Dr Jill Madine PhD
Research Fellow/Lecturer Biochemistry
- +44 (0)151 794 9509
- Work email J.Madine@liverpool.ac.uk
Publications
Selected Publications
- Oxidative Stress Alters the Morphology and Toxicity of Aortic Medial Amyloid (Journal article - 2015)
- Site-Specific Identification of an A ss Fibril-Heparin Interaction Site by Using Solid-State NMR Spectroscopy (Journal article - 2012)
- Comparison of aggregation enhancement and inhibition as strategies for reducing the cytotoxicity of the aortic amyloid polypeptide medin (Journal article - 2010)
- Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR (Journal article - 2008)
- Cross-beta Spine Architecture of Fibrils Formed by the Amyloidogenic Segment NFGSVQFV of Medin from Solid-State NMR and X-ray Fiber Diffraction Measurements (Journal article - 2009)
2019
Bicuspid valve aortopathy is associated with distinct patterns of matrix degradation. (Journal article)
Chim, Y. H., Davies, H. A., Mason, D., Nawaytou, O., Field, M., Madine, J., & Akhtar, R. (2019). Bicuspid valve aortopathy is associated with distinct patterns of matrix degradation.. The Journal of thoracic and cardiovascular surgery. doi:10.1016/j.jtcvs.2019.08.094
Idiopathic degenerative thoracic aneurysms are associated with increased aortic medial amyloid (Journal article)
Davies, H. A., Caamano-Gutierrez, E., Chim, Y. H., Field, M., Nawaytou, O., Ressel, L., . . . Madine, J. (2019). Idiopathic degenerative thoracic aneurysms are associated with increased aortic medial amyloid. AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, 26(3), 148-155. doi:10.1080/13506129.2019.1625323
BAV AORTOPATHY EXHIBITS A UNIQUE PATTERN OF AORTIC DEGRADATION EVEN THOUGH THE CLINICAL RISK OF RUPTURE MIRRORS OTHER ANEURYSMS - A MICROMECHANICAL AND MICROSTRUCTURAL APPROACH (Conference Paper)
Chim, Y. H., Davies, H., Field, M., Madine, J., & Akhtar, R. (2019). BAV AORTOPATHY EXHIBITS A UNIQUE PATTERN OF AORTIC DEGRADATION EVEN THOUGH THE CLINICAL RISK OF RUPTURE MIRRORS OTHER ANEURYSMS - A MICROMECHANICAL AND MICROSTRUCTURAL APPROACH. In HEART Vol. 105 (pp. A162). doi:10.1136/heartjnl-2019-BCS.196
Cofactor-mediated amyloidogenesis (Journal article)
Madine, J. (2019). Cofactor-mediated amyloidogenesis. BIOSCIENCE REPORTS, 39. doi:10.1042/BSR20190327
Discerning How Vascular Inflammation Modulates Neuroinflammation Using Novel Vascular Brain Organ-On-A-Chip: Proof-of-Concept Study. (Conference Paper)
Veldhuizen, J., Truran, S., Madine, J., Davies, H., Karamanova, N., Nikkhah, M., & Migrino, R. Q. (2019). Discerning How Vascular Inflammation Modulates Neuroinflammation Using Novel Vascular Brain Organ-On-A-Chip: Proof-of-Concept Study.. In STROKE Vol. 50. Retrieved from http://gateway.webofknowledge.com/
Endothelial Cell Proinflammatory Priming by Amyloidogenic Medin via NF[kappa]B and Inflammasome Pathways and Reversal by Monosialoganglioside Nanoliposomes (Conference Paper)
Karamanova, N., Truran, S., Madine, J., Davies, H., Zhang, W., Franco, D., . . . Migrino, R. Q. (2019). Endothelial Cell Proinflammatory Priming by Amyloidogenic Medin via NF[kappa]B and Inflammasome Pathways and Reversal by Monosialoganglioside Nanoliposomes. In STROKE Vol. 50. Retrieved from http://gateway.webofknowledge.com/
Elastic, Viscoelastic and Dissection Resistance Properties of the Ovine Aorta: Correlation with Regional Variations in Collagen, Elastin and Glycosominoglycan Levels (Journal article)
Panpho, P., Al-Matari, M., Field, M., Madine, J., & Akhtar, R. (2019). Elastic, Viscoelastic and Dissection Resistance Properties of the Ovine Aorta: Correlation with Regional Variations in Collagen, Elastin and Glycosominoglycan Levels.
2018
Isolation and purification of recombinant immunoglobulin light chain variable domains from the periplasmic space of Escherichia coli (Journal article)
Hand, K., Wilkinson, M. C., & Madine, J. (2018). Isolation and purification of recombinant immunoglobulin light chain variable domains from the periplasmic space of Escherichia coli. PLOS ONE, 13(10). doi:10.1371/journal.pone.0206167
Peripheral Adipose Arteriole Dilator Response to Amyloid Proteins and Palmitic Acid Recapitulates Central Leptomeningeal Arteriole Response: Validation of a Novel Human Tissue Model (Conference Paper)
Truran, S., Karamanova, N., Serrano, G., Madine, J., Davies, H., Beach, T., & Migrino, R. Q. (2018). Peripheral Adipose Arteriole Dilator Response to Amyloid Proteins and Palmitic Acid Recapitulates Central Leptomeningeal Arteriole Response: Validation of a Novel Human Tissue Model. In FASEB JOURNAL Vol. 32. Retrieved from http://gateway.webofknowledge.com/
Human cerebral collateral arteriole function in subjects with normal cognition, mild cognitive impairment, and dementia (Journal article)
Migrino, R. Q., Truran, S., Karamanova, N., Serrano, G. E., Madrigal, C., Davies, H. A., . . . Beach, T. G. (2018). Human cerebral collateral arteriole function in subjects with normal cognition, mild cognitive impairment, and dementia. AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY, 315(2), H284-H290. doi:10.1152/ajpheart.00206.2018
Insights into the Origin of Distinct Medin Fibril Morphologies Induced by Incubation Conditions and Seeding (Journal article)
Davies, H. A., Lee, C. F., Miller, L., Liu, L. -N., & Madine, J. (2018). Insights into the Origin of Distinct Medin Fibril Morphologies Induced by Incubation Conditions and Seeding. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 19(5). doi:10.3390/ijms19051357
Amyloidogenic Medin Impairs Endothelial Cell Autophagy and Viability that is Reversed by Monosialoganglioside Nanoliposomes (Conference Paper)
Karamanova, N., Truran, S., Weissig, V., Madine, J., Davies, H., Guzman-Villanueva, D., & Migrino, R. (2018). Amyloidogenic Medin Impairs Endothelial Cell Autophagy and Viability that is Reversed by Monosialoganglioside Nanoliposomes. In FASEB JOURNAL Vol. 32. Retrieved from http://gateway.webofknowledge.com/
Monitoring Native and Aggregate Structure of Amino Acids and Human Insulin with Blue Autofluorescence (Conference Paper)
Cumberbatch, N., Madine, J., & Arnolds, H. (2018). Monitoring Native and Aggregate Structure of Amino Acids and Human Insulin with Blue Autofluorescence. In BIOPHYSICAL JOURNAL Vol. 114 (pp. 172A). doi:10.1016/j.bpj.2017.11.959
Comparison of Ex-vivo Human Leptomeningeal Arteriole Function in Cognitively Normal and Dementia Disorders From Rapid Autopsy Brain Donors (Conference Paper)
Madrigal, C., Truran, S., Karamanova, N., Serrano, G., Madine, J., Davies, H., . . . Migrino, R. Q. (2018). Comparison of Ex-vivo Human Leptomeningeal Arteriole Function in Cognitively Normal and Dementia Disorders From Rapid Autopsy Brain Donors. In STROKE Vol. 49. Retrieved from http://gateway.webofknowledge.com/
2017
Medin Amyloid Protein-Induced Human Leptomeningeal Arteriole Endothelial Dysfunction and Pro-Inflammatory Signaling are Reversed by Monosialoganglioside Nanoliposomes (Conference Paper)
Truran, S., Karamanova, N., Madine, J., Davies, H., Guzman-Villanueva, D., Serrano, G., . . . Migrino, R. Q. (2017). Medin Amyloid Protein-Induced Human Leptomeningeal Arteriole Endothelial Dysfunction and Pro-Inflammatory Signaling are Reversed by Monosialoganglioside Nanoliposomes. In CIRCULATION Vol. 136. Retrieved from http://gateway.webofknowledge.com/
Medin Amyloid, but Not beta-amyloid, Induces Pro-Inflammatory Signaling in Endothelial Cells That is Synergistic With Palmitic Acid (Conference Paper)
Karamanova, N., Truran, S., Madine, J., Davies, H., Anderson, J., Franco, D. A., . . . Migrino, R. Q. (2017). Medin Amyloid, but Not beta-amyloid, Induces Pro-Inflammatory Signaling in Endothelial Cells That is Synergistic With Palmitic Acid. In CIRCULATION Vol. 136. Retrieved from http://gateway.webofknowledge.com/
Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein (Journal article)
Phelan, M. M., Caamano-Gutierrez, E., Gant, M. S., Grosman, R. X., & Madine, J. (2017). Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein. METABOLOMICS, 13(12). doi:10.1007/s11306-017-1289-5
Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study (Journal article)
Mukherjee, S., Pondaven, S. P., Hand, K., Madine, J., & Jaroniec, C. P. (2017). Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study. SCIENTIFIC REPORTS, 7. doi:10.1038/s41598-017-10906-w
Amyloidogenic Medin Induces Endothelial Dysfunction and Vascular Inflammation through the Receptor for Advanced Glycation Endproducts (Journal article)
Migrino, R. Q., Davies, H. A., Truran, S., Karamanova, N., Franco, D. A., Beach, T. G., . . . Madine, J. (2017). Amyloidogenic medin induces endothelial dysfunction and vascular inflammation through the receptor for advanced glycation endproducts. CARDIOVASCULAR RESEARCH, 113(11), 1389-1402. doi:10.1093/cvr/cvx135
Amyloidogenic Medin Induces Endothelial Dysfunction and Vascular Inflammation Through the Receptor for Advanced Glycation Endproducts (Conference Paper)
Migrino, R. Q., Davies, H., Truran, S., Karamanova, N., Franco, D. A., Serrano, G., . . . Madine, J. (2017). Amyloidogenic Medin Induces Endothelial Dysfunction and Vascular Inflammation Through the Receptor for Advanced Glycation Endproducts. In FASEB JOURNAL Vol. 31. Retrieved from http://gateway.webofknowledge.com/
Probing Medin Monomer Structure and its Amyloid Nucleation Using C-13-Direct Detection NMR in Combination with Structural Bioinformatics (Journal article)
Davies, H. A., Rigden, D. J., Phelan, M. M., & Madine, J. (2017). Probing Medin Monomer Structure and its Amyloid Nucleation Using C-13-Direct Detection NMR in Combination with Structural Bioinformatics. SCIENTIFIC REPORTS, 7. doi:10.1038/srep45224
2016
Heparin and Methionine Oxidation Promote the Formation of Apolipoprotein A-I Amyloid Comprising alpha-Helical and beta-Sheet Structures (Journal article)
Townsend, D., Hughes, E., Hussain, R., Siligardi, G., Baldock, S., Madine, J., & Middleton, D. A. (2017). Heparin and Methionine Oxidation Promote the Formation of Apolipoprotein A-I Amyloid Comprising alpha-Helical and beta-Sheet Structures. BIOCHEMISTRY, 56(11), 1632-1644. doi:10.1021/acs.biochem.6b01120
HUMAN MICROVASCULAR ENDOTHELIAL DYSFUNCTION INDUCED BY AMYLOIDOGENIC MEDIN PROTEIN (Conference Paper)
Migrino, R. Q., Truran, S., Karamanova, N., Franco, D., Davies, H. A., Burciu, C., & Madine, J. (2016). HUMAN MICROVASCULAR ENDOTHELIAL DYSFUNCTION INDUCED BY AMYLOIDOGENIC MEDIN PROTEIN. In JOURNAL OF THE AMERICAN COLLEGE OF CARDIOLOGY Vol. 67 (pp. 2310). doi:10.1016/S0735-1097(16)32311-7
2015
Nanoliposomes protect against human arteriole endothelial dysfunction induced by beta-amyloid peptide (Journal article)
Truran, S., Weissig, V., Madine, J., Davies, H. A., Guzman-Villanueva, D., Franco, D. A., . . . Migrino, R. Q. (2016). Nanoliposomes protect against human arteriole endothelial dysfunction induced by beta-amyloid peptide. JOURNAL OF CEREBRAL BLOOD FLOW AND METABOLISM, 36(2), 405-412. doi:10.1177/0271678X15610134
H-1, N-15 and C-13 assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques (Journal article)
Davies, H. A., Phelan, M. M., & Madine, J. (2016). H-1, N-15 and C-13 assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques. BIOMOLECULAR NMR ASSIGNMENTS, 10(1), 75-77. doi:10.1007/s12104-015-9641-z
beta-amyloid Peptide-Induced Human Arteriole Endothelial Dysfunction is Attenuated by Nanoliposomes (Conference Paper)
Guzman-Villanueva, D., Madine, J., Truran, S., Davies, H., Burciu, C., Franco, D., . . . Migrino, R. (2015). beta-amyloid Peptide-Induced Human Arteriole Endothelial Dysfunction is Attenuated by Nanoliposomes. In FASEB JOURNAL Vol. 29. Retrieved from http://gateway.webofknowledge.com/
Comparisons with Amyloid-beta Reveal an Aspartate Residue That Stabilizes Fibrils of the Aortic Amyloid Peptide Medin (Journal article)
Davies, H. A., Madine, J., & Middleton, D. A. (2015). Comparisons with Amyloid-beta Reveal an Aspartate Residue That Stabilizes Fibrils of the Aortic Amyloid Peptide Medin. JOURNAL OF BIOLOGICAL CHEMISTRY, 290(12), 7791-7803. doi:10.1074/jbc.M114.602177
Oxidative Stress Alters the Morphology and Toxicity of Aortic Medial Amyloid (Journal article)
Davies, H. A., Phelan, M. M., Wilkinson, M. C., Migrino, R. Q., Truran, S., Franco, D. A., . . . Madine, J. (2015). Oxidative Stress Alters the Morphology and Toxicity of Aortic Medial Amyloid. BIOPHYSICAL JOURNAL, 109(11), 2363-2370. doi:10.1016/j.bpj.2015.10.034
2013
Heparin Promotes the Rapid Fibrillization of a Peptide with Low Intrinsic Amyloidogenicity (Journal article)
Madine, J., Davies, H. A., Hughes, E., & Middleton, D. A. (2013). Heparin Promotes the Rapid Fibrillization of a Peptide with Low Intrinsic Amyloidogenicity. BIOCHEMISTRY, 52(50), 8984-8992. doi:10.1021/bi401231u
Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample (Journal article)
Middleton, D. A., Madine, J., Castelletto, V., & Hamley, I. W. (2013). Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 52(40), 10537-10540. doi:10.1002/anie.201301960
2012
Insights into the aggregation pathway of α-synuclein (Chapter)
Madine, J. (2012). Insights into the aggregation pathway of α-synuclein. In Amyloids: Composition, Functions and Pathology (pp. 149-162).
