., Frezza, M., Schmitt, S. M., Kanwar, J., & Dou, Q. P. (2011) · Current Cancer Drug Targets · doi:10.2174/156800911794519752 · Cited by 796 · see citing works

Relationship between configuration, function, and permeability in calcium-treated mitochondria.

Hunter, D. R., Haworth, R. A., & Southard, J. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33220-9 · Cited by 619 · see citing works

Mitochondrial Control of Cellular Life, Stress, and Death

Galluzzi, L., Kepp, O., Trojel‐Hansen, C., & Kroemer, G. (2012) · Circulation Research · doi:10.1161/circresaha.112.268946 · Cited by 545 · see citing works

HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease)

Klein, C., Grudzien, M., Appaswamy, G., Germeshausen, M., Sandrock, I., Schäffer, A. A., Rathinam, C., Boztuǧ, K., Schwinzer, B., Rezaei, N., et al. (2006) · Nature Genetics · doi:10.1038/ng1940 · Cited by 501 · see citing works

Cardiomyocyte death: mechanisms and translational implications

Chiong, M., Wang, Z. V., Pedrozo, Z., Cao, D. J., Troncoso, R., Ibacache, M. E., Criollo, A., Nemchenko, A., Hill, J. A., & Lavandero, S. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.130 · Cited by 492 · see citing works

National Academy of Clinical Biochemistry Laboratory Medicine Practice Guidelines: Clinical Characteristics and Utilization of Biochemical Markers in Acute Coronary Syndromes

NACB WRITING GROUP MEMBERS, Morrow, D. A., Cannon, C. P., Jesse, R. L., Newby, L. K., Ravkilde, J., Storrow, A. B., Wu, A. H. B., Christenson, R. H., Christenson, R. H., et al. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2006.084194 · Cited by 473 · see citing works

Regulation of Tumor Cell Mitochondrial Homeostasis by an Organelle-Specific Hsp90 Chaperone Network

Kang, B. H., Plescia, J., Dohi, T., Rosa, J., Doxsey, S., & Altieri, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.08.028 · Cited by 445 · see citing works

Bax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in mice

Karch, J., Kwong, J. Q., Burr, A. R., Sargent, M. A., Elrod, J. W., Peixoto, P. M., Martinez-Caballero, S., Osinska, H., Cheng, E. H.-Y., Robbins, J., et al. (2013) · eLife · doi:10.7554/elife.00772 · Cited by 290 · cited 3× · see citing works

Physiologic Functions of Cyclophilin D and the Mitochondrial Permeability Transition Pore

Elrod, J. W., & Molkentin, J. D. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-0321 · Cited by 266 · see citing works

HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases

Suzuki, Y., Demolière, C., Kitamura, D., et al. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.6.2736 · Cited by 258 · see citing works

Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons

Chao, J.-R., Parganas, E., Boyd, K. L., Hong, C. Y., Opferman, J. T., & Ihle, J. N. (2008) · Nature · doi:10.1038/nature06604 · Cited by 245 · see citing works

Role of the Ubiquitin Proteasome System in the Heart

Pagan, J. K., Seto, T., Pagano, M., & Cittadini, A. (2013) · Circulation Research · doi:10.1161/circresaha.112.300521 · Cited by 139 · see citing works

Hsp20 Functions as a Novel Cardiokine in Promoting Angiogenesis via Activation of VEGFR2

Zhang, X., Wang, X., Zhu, H., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032765 · Cited by 121 · see citing works

HAX-1: A multifunctional protein with emerging roles in human disease

Fadeel, B., & Grzybowska, E. A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.004 · Cited by 117 · see citing works

Matrix Revisited

Carley, A. N., Taegtmeyer, H., & Lewandowski, E. D. (2014) · Circulation Research · doi:10.1161/circresaha.114.301863 · Cited by 99 · see citing works

Phospholamban Interacts with HAX-1, a Mitochondrial Protein with Anti-apoptotic Function

Vafiadaki, E., Sanoudou, D., Arvanitis, D. A., Catino, D. H., Kranias, E. G., & Kontrogianni‐Konstantopoulos, A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.057 · Cited by 99 · see citing works

The mitochondrial permeability transition pore and its adaptive responses in tumor cells

Rasola, A., & Bernardi, P. (2014) · Cell Calcium · doi:10.1016/j.ceca.2014.10.003 · Cited by 91 · see citing works

Highly Sensitive Cardiac Troponin T Values Remain Constant after Brief Exercise- or Pharmacologic-Induced Reversible Myocardial Ischemia

Kurz, K., Giannitsis, E., Zehelein, J., et al. (2008) · Clinical Chemistry · doi:10.1373/clinchem.2007.097865 · Cited by 91 · see citing works

Novel Role of HAX-1 in Ischemic Injury Protection Involvement of Heat Shock Protein 90

Lam, C. K., Zhao, W. H., Cai, W., Vafiadaki, E., Florea, S. M., Ren, X., Liu, Y., Robbins, N., Zhang, Z., Zhou, X., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.279935 · Cited by 78 · see citing works

Disruption of the PRKCD–FBXO25–HAX-1 axis attenuates the apoptotic response and drives lymphomagenesis

Baumann, Ü., Fernández‐Sáiz, V., Rudelius, M., Lemeer, S., Rad, R., Knorn, A.-M., Slawska, J., Engel, K. C., Jeremias, I., Li, Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3740 · Cited by 62 · see citing works

Mitochondria and heart failure: new insights into an energetic problem.

