Andrew P. Halestrap
School of Biochemistry
Medical Sciences Building
University Walk
Bristol BS8 1TD
UK
Name/email consistency: high
- The mitochondrial pyruvate carrier: has it been unearthed at last? Halestrap, A.P. Cell Metab. (2012)
- The monocarboxylate transporter family-Role and regulation. Halestrap, A.P., Wilson, M.C. IUBMB. Life (2012)
- The monocarboxylate transporter family--Structure and functional characterization. Halestrap, A.P. IUBMB. Life (2012)
- What is the mitochondrial permeability transition pore? Halestrap, A.P. J. Mol. Cell. Cardiol. (2009)
- Mitochondria and reperfusion injury of the heart--a holey death but not beyond salvation. Halestrap, A.P. J. Bioenerg. Biomembr. (2009)
- The role of the mitochondrial permeability transition pore in heart disease. Halestrap, A.P., Pasdois, P. Biochim. Biophys. Acta (2009)
- The role of mitochondria in protection of the heart by preconditioning. Halestrap, A.P., Clarke, S.J., Khaliulin, I. Biochim. Biophys. Acta (2007)
- Calcium, mitochondria and reperfusion injury: a pore way to die. Halestrap, A.P. Biochem. Soc. Trans. (2006)
- The SLC16 gene family-from monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond. Halestrap, A.P., Meredith, D. Pflugers Arch. (2004)
- Mitochondrial permeability transition pore opening during myocardial reperfusion--a target for cardioprotection. Halestrap, A.P., Clarke, S.J., Javadov, S.A. Cardiovasc. Res. (2004)
- Mitochondrial permeability: dual role for the ADP/ATP translocator?. Halestrap, A.P. Nature (2004)
- The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death. Halestrap, A.P., Brenner, C. Curr. Med. Chem. (2003)
- The permeability transition pore complex: another view. Halestrap, A.P., McStay, G.P., Clarke, S.J. Biochimie (2002)
- The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Halestrap, A.P., Price, N.T. Biochem. J. (1999)
- Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. Halestrap, A.P., Woodfield, K.Y., Connern, C.P. J. Biol. Chem. (1997)
