Publications for David Pattison
Publications for David Pattison
2016
Jonberg, S., Lund, M., Pattison, D., Skibsted, L.,
Davies, M. (2016). Competitive kinetics as a tool
to determine rate constants for reduction of
ferrylmyoglobin by food components. Food
Chemistry, 199, 36-41. <a
href="http://dx.doi.org/10.1016/j.foodchem.2015
.11.120">[More Information]</a>
Cook, N., Moeke, C., Fantoni, L., Pattison, D.,
Davies, M. (2016). The myeloperoxidase-derived
oxidant hypothiocyanous acid inhibits protein
tyrosine phosphatases via oxidation of key
cysteine residues. Free Radical Biology and
Medicine, 90, 195-205. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2015.11.025">[More Information]</a>
2015
Storkey, C., Pattison, D., Ignasiak, M., Schiesser,
C., Davies, M. (2015). Kinetics of reaction of
peroxynitrite with selenium- and
sulfur-containing compounds: Absolute rate
constants and assessment of biological
significance. Free Radical Biology and
Medicine, 89, 1049-1056. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2015.10.424">[More Information]</a>
Storkey, C., Pattison, D., Koehler, J., Gaspard,
D., Evans, J., Hagestuen, E., Davies, M. (2015).
Prevention of degradation of the natural high
potency sweetener (2R,4R)-monatin in mock
beverage solutions. Food Chemistry, 173,
645-651. <a
href="http://dx.doi.org/10.1016/j.foodchem.2014
.10.054">[More Information]</a>
Carroll, L., Davies, M., Pattison, D. (2015).
Reaction of low-molecular-mass organoselenium
compounds (and their sulphur analogues) with
inflammation-associated oxidants. Free Radical
Research, 49(6), 750-767. <a
href="http://dx.doi.org/10.3109/10715762.2015.
1018247">[More Information]</a>
Carroll, L., Pattison, D., Fu, S., Schiesser, C.,
Davies, M., Hawkins, C. (2015). Reactivity of
selenium-containing compounds with
myeloperoxidase-derived chlorinating oxidants:
Second-order rate constants and implications for
biological damage. Free Radical Biology and
Medicine, 84, 279-288. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2015.03.029">[More Information]</a>
2014
Gad, N., Mizdrak, J., Pattison, D., Davies, M.,
Truscott, R., Jamie, J. (2014). Detection,
quantification, and total synthesis of novel
3-hydroxykynurenine glucoside-derived
metabolites present in human lenses.
Investigative Ophthalmology & Visual Science,
55(2), 849-855. <a
href="http://dx.doi.org/10.1167/iovs.13-13464">
[More Information]</a>
Storkey, C., Pattison, D., Gaspard, D.,
Hagestuen, E., Davies, M. (2014). Mechanisms
of degradation of the natural high-potency
sweetener (2R,4R)-monatin in mock beverage
solutions. Journal of Agricultural and Food
Chemistry, 62(15), 3476-3487. <a
href="http://dx.doi.org/10.1021/jf404198w">[M
ore Information]</a>
Storkey, C., Davies, M., Pattison, D. (2014).
Reevaluation of the rate constants for the
reaction of hypochlorous acid (HOCl) with
cysteine, methionine, and peptide derivatives
using a new competition kinetic approach. Free
Radical Biology and Medicine, 73, 60-66. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2014.04.024">[More Information]</a>
Bonifay, V., Barrett, T., Pattison, D., Davies, M.,
Hawkins, C., Ashby, M. (2014). Tryptophan
oxidation in proteins exposed to
thiocyanate-derived oxidants. Archives of
Biochemistry and Biophysics, 564, 1-11. <a
href="http://dx.doi.org/10.1016/j.abb.2014.08.01
4">[More Information]</a>
2013
Morgan, P., Sheahan, P., Pattison, D., Davies, M.
(2013). Methylglyoxal-induced modification of
arginine residues decreases the activity of
NADPH-generating enzymes. Free Radical
Biology and Medicine, 61, 229-242. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2013.03.025">[More Information]</a>
Hadfield, K., Pattison, D., Brown, B., Hou, L.,
Rye, K., Davies, M., Hawkins, C. (2013).
Myeloperoxidase-derived oxidants modify
apolipoprotein A-I and generate dysfunctional
high-density lipoproteins: comparison of
hypothiocyanous acid (HOSCN) with
hypochlorous acid (HOCI). The Biochemical
Journal, 449(2), 531-542. <a
href="http://dx.doi.org/10.1042/BJ20121210">[
More Information]</a>
2012
Karton, A., O'Reilly, R., Pattison, D., Davies,
M., Radom, L. (2012). Computational design of
effective, bioinspired HOCI antioxidants: The
role of intramolecular C1(+) and H(+) shifts.
