Christopher P Garnham
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Explore the profile of Christopher P Garnham including associated specialties, affiliations and a list of published articles.
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25
Citations
749
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Recent Articles
11.
Guo S, Garnham C, Partha S, Campbell R, Allingham J, Davies P
FEBS J
. 2013 Sep;
280(22):5919-32.
PMID: 24024640
A Ca(2+) -dependent 1.5-MDa antifreeze protein present in an Antarctic Gram-negative bacterium, Marinomonas primoryensis (MpAFP), has recently been reassessed as an ice-binding adhesin. The non-ice-binding region II (RII), one of...
12.
Liu Y, Garnham C, Roll-Mecak A, Tanner M
Bioorg Med Chem Lett
. 2013 Jun;
23(15):4408-12.
PMID: 23777780
Tubulin is subject to a reversible post-translational modification involving polyglutamylation and deglutamylation of glutamate residues in its C-terminal tail. This process plays key roles in regulating the function of microtubule...
13.
Guo S, Garnham C, Whitney J, Graham L, Davies P
PLoS One
. 2012 Nov;
7(11):e48805.
PMID: 23144980
A novel role for antifreeze proteins (AFPs) may reside in an exceptionally large 1.5-MDa adhesin isolated from an Antarctic Gram-negative bacterium, Marinomonas primoryensis. MpAFP was purified from bacterial lysates by...
14.
Garnham C, Nishimiya Y, Tsuda S, Davies P
FEBS Lett
. 2012 Sep;
586(21):3876-81.
PMID: 23017208
Type III antifreeze proteins (AFPs) can be sub-divided into three classes of isoforms. SP and QAE2 isoforms can slow, but not stop, the growth of ice crystals by binding to...
15.
Kondo H, Hanada Y, Sugimoto H, Hoshino T, Garnham C, Davies P, et al.
Proc Natl Acad Sci U S A
. 2012 May;
109(24):9360-5.
PMID: 22645341
Antifreeze proteins (AFPs) are found in organisms ranging from fish to bacteria, where they serve different functions to facilitate survival of their host. AFPs that protect freeze-intolerant fish and insects...
16.
Garnham C, Roll-Mecak A
Cytoskeleton (Hoboken)
. 2012 Mar;
69(7):442-63.
PMID: 22422711
Cellular microtubules are marked by abundant and evolutionarily conserved post-translational modifications that have the potential to tune their functions. This review focuses on the astonishing chemical complexity introduced in the...
17.
Garnham C, Campbell R, Walker V, Davies P
BMC Struct Biol
. 2011 Sep;
11:36.
PMID: 21951648
Background: Ice nucleation proteins (INPs) allow water to freeze at high subzero temperatures. Due to their large size (>120 kDa), membrane association, and tendency to aggregate, an experimentally-determined tertiary structure...
18.
Garnham C, Campbell R, Davies P
Proc Natl Acad Sci U S A
. 2011 Apr;
108(18):7363-7.
PMID: 21482800
The mechanism by which antifreeze proteins (AFPs) irreversibly bind to ice has not yet been resolved. The ice-binding site of an AFP is relatively hydrophobic, but also contains many potential...
19.
Garnham C, Natarajan A, Middleton A, Kuiper M, Braslavsky I, Davies P
Biochemistry
. 2010 Sep;
49(42):9063-71.
PMID: 20853841
By binding to the surface of ice crystals, type III antifreeze protein (AFP) can depress the freezing point of fish blood to below that of freezing seawater. This 7-kDa globular...
20.
Garnham C, Hanna R, Chou J, Low K, Gourlay K, Campbell R, et al.
Biochemistry
. 2009 Feb;
48(15):3457-67.
PMID: 19226146
Loss-of-function mutations in calpain 3 have been shown to cause limb-girdle muscular dystrophy type 2A (LGMD2A), an autosomal recessive disorder that results in gradual wasting of the muscles of the...