Fibrils and nanotubes assembled from a modified amyloid-beta peptide fragment differ in the packing of the same beta-sheet building blocks (Journal article)
Madine, J., Davies, H. A., Shaw, C., Hamley, I. W., & Middleton, D. A. (2012). Fibrils and nanotubes assembled from a modified amyloid-beta peptide fragment differ in the packing of the same beta-sheet building blocks. CHEMICAL COMMUNICATIONS, 48(24), 2976-2978. doi:10.1039/c2cc17118j
Site-Specific Identification of an A ss Fibril-Heparin Interaction Site by Using Solid-State NMR Spectroscopy (Journal article)
Madine, J., Pandya, M. J., Hicks, M. R., Rodger, A., Yates, E. A., Radford, S. E., & Middleton, D. A. (2012). Site-Specific Identification of an A ss Fibril-Heparin Interaction Site by Using Solid-State NMR Spectroscopy. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 51(52), 13140-13143. doi:10.1002/anie.201204459
Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin (Journal article)
Davies, H. A., Madine, J., & Middleton, D. A. (2012). Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin. JOURNAL OF PEPTIDE SCIENCE, 18(1), 65-72. doi:10.1002/psc.1418
2011
Insights into the aggregation pathway of a-synuclein (Chapter)
Madine, J. (2011). Insights into the aggregation pathway of a-synuclein. In Amyloids: Composition, Functions and Pathology (pp. in press). New York: Nova Science Publishers.
2010
Comparison of aggregation enhancement and inhibition as strategies for reducing the cytotoxicity of the aortic amyloid polypeptide medin (Journal article)
Madine, J., & Middleton, D. A. (2010). Comparison of aggregation enhancement and inhibition as strategies for reducing the cytotoxicity of the aortic amyloid polypeptide medin. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 39(9), 1281-1288. doi:10.1007/s00249-010-0581-3
Measurement of multiple torsional angles from one-dimensional solid-state NMR spectra: application to the conformational analysis of a ligand in its biological receptor site (Journal article)
Edwards, R., Madine, J., Fielding, L., & Middleton, D. A. (2010). Measurement of multiple torsional angles from one-dimensional solid-state NMR spectra: application to the conformational analysis of a ligand in its biological receptor site. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 12(42), 13999-14008. doi:10.1039/c0cp00326c
2009
Inhibitors of protein aggregation and toxicity (Journal article)
Amijee, H., Madine, J., Middleton, D. A., & Doig, A. J. (2009). Inhibitors of protein aggregation and toxicity. BIOCHEMICAL SOCIETY TRANSACTIONS, 37, 692-696. doi:10.1042/BST0370692
Cross-beta Spine Architecture of Fibrils Formed by the Amyloidogenic Segment NFGSVQFV of Medin from Solid-State NMR and X-ray Fiber Diffraction Measurements (Journal article)
Madine, J., Copland, A., Serpell, L. C., & Middleton, D. A. (2009). Cross-beta Spine Architecture of Fibrils Formed by the Amyloidogenic Segment NFGSVQFV of Medin from Solid-State NMR and X-ray Fiber Diffraction Measurements. BIOCHEMISTRY, 48(14), 3089-3099. doi:10.1021/bi802164e
Evaluation of beta-Alanine- and GABA-Substituted Peptides as Inhibitors of Disease-Linked Protein Aggregation (Journal article)
Madine, J., Wang, X., Brown, D. R., & Middleton, D. A. (2009). Evaluation of beta-Alanine- and GABA-Substituted Peptides as Inhibitors of Disease-Linked Protein Aggregation. CHEMBIOCHEM, 10(12), 1982-1987. doi:10.1002/cbic.200900219
Exploiting a C-13-labelled heparin analogue for in situ solid-state NMR investigations of peptide-glycan interactions within amyloid fibrils (Journal article)
Madine, J., Clayton, J. C., Yates, E. A., & Middleton, D. A. (2009). Exploiting a C-13-labelled heparin analogue for in situ solid-state NMR investigations of peptide-glycan interactions within amyloid fibrils. ORGANIC & BIOMOLECULAR CHEMISTRY, 7(11), 2414-2420. doi:10.1039/b820808e
TARGETING alpha-SYNUCLEIN AGGREGATION FOR PARKINSON'S DISEASE TREATMENT (Journal article)
Madine, J., & Middleton, D. A. (2009). TARGETING alpha-SYNUCLEIN AGGREGATION FOR PARKINSON'S DISEASE TREATMENT. DRUGS OF THE FUTURE, 34(8), 655-663. doi:10.1358/dof.2009.034.08.1391472
Targeting alpha-synuclein aggregation for Parkinson's disease treatement (Journal article)
Madine, J., & Middleton, D. A. (2009). Targeting alpha-synuclein aggregation for Parkinson's disease treatement. Drugs of the Future, 34(8), 655. doi:10.1358/dof.2009.034.08.1391472
2008
Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR (Journal article)
Madine, J., Doig, A. J., & Middleton, D. A. (2008). Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR. J. Am. Chem. Soc., 130(7873-7).
Membrane interactions of peptides representing the polybasic regions of three Rho GTPases are sensitive to the distribution of arginine and lysine residues (Journal article)
Jack, E. R., Madine, J., Lian, L. -Y., & Middleton, D. A. (2008). Membrane interactions of peptides representing the polybasic regions of three Rho GTPases are sensitive to the distribution of arginine and lysine residues. MOLECULAR MEMBRANE BIOLOGY, 25(1), 14-22. doi:10.1080/09687680701494007
Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20-29 of Amylin Revealed by Solid-State NMR and X-ray Fiber Diffraction (Journal article)
Madine, J., Jack, E., Stockley, P. G., Radford, S. E., Serpell, L. C., & Middleton, D. A. (2008). Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20-29 of Amylin Revealed by Solid-State NMR and X-ray Fiber Diffraction. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 130(45), 14990-15001. doi:10.1021/ja802483d
The effects of -synuclein on phospholipid vesicle integrity: a study using 31P NMR and electron microscopy (Journal article)
Madine, J., Hughes, E., Doig, A. J., & Middleton, D. A. (2008). The effects of -synuclein on phospholipid vesicle integrity: a study using 31P NMR and electron microscopy. MOLECULAR MEMBRANE BIOLOGY, 25(6-7), 518-527. doi:10.1080/09687680802467977
2006
A study of the regional effects of alpha-synuclein on the organization and stability of phospholipid bilayers (Journal article)
Madine, J., Doig, A. J., & Middleton, D. A. (2006). A study of the regional effects of alpha-synuclein on the organization and stability of phospholipid bilayers. BIOCHEMISTRY, 45(18), 5783-5792. doi:10.1021/bi052151q
An NMR strategy for obtaining multiple conformational constraints for N-15-C-13 spin-pair labelled organic solids (Journal article)
Madine, J., & Middleton, D. A. (2006). An NMR strategy for obtaining multiple conformational constraints for N-15-C-13 spin-pair labelled organic solids. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 8(44), 5223-5228. doi:10.1039/b610014g
2005
Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment. (Journal article)
Madine, J., Doig, A. J., Kitmitto, A., & Middleton, D. A. (2005). Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment.. Biochemical Society transactions, 33(Pt 5), 1113-1115. doi:10.1042/bst20051113
Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment (Journal article)
Madine, J., Doig, A. J., Kitmitto, A., & Middleton, D. A. (2005). Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment. BIOCHEMICAL SOCIETY TRANSACTIONS, 33, 1113-1115. doi:10.1042/BST0331113
2004
Screening molecular associations with lipid membranes using natural abundance C-13 cross-polarization magic-angle spinning NMR and principal component analysis (Journal article)
Middleton, D. A., Hughes, E., & Madine, J. (2004). Screening molecular associations with lipid membranes using natural abundance C-13 cross-polarization magic-angle spinning NMR and principal component analysis. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 126(31), 9478-9479. doi:10.1021/ja048226f
Screening molecular associations with lipid membranes using natural abundance 13C cross-polarization magic-angle spinning NMR and principal component analysis. (Journal article)
Middleton, D. A., Hughes, E., & Madine, J. (2004). Screening molecular associations with lipid membranes using natural abundance 13C cross-polarization magic-angle spinning NMR and principal component analysis.. Journal of the American Chemical Society, 126(31), 9478-9479. doi:10.1021/ja048226f
The aggregation and membrane-binding properties of an alpha-synuclein peptide fragment (Journal article)
Madine, J., Doig, A. J., & Middleton, D. A. (2004). The aggregation and membrane-binding properties of an alpha-synuclein peptide fragment. BIOCHEMICAL SOCIETY TRANSACTIONS, 32, 1127-1129. doi:10.1042/BST0321127