Journal of the American Chemical Society,
134(46), 19240-19245. <a
href="http://dx.doi.org/10.1021/ja309273n">[Mo
re Information]</a>
Talib, J., Pattison, D., Harmer, J., Celermajer, D.,
Davies, M. (2012). High plasma thiocyanate
Publications for David Pattison
levels modulate protein damage induced by
myeloperoxidase and perturb measurement of
3-chlorotyrosine. Free Radical Biology and
Medicine, 53(1), 20-29. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2012.04.018">[More Information]</a>
Barrett, T., Pattison, D., Leonard, S., Carroll, K.,
Davies, M., Hawkins, C. (2012). Inactivation of
thiol-dependent enzymes by hypothiocyanous
acid: role of sulfenyl thiocyanate and sulfenic
acid intermediates. Free Radical Biology and
Medicine, 52(6), 1075-1085. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2011.12.024">[More Information]</a>
Cook, N., Pattison, D., Davies, M. (2012).
Myeloperoxidase-derived oxidants rapidly
oxidize and disrupt zinc-cysteine/histidine
clusters in proteins. Free Radical Biology and
Medicine, 53(11), 2072-2080. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2012.09.033">[More Information]</a>
Pattison, D., Rahmanto, A., Davies, M. (2012).
Photo-oxidation of proteins. Photochemical and
Photobiological Sciences, 11(1), 38-53. <a
href="http://dx.doi.org/10.1039/c1pp05164d">[
More Information]</a>
Rahmanto, A., Pattison, D., Davies, M. (2012).
Photo-oxidation-induced inactivation of the
selenium-containing protective enzymes
thioredoxin reductase and glutathione
peroxidase. Free Radical Biology and Medicine,
53(6), 1308-1316. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2012.07.016">[More Information]</a>
Storkey, C., Pattison, D., White, J., Schiesser, C.,
Davies, M. (2012). Preventing Protein Oxidation
with Sugars: Scavenging of Hypohalous Acids
by 5-Selenopyranose and 4-Selenofuranose
Derivatives. Chemical Research in Toxicology,
25(11), 2589-2599. <a
href="http://dx.doi.org/10.1021/tx3003593">[M
ore Information]</a>
Morgan, P., Pattison, D., Davies, M. (2012).
Quantification of hydroxyl radical-derived
oxidation products in peptides containing
glycine, alanine, valine, and proline. Free
Radical Biology and Medicine, 52(2), 328-339.
<a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2011.10.448">[More Information]</a>
Pattison, D., Davies, M., Hawkins, C. (2012).
Reactions and reactivity of
myeloperoxidase-derived oxidants: Differential
biological effects of hypochlorous and
hypothiocyanous acids. Free Radical Research,
46(8), 975-995. <a
href="http://dx.doi.org/10.3109/10715762.2012.
667566">[More Information]</a>
Skaff, O., Pattison, D., Morgan, P., Bachana, R.,
Jain, V., Priyadarsini, I., Davies, M. (2012).
Selenium-containing amino acids are targets for
myeloperoxidase-derived hypothiocyanous acid:
determination of absolute rate constants and
implications for biological damage. The
Biochemical Journal, 441(1), 305-316. <a
href="http://dx.doi.org/10.1042/BJ20101762">[
More Information]</a>
Pattison, D., Lam, M., Shinde, S., Anderson, R.,
Davies, M. (2012). The nitroxide TEMPO is an
efficient scavenger of protein radicals: Cellular
and kinetic studies. Free Radical Biology and
Medicine, 53, 1664-1674. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2012.08.578">[More Information]</a>
2011
Morgan, P., Pattison, D., Talib, J., Summers, F.,
Harmer, J., Celermajer, D., Hawkins, C., Davies,
M. (2011). High plasma thiocyanate levels in
smokers are a key determinant of thiol oxidation
induced by myeloperoxidase. Free Radical
Biology and Medicine, 51(9), 1815-1822. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2011.08.008">[More Information]</a>
Pattison, D., O'Reilly, R., Skaff, O., Radom, L.,
Anderson, R., Davies, M. (2011). One-electron
Reduction of N-chlorinated and N-Brominated
Species Is a Source of Radicals and Bromine
Atom Formation. Chemical Research in
Toxicology, 24(3), 371-382. <a
href="http://dx.doi.org/10.1021/tx100325z">[Mo
re Information]</a>
2010
Stanley, N., Pattison, D., Hawkins, C. (2010).
Ability of Hypochlorous Acid and
N-Chloramines to Chlorinate DNA and Its
Constituents. Chemical Research in Toxicology,
23(7), 1293-1302. <a
href="http://dx.doi.org/10.1021/tx100188b">[M
ore Information]</a>
Koelsch, M., Mallak, R., Graham, G., Kajer, T.,
Milligan, M., Nguyen, L., Newsham, D., Keh, J.,
Kettle, A., Scott, K., Pattison, D., Hawkins, C.,
Davies, M., et al (2010). Acetaminophen
(paracetamol) inhibits
myeloperoxidase-catalyzed oxidant production
and biological damage at therapeutically
achievable concentrations. Biochemical
Pharmacology, 79(8), 1156-1164. <a
href="http://dx.doi.org/10.1016/j.bcp.2009.11.02
4">[More Information]</a>
Szuchman-Sapir, A., Pattison, D., Davies, M.,
Witting, P. (2010). Site-specific hypochlorous
acid-induced oxidation of recombinant human
myoglobin affects specific amino acid residues
and the rate of cytochrome b(5)-mediated heme
Publications for David Pattison
reduction. Free Radical Biology and Medicine,
48(1), 35-46. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2009.09.023">[More Information]</a>
2009
Skaff, O., Pattison, D., Davies, M. (2009).
Hypothiocyanous acid reactivity with
low-molecular-mass and protein thiols: absolute
rate constants and assessment of biological
relevance. Biochemical Journal, 422(1),
111-117. <a
href="http://dx.doi.org/10.1042/BJ20090276">[
More Information]</a>
Gracanin, M., Hawkins, C., Pattison, D., Davies,
M. (2009). Singlet-oxygen-mediated amino acid
and protein oxidation: formation of tryptophan
peroxides and decomposition products. Free
Radical Biology and Medicine, 47(1), 92-102. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2009.04.015">[More Information]</a>
Pattison, D., Hawkins, C., Davies, M. (2009).
What are the plasma targets of the oxidant
hypochlorous acid? A kinetic modeling
approach. Chemical Research in Toxicology,
22(5), 807-817. <a
href="http://dx.doi.org/10.1021/tx800372d">[M
ore Information]</a>
2008
Szuchman-Sapir, A., Pattison, D., Ellis, N.,
Hawkins, C., Davies, M., Witting, P. (2008).
Hypochlorous acid oxidizes methionine and
tryptophan residues in myoglobin. Free Radical
Biology and Medicine, 45(6), 789-798. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2008.06.010">[More Information]</a>
Davies, M., Hawkins, C., Pattison, D., Rees, M.
(2008). Mammalian heme peroxidases: from
molecular mechanisms to health implications.
Antioxidants & Redox Signaling, 10(7),
1199-1234. <a
href="http://dx.doi.org/10.1089/ars.2007.1927">
[More Information]</a>
Lam, M., Pattison, D., Bottle, S., Keddie, D.,
Davies, M. (2008). Nitric Oxide and Nitroxides
Can Act as Efficient Scavengers of
Protein-Derived Free Radicals. Chemical
Research in Toxicology, 21(11), 2111-2119. <a
href="http://dx.doi.org/10.1021/tx800183t">[Mo
re Information]</a>
Morgan, P., Pattison, D., Hawkins, C., Davies,
M. (2008). Separation, detection, and
quantification of hydroperoxides formed at
side-chain and backbone sites on amino acids,
peptides, and proteins. Free Radical Biology and
Medicine, 45(9), 1279-1289. <a
href="http://dx.doi.org/10.1016/j.freeradbiomed.
2008.08.004">[More Information]</a>
Skaff, O., Pattison, D., Davies, M. (2008). The
vinyl ether linkages of plasmalogens are favored
targets for myeloperoxidase-derived oxidants: a
kinetic study. Biochemistry, 47(31), 8237-8245.
<a
href="http://dx.doi.org/10.1021/bi800786q">[M
ore Information]</a>
Hawkins, C., Pattison, D., Stanley, N., Davies,
M. (2008). Tryptophan residues are targets in
hypothiocyanous acid-mediated protein
oxidation. Biochemical Journal, 416(3),
441-452. <a
href="http://dx.doi.org/10.1042/BJ20070941">[
More Information]</a>
2007
Hawkins, C., Pattison, D., Whiteman, M.,
Davies, M. (2007). Chlorination and nitration of
DNA and nucleic acid components. In Evans
M; Cooke M (Eds.), Oxidative Damage to
Nucleic Acids, (pp. 14-39). United States:
Springer.
