Brian C Bryksa
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Explore the profile of Brian C Bryksa including associated specialties, affiliations and a list of published articles.
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15
Citations
106
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Recent Articles
1.
Grahame D, Dupuis J, Bryksa B, Tanaka T, Yada R
Enzyme Microb Technol
. 2021 Sep;
150:109871.
PMID: 34489030
The present study sought to identify the structural determinants of aspartic protease structural stability and activity at elevated pH. Various hypotheses have been published regarding the features responsible for the...
2.
Grahame D, Dupuis J, Bryksa B, Tanaka T, Yada R
Enzyme Microb Technol
. 2020 Oct;
141:109632.
PMID: 33051007
Pepsin, the archetypal pepsin-like aspartic protease, is irreversibly denatured when exposed to neutral pH conