Dr Mark Bannister

Uwch-ddarlithydd, Biomedical Sciences

m.l.bannister@abertawe.ac.uk

Swyddfa Academaidd - 142
Llawr Cyntaf
Y Sefydliad Gwyddor Bywyd 1
Campws Singleton

Ar gael ar gyfer Goruchwyliaeth Ôl-raddedig

Dolenni Ymchwil

https://orcid.org/0000-0002-0865-5912

Trosolwg

Ar ôl ennill ei PhD yn Ysgol Cemeg Prifysgol Leeds, mae Dr Bannister wedi dal swyddi ôl-ddoethurol yng Ngholeg Imperial, Sefydliad Ymchwil Biofeddygol Boston, a Phrifysgol Caerdydd. Symudodd i Abertawe yn 2017 fel PI a ariennir gan Sefydliad y Galon Prydain lle mae'n ymchwilydd yn y grŵp Cardioleg Foleciwlaidd ac yn Oruchwyliwr Amddiffyn rhag Ymbelydredd ar gyfer yr Ysgol Feddygaeth. Mae ei ymchwil yn canolbwyntio ar ddeall mecanweithiau rheoleiddio ffarmacolegol y derbynnydd ryanodine.

Meysydd Arbenigedd

Signalau calsiwm
Sianeli ïon
Systemau pilen enghreifftiol

Cyhoeddiadau

Uchafbwyntiau Ymchwil

Williams, A., Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2016). Questioning flecainide's mechanism of action in the treatment of catecholaminergic polymorphic ventricular tachycardia. The Journal of Physiology, 594(21), 6431-6432.
https://doi.org/10.1113/jp272497, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34319
http://europepmc.org/abstract/med/27800620
Aggeli, A., Bannister, M., Bell, M., Boden, N., Findlay, J., Hunter, M., Knowles, P., Yang, J., & Bannister, M. (1998). Conformation and Ion-Channeling Activity of a 27-Residue Peptide Modeled on the Single-Transmembrane Segment of the IsK (minK) Protein†,‡. Biochemistry, 37(22), 8121-8131.
https://doi.org/10.1021/bi972112h, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34333
http://europepmc.org/abstract/med/9609707
Bannister, M., Williams, A., Sitsapesan, R., Bannister, M., & Williams, A. (2004). Removal of clustered positive charge from dihydropyridine receptor II–III loop peptide augments activation of ryanodine receptors. Biochemical and Biophysical Research Communications, 314(3), 667-674.
https://doi.org/10.1016/j.bbrc.2003.12.128, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34332
http://europepmc.org/abstract/med/14741687
Bannister, M., Williams, A., Bannister, M., & Williams, A. (2004). Activation of the sheep cardiac Ca2+ release channel by simple heteroaromatics. Biochemical and Biophysical Research Communications, 317(2), 397-400.
https://doi.org/10.1016/j.bbrc.2004.03.073, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34331
http://europepmc.org/abstract/med/15063771
Kobayashi, S., Bannister, M., Gangopadhyay, J., Hamada, T., Parness, J., Ikemoto, N., & Bannister, M. (2005). Dantrolene Stabilizes Domain Interactions within the Ryanodine Receptor. Journal of Biological Chemistry, 280(8), 6580-6587.
https://doi.org/10.1074/jbc.m408375200, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34330
http://europepmc.org/abstract/med/15611117
Bannister, M., Ikemoto, N., & Bannister, M. (2006). Effects of peptide C corresponding to the Glu724–Pro760region of the II–III loop of the DHP (dihydropyridine) receptor α1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+channels. Biochemical Journal, 394(1), 145-152.
https://doi.org/10.1042/bj20051373, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34329
http://europepmc.org/abstract/med/16302848
Bannister, M., Hamada, T., Murayama, T., Harvey, P., Casarotto, M., Dulhunty, A., Ikemoto, N., & Bannister, M. (2007). Malignant hyperthermia mutation sites in the Leu2442–Pro2477(DP4) region of RyR1 (ryanodine receptor 1) are clustered in a structurally and functionally definable area. Biochemical Journal, 401(1), 333-339.
https://doi.org/10.1042/bj20060902, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34328
http://europepmc.org/abstract/med/16958617
Hamada, T., Bannister, M., Ikemoto, N., & Bannister, M. (2007). Peptide Probe Study of the Role of Interaction between the Cytoplasmic and Transmembrane Domains of the Ryanodine Receptor in the Channel Regulation Mechanism†. Biochemistry, 46(14), 4272-4279.
https://doi.org/10.1021/bi061557f, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34327
http://europepmc.org/abstract/med/17361990
Toth, A., Nickson, P., Mandl, A., Bannister, M., Toth, K., Erhardt, P., & Bannister, M. (2007). Endoplasmic Reticulum Stress as a Novel Therapeutic Target in Heart Diseases. Cardiovascular & Hematological Disorders-Drug Targets, 7(3), 205-218.
https://doi.org/10.2174/187152907781745260, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34326
http://europepmc.org/abstract/med/17896961
Shtifman, A., Ward, C., Laver, D., Bannister, M., Lopez, J., Kitazawa, M., LaFerla, F., Ikemoto, N., Querfurth, H., & Bannister, M. (2010). Amyloid-β protein impairs Ca2+ release and contractility in skeletal muscle. Neurobiology of Aging, 31(12), 2080-2090.
https://doi.org/10.1016/j.neurobiolaging.2008.11.003, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34325
http://europepmc.org/abstract/med/19108934
Lyon, A., Bannister, M., Collins, T., Pearce, E., Sepehripour, A., Dubb, S., Garcia, E., O'Gara, P., Liang, L., Kohlbrenner, E., Hajjar, R., Peters, N., Poole-Wilson, P., Macleod, K., Harding, S., & Bannister, M. (2011). SERCA2a Gene Transfer Decreases Sarcoplasmic Reticulum Calcium Leak and Reduces Ventricular Arrhythmias in a Model of Chronic Heart Failure. Circulation: Arrhythmia and Electrophysiology, 4(3), 362-372.
https://doi.org/10.1161/circep.110.961615, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34324
http://europepmc.org/abstract/med/21406682
Mason, S., Viero, C., Euden, J., Bannister, M., West, D., Chen, S., Williams, A., Bannister, M., & Williams, A. (2012). The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations andShakerB inactivation peptides. The Journal of General Physiology, 140(3), 325-339.
https://doi.org/10.1085/jgp.201210851, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34323
http://europepmc.org/abstract/med/22930804
Bannister, M., Alvarez-Laviada, A., Thomas, N., Mason, S., Coleman, S., du, P., Moran, A., Neill-Hall, D., Osman, H., Bagley, M., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., & Williams, A. (2016). Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor. British Journal of Pharmacology, 173(15), 2446-2459.
https://doi.org/10.1111/bph.13521, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34321
http://europepmc.org/abstract/med/27237957
George, C., Mitchell, A., Preece, R., Bannister, M., Yousef, Z., Bannister, M., & George, C. (2016). Pleiotropic mechanisms of action of perhexiline in heart failure. Expert Opinion on Therapeutic Patents, 26(9), 1049-1059.
https://doi.org/10.1080/13543776.2016.1211111, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34320
Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2015). The Mechanism of Flecainide Action in CPVT Does Not Involve a Direct Effect on RyR2. Circulation Research, 116(8), 1324-1335.
https://doi.org/10.1161/CIRCRESAHA.116.305347, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34834
Seidel, M., Rabesahala de Meritens, C., Johnson, L., Parthimos, D., Bannister, M., Thomas, N., Ozekhome-Mike, E., Lai, F., & Zisimopoulos, S. (2021). Identification of an amino-terminus determinant critical for ryanodine receptor/Ca2+ release channel function. Cardiovascular Research, 117(3), 780-791.
https://doi.org/10.1093/cvr/cvaa043, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa53861
Bannister, M., MacLeod, K., & George, C. (2022). Moving in the right direction: elucidating the mechanisms of interaction between flecainide and the cardiac ryanodine receptor. British Journal of Pharmacology, 179(11), 2558-2563.
https://doi.org/10.1111/bph.15718, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa58568

Holl Ymchwil

Erthyglau Cylchgronau

Bannister, M., MacLeod, K., & George, C. (2022). Moving in the right direction: elucidating the mechanisms of interaction between flecainide and the cardiac ryanodine receptor. British Journal of Pharmacology, 179(11), 2558-2563.
https://doi.org/10.1111/bph.15718, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa58568
Seidel, M., Rabesahala de Meritens, C., Johnson, L., Parthimos, D., Bannister, M., Thomas, N., Ozekhome-Mike, E., Lai, F., & Zisimopoulos, S. (2021). Identification of an amino-terminus determinant critical for ryanodine receptor/Ca2+ release channel function. Cardiovascular Research, 117(3), 780-791.
https://doi.org/10.1093/cvr/cvaa043, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa53861
Williams, A., Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2016). Questioning flecainide's mechanism of action in the treatment of catecholaminergic polymorphic ventricular tachycardia. The Journal of Physiology, 594(21), 6431-6432.
https://doi.org/10.1113/jp272497, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34319
http://europepmc.org/abstract/med/27800620
George, C., Mitchell, A., Preece, R., Bannister, M., Yousef, Z., Bannister, M., & George, C. (2016). Pleiotropic mechanisms of action of perhexiline in heart failure. Expert Opinion on Therapeutic Patents, 26(9), 1049-1059.
https://doi.org/10.1080/13543776.2016.1211111, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34320
Bannister, M., Alvarez-Laviada, A., Thomas, N., Mason, S., Coleman, S., du, P., Moran, A., Neill-Hall, D., Osman, H., Bagley, M., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., & Williams, A. (2016). Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor. British Journal of Pharmacology, 173(15), 2446-2459.
https://doi.org/10.1111/bph.13521, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34321
http://europepmc.org/abstract/med/27237957
Bannister, M., Thomas, N., Sikkel, M., Mukherjee, S., Maxwell, C., MacLeod, K., George, C., Williams, A., Bannister, M., George, C., Thomas, N., Mukherjee, S., & Williams, A. (2015). The Mechanism of Flecainide Action in CPVT Does Not Involve a Direct Effect on RyR2. Circulation Research, 116(8), 1324-1335.
https://doi.org/10.1161/CIRCRESAHA.116.305347, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34834
Mason, S., Viero, C., Euden, J., Bannister, M., West, D., Chen, S., Williams, A., Bannister, M., & Williams, A. (2012). The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations andShakerB inactivation peptides. The Journal of General Physiology, 140(3), 325-339.
https://doi.org/10.1085/jgp.201210851, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34323
http://europepmc.org/abstract/med/22930804
Lyon, A., Bannister, M., Collins, T., Pearce, E., Sepehripour, A., Dubb, S., Garcia, E., O'Gara, P., Liang, L., Kohlbrenner, E., Hajjar, R., Peters, N., Poole-Wilson, P., Macleod, K., Harding, S., & Bannister, M. (2011). SERCA2a Gene Transfer Decreases Sarcoplasmic Reticulum Calcium Leak and Reduces Ventricular Arrhythmias in a Model of Chronic Heart Failure. Circulation: Arrhythmia and Electrophysiology, 4(3), 362-372.
https://doi.org/10.1161/circep.110.961615, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34324
http://europepmc.org/abstract/med/21406682
Shtifman, A., Ward, C., Laver, D., Bannister, M., Lopez, J., Kitazawa, M., LaFerla, F., Ikemoto, N., Querfurth, H., & Bannister, M. (2010). Amyloid-β protein impairs Ca2+ release and contractility in skeletal muscle. Neurobiology of Aging, 31(12), 2080-2090.
https://doi.org/10.1016/j.neurobiolaging.2008.11.003, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34325