Chen, L., & Knowlton, A. A. (2010) · PubMed · Cited by 60 · see citing works

Increased expression and intramitochondrial translocation of cyclophilin-D associates with increased vulnerability of the permeability transition pore to stress-induced opening during compensated ventricular hypertrophy

Matas, J., Young, N. T. S., Bourcier‐Lucas, C., Ascah, A., Marcil, M., Deschepper, C. F., & Burelle, Y. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.10.020 · Cited by 59 · see citing works

The anti-apoptotic protein HAX-1 is a regulator of cardiac function

Zhao, W. H., Waggoner, J. R., Zhang, Z., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906998106 · Cited by 59 · see citing works

Inhibition of the mitochondrial Hsp90 chaperone network: A novel, efficient treatment strategy for cancer?

Siegelin, M. D. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.01.045 · Cited by 55 · see citing works

HAX‐1: A family of apoptotic regulators in health and disease

Yap, S. V., Koontz, J., & Kontrogianni‐Konstantopoulos, A. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22638 · Cited by 53 · see citing works

Deregulation of Mitochondrial Membrane Potential by Mitochondrial Insertion of Granzyme B and Direct Hax-1 Cleavage

Han, J., Goldstein, L. A., Hou, W., Froelich, C. J., Watkins, S. C., & Rabinowich, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086587 · Cited by 46 · see citing works

Proteasome Inhibition and Combination Therapy for Non-Hodgkin's Lymphoma: From Bench to Bedside

Mato, A. R., Feldman, T. A., & Goy, A. H. (2012) · The Oncologist · doi:10.1634/theoncologist.2011-0341 · Cited by 36 · see citing works

HAX-1: A multifaceted antiapoptotic protein localizing in the mitochondria and the sarcoplasmic reticulum of striated muscle cells

Yap, S. V., Vafiadaki, E., Strong, J. C., & Kontrogianni‐Konstantopoulos, A. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.10.028 · Cited by 33 · see citing works

Novel HAX1 gene mutations associated to neurodevelopment abnormalities in two Italian patients with severe congenital neutropenia

Lanciotti, M., Indaco, S., Bonanomi, S., et al. (2010) · Haematologica · doi:10.3324/haematol.2009.015370 · Cited by 20 · see citing works

A novel HAX1 gene mutation in severe congenital neutropenia (SCN) associated with neurological manifestations

Faiyaz‐Ul‐Haque, M., Al‐Jefri, A., Al‐Dayel, F., et al. (2010) · European Journal of Pediatrics · doi:10.1007/s00431-010-1150-6 · Cited by 18 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

The path from mitochondrial <scp>ROS</scp> to aging runs through the mitochondrial permeability transition pore

Rottenberg, H., & Hoek, J. B. (2017) · Aging Cell · doi:10.1111/acel.12650 · Cited by 275 · see citing works

Mitochondria and cardiovascular diseases-from pathophysiology to treatment

Siasos, G., Tsigkou, V., Kosmopoulos, M., Theodosiadis, D., Simantiris, S., Tagkou, N. M., Tsimpiktsioglou, A., Stampouloglou, P. K., Oikonomou, E., Mourouzis, K., et al. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.06.21 · Cited by 245 · see citing works

Inhibition of HIV-1 Replication by Cyclosporine A or Related Compounds Correlates with the Ability to Disrupt the Gag–Cyclophilin A Interaction

Franke, E. K., & Luban, J. (1996) · Virology · doi:10.1006/viro.1996.0421 · Cited by 145 · see citing works

Functional association of cyclophilin A with HIV-1 virions

Thali, M., Bukovsky, A., Kondo, E., Rosenwlrth, B., Walsh, C. T., Sodroski, J., & Göttlinger, H. G. (1994) · Nature · doi:10.1038/372363a0 · Cited by 629 · see citing works

Structure-based identification of small molecule compounds targeting cell cyclophilin A with anti-HIV-1 activity

Chen, D., Zhao, X., Tan, J., Lü, H., Qi, Z., Huang, Q., Zeng, X., Zhang, M., Jiang, S., Jiang, H., et al. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.03.023 · Cited by 23 · see citing works

Specific incorporation of cyclophilin A into HIV-1 virions

Franke, E. K., Yuan, H. E. H., & Luban, J. (1994) · Nature · doi:10.1038/372359a0 · Cited by 745 · see citing works

Cyclosporine A-resistant human immunodeficiency virus type 1 mutants demonstrate that Gag encodes the functional target of cyclophilin A

Braaten, D., Aberham, C., Franke, E., Yin, L., Phares, W., & Luban, J. (1996) · Journal of Virology · doi:10.1128/jvi.70.8.5170-5176.1996 · Cited by 161 · see citing works