J Andrew Aquilina
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Explore the profile of J Andrew Aquilina including associated specialties, affiliations and a list of published articles.
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Recent Articles
21.
Aquilina J
Proteins
. 2008 Oct;
75(2):478-85.
PMID: 18951409
Asymmetric dissociation of multiply charged protein assemblies has been frequently reported. This phenomenon, which relies on the dissociation of one or more highly charged monomers, has been shown to provide...
22.
Benesch J, Ayoub M, Robinson C, Aquilina J
J Biol Chem
. 2008 Aug;
283(42):28513-7.
PMID: 18713743
The alpha-crystallins are members of the small heat shock protein family of molecular chaperones that have evolved to minimize intracellular protein aggregation; however, they are also implicated in a number...
23.
Korlimbinis A, Aquilina J, Truscott R
Exp Eye Res
. 2007 Jun;
85(2):219-25.
PMID: 17574241
In human cataract lenses the UV filters, 3-hydroxykynurenine glucoside (3OHKG) and kynurenine (Kyn) were found to be covalently bound to proteins and the levels in the nucleus were much higher...
24.
Ahrman E, Lambert W, Aquilina J, Robinson C, Emanuelsson C
Protein Sci
. 2007 Jun;
16(7):1464-78.
PMID: 17567739
The molecular mechanism whereby the small heat-shock protein (sHsp) chaperones interact with and prevent aggregation of other proteins is not fully understood. We have characterized the sHsp-substrate protein interaction at...
25.
Korlimbinis A, Aquilina J, Truscott R
Invest Ophthalmol Vis Sci
. 2007 Mar;
48(4):1718-23.
PMID: 17389504
Purpose: To survey the levels of protein-bound UV filters in the cortices and nuclei of normal human lenses as a function of age and to relate this to the concentration...
26.
Stewart E, Aquilina J, Easterbrook-Smith S, Murphy-Durland D, Jacobsen C, Moestrup S, et al.
Biochemistry
. 2007 Jan;
46(5):1412-22.
PMID: 17260971
Clusterin is the first well characterized, constitutively secreted extracellular chaperone that binds to exposed regions of hydrophobicity on non-native proteins. It may help control the folding state of extracellular proteins...
27.
Aquilina J, Watt S
Biochem Biophys Res Commun
. 2007 Jan;
353(4):1115-20.
PMID: 17207466
Alpha-crystallin, a major structural protein of the lens can also function as a molecular chaperone by binding to unfolding substrate proteins. We have used a combination of limited proteolysis at...
28.
Ecroyd H, Meehan S, Horwitz J, Aquilina J, Benesch J, Robinson C, et al.
Biochem J
. 2006 Aug;
401(1):129-41.
PMID: 16928191
AlphaB-crystallin is a member of the sHsp (small heat-shock protein) family that prevents misfolded target proteins from aggregating and precipitating. Phosphorylation at three serine residues (Ser19, Ser45 and Ser59) is...
29.
Benesch J, Aquilina J, Ruotolo B, Sobott F, Robinson C
Chem Biol
. 2006 Jun;
13(6):597-605.
PMID: 16793517
The application of mass spectrometry (MS) to the study of progressively larger and more complex macromolecular assemblies is proving increasingly useful for structural biologists. The scope of this approach has...
30.
Pepys M, Hirschfield G, Tennent G, Gallimore J, Kahan M, Bellotti V, et al.
Nature
. 2006 Apr;
440(7088):1217-21.
PMID: 16642000
Complement-mediated inflammation exacerbates the tissue injury of ischaemic necrosis in heart attacks and strokes, the most common causes of death in developed countries. Large infarct size increases immediate morbidity and...