http://europepmc.org/abstract/med/19108934
Toth, A., Nickson, P., Mandl, A., Bannister, M., Toth, K., Erhardt, P., & Bannister, M. (2007). Endoplasmic Reticulum Stress as a Novel Therapeutic Target in Heart Diseases. Cardiovascular & Hematological Disorders-Drug Targets, 7(3), 205-218.
https://doi.org/10.2174/187152907781745260, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34326
http://europepmc.org/abstract/med/17896961
Hamada, T., Bannister, M., Ikemoto, N., & Bannister, M. (2007). Peptide Probe Study of the Role of Interaction between the Cytoplasmic and Transmembrane Domains of the Ryanodine Receptor in the Channel Regulation Mechanism†. Biochemistry, 46(14), 4272-4279.
https://doi.org/10.1021/bi061557f, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34327
http://europepmc.org/abstract/med/17361990
Bannister, M., Hamada, T., Murayama, T., Harvey, P., Casarotto, M., Dulhunty, A., Ikemoto, N., & Bannister, M. (2007). Malignant hyperthermia mutation sites in the Leu2442–Pro2477(DP4) region of RyR1 (ryanodine receptor 1) are clustered in a structurally and functionally definable area. Biochemical Journal, 401(1), 333-339.
https://doi.org/10.1042/bj20060902, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34328
http://europepmc.org/abstract/med/16958617
Bannister, M., Ikemoto, N., & Bannister, M. (2006). Effects of peptide C corresponding to the Glu724–Pro760region of the II–III loop of the DHP (dihydropyridine) receptor α1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+channels. Biochemical Journal, 394(1), 145-152.
https://doi.org/10.1042/bj20051373, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34329
http://europepmc.org/abstract/med/16302848
Kobayashi, S., Bannister, M., Gangopadhyay, J., Hamada, T., Parness, J., Ikemoto, N., & Bannister, M. (2005). Dantrolene Stabilizes Domain Interactions within the Ryanodine Receptor. Journal of Biological Chemistry, 280(8), 6580-6587.
https://doi.org/10.1074/jbc.m408375200, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34330
http://europepmc.org/abstract/med/15611117
Bannister, M., Williams, A., Bannister, M., & Williams, A. (2004). Activation of the sheep cardiac Ca2+ release channel by simple heteroaromatics. Biochemical and Biophysical Research Communications, 317(2), 397-400.
https://doi.org/10.1016/j.bbrc.2004.03.073, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34331
http://europepmc.org/abstract/med/15063771
Bannister, M., Williams, A., Sitsapesan, R., Bannister, M., & Williams, A. (2004). Removal of clustered positive charge from dihydropyridine receptor II–III loop peptide augments activation of ryanodine receptors. Biochemical and Biophysical Research Communications, 314(3), 667-674.
https://doi.org/10.1016/j.bbrc.2003.12.128, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34332
http://europepmc.org/abstract/med/14741687
Aggeli, A., Bannister, M., Bell, M., Boden, N., Findlay, J., Hunter, M., Knowles, P., Yang, J., & Bannister, M. (1998). Conformation and Ion-Channeling Activity of a 27-Residue Peptide Modeled on the Single-Transmembrane Segment of the IsK (minK) Protein†,‡. Biochemistry, 37(22), 8121-8131.
https://doi.org/10.1021/bi972112h, SU Repository: https://cronfa.swan.ac.uk/Record/cronfa34333
http://europepmc.org/abstract/med/9609707

Modiwlau a Addysgir

PM-130 Fundamental Research Skills

This module is designed to develop the skills required for students of biochemistry and genetics degree programmes. Students meet with their tutors and will be given a series of assignments designed to develop skills in key areas such as essay writing, presentations and general numeracy.
PM-154 Human Physiology

Human physiology is the study of how our body works in an integrated way. A central principle of human physiology is homeostasis, the maintenance of a relatively stable internal environment. Failure to maintain homeostasis disrupts normal function that may lead to disease (or pathophysiology). Students will be taught the key concepts of homeostasis in the physiological systems of the body, enabling the student to understand the consequences of pathophysiology to human health. Emphasis will be given to how malfunction of key physiological systems gives rise to disease, using specific examples to enable students to appreciate the relationship between physiology/anatomy and medicine. Fundamental principles of physiology will be illustrated with appropriate clinical examples and during lectures and in practical assignments. Students will gain practical experience in assessing physiological function during four laboratory-based exercises. The impact of pathophysiology of such systems will be assessed through clinical case studies.
PM-154C Ffisioleg Ddynol

Ffisioleg Ddynol yw astudio sut mae ein cyrff yn gweithio mewn ffordd integredig. Egwyddor sydd wrth wraidd ffisioleg ddynol yw homeostasis, sef cynnal amgylchedd mewnol cymharol sefydlog. Os na chynhelir homeostasis, bydd yn amharu ar swyddogaeth arferol a allai arwain at glefyd (neu bathoffisioleg). Caiff myfyrwyr eu haddysgu am gysyniadau allweddol homeostasis yn systemau ffisiolegol y corff, gan alluogi'r myfyriwr i ddeall canlyniadau pathoffisioleg i iechyd pobl.Rhoddir pwyslais ar y ffordd y mae methiannau systemau ffisiolegol allweddol yn arwain at glefyd, gan ddefnyddio enghreifftiau penodol i alluogi myfyrwyr i werthfawrogi'r berthynas rhwng ffisioleg/anatomeg a meddygaeth.Caiff egwyddorion sylfaenol ffisioleg eu hesbonio ag enghreifftiau clinigol priodol ac yn ystod darlithoedd ac mewn aseiniadau ymarferol.Bydd myfyrwyr yn cael profiad ymarferol o asesu swyddogaeth ffisiolegol yn ystod pedwar ymarfer yn y labordy. Asesir effaith pathoffisioleg mewn systemau o'r fath drwy astudiaethau achos clinigol.
PM-266 The Cardiovascular System

Leading on from the first year Human Physiology Module (PM-154), the Cardiovascular Module will introduce and define the fundamental cellular mechanisms that regulate the physiology of healthy cardiovascular function. The Module will describe the processes that allow regular heartbeat and blood vessel function and how perturbations in the systems covered may lead to pathophysiological conditions. There will be an emphasis on experimental approaches used to study the cardiovascular mechanisms described.
PM-344 Capstone Project

The aim of this module is to provide a capstone experience to students¿ learning, through participating in their own enquiry-based research project, with guidance from an academic supervisor. The project may be laboratory or non-laboratory based, but it will always involve a research question that is drawn from the literature, and focused on a topic relevant to the life sciences. It will ask a research question and involve the critical analysis of research findings. Students will refine their oral and written communication skills to a graduate level through an oral presentation and dissertation on their research findings and conclusions.
PMGM17 Dissertation Project

The module is for students to build on their previous knowledge, skills and experience by undertaking a laboratory based or suitable non-laboratory based project on a specific subject related to genomics.

Dr Mark Bannister

Cyfeiriad ebost

Dolenni Ymchwil

Trosolwg

Meysydd Arbenigedd

Cyhoeddiadau

Uchafbwyntiau Ymchwil

Holl Ymchwil

Erthyglau Cylchgronau

Modiwlau a Addysgir

PM-130 Fundamental Research Skills

PM-154 Human Physiology

PM-154C Ffisioleg Ddynol

PM-266 The Cardiovascular System

PM-344 Capstone Project

PMGM17 Dissertation Project