Pattison, D., Hawkins, C., Davies, M. (2007).
Hypochlorous Acid-Mediated Protein Oxidation:
How Important Are Chloramine Transfer
Reactions and Protein Tertiary Structure?
Biochemistry, 46(34), 9853-9864. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17676767">[More Information]</a>
Skaff, O., Pattison, D., Davies, M. (2007).
Kinetics of hypobromous acid-mediated
oxidation of lipid components and antioxidants.
Chemical Research in Toxicology, 20(12),
1980-1988. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=18047295">[More Information]</a>
2006
Pattison, D., Davies, M. (2006). Actions of
ultraviolet light on cellular structures. EXS, 96,
131-157. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16383017">[More Information]</a>
Pattison, D., Davies, M. (2006). Evidence for
rapid inter- and intramolecular chlorine transfer
reactions of histamine and carnosine
chloramines: implications for the prevention of
hypochlorous-Acid-mediated damage.
Biochemistry, 45(26), 8152-8162. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16800640">[More Information]</a>
Pattison, D., Davies, M. (2006). Reactions of
myeloperoxidase-derived oxidants with
biological substrates: gaining chemical insight
into human inflammatory diseases. Current
Publications for David Pattison
Medicinal Chemistry, 13(27), 3271-3290. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17168851">[More Information]</a>
2005
Pattison, D., Davies, M. (2005). Histidine
side-chain chloramines are important
intermediates in HOCL-mediated protein
oxidation. 13th Biennial Meeting of the Society
for Free Radical Research, United Kingdom:
Taylor and Francis.
Pattison, D., Davies, M. (2005). Kinetic analysis
of the role of histidine chloramines in
hypochlorous acid mediated protein oxidation.
Biochemistry, 44(19), 7378-7387. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=15882077">[More Information]</a>
Rees, M., Pattison, D., Davies, M. (2005).
Oxidation of heparan sulphate by hypochlorite:
role of N-chloro derivatives and
dichloramine-dependent fragmentation.
Biochemical Journal, 391(Pt 1), 125-134. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=15932347">[More Information]</a>
2004
Pattison, D., Davies, M. (2004). Kinetic Analysis
Of The Reactions Of Hypobromous Acid With
Protein Components: Implications For Cellular
Damage And Use Of 3-Bromotyrosine As A
Marker Of Oxidative Stress. Biochemistry,
43(16), 4799-4809.
Levina, A., Foran, G., Pattison, D., Lay, P.
(2004). X-Ray Absorption Spectroscopic And
Electrochemical Studies Of Tris(Catecholato
(2-))Chromate (V/I V/Iii) Complexes.
Angewandte Chemie (International Edition),
43(4), 462-465. <a
href="http://dx.doi.org/10.1002/anie.200352418"
>[More Information]</a>
2003
Hawkins, C., Pattison, D., Davies, M. (2003).
Hypochlorite-induced oxidation of amino acids,
peptides and proteins. Amino Acids, 25(3-4),
259-274. <a
href="http://dx.doi.org/10.1007/s00726-003-001
6-x">[More Information]</a>
Pattison, D., Hawkins, C., Davies, M. (2003).
Hypochlorous Acid-Mediated Oxidation of Lipid
Components and Antioxidants Present in LowDensity Lipoproteins: Absolute Rate Constants,
Product Analysis, and Computational Modeling.
Chemical Research in Toxicology, 16(4),
439-449.
2002
Hawkins, C., Pattison, D., Davies, M. (2002).
Reaction of protein chloramines with DNA and
nucleosides: evidence for the formation of
radicals, protein-DNA cross-links and DNA
fragmentation. Biochemical Journal, 365(3),
605-615.
2001
Pattison, D., Levina, A., Lay, P., Davies, M.
(2001). An investigation of the chromium
oxidation state of a monoanionic chromium
tris(catecholate) complex by X-ray absorption
and EPR spectroscopies. Inorganic Chemistry,
40, 214-217.
Pattison, D., Levina, A., Lay, P., Davies, M.,
Dixon, N. (2001). Chromium(VI) reduction by
catechol(amine)s results in DNA cleavage in
vitro: Relevance to chromium genotoxicity.
Chemical Research in Toxicology, 14, 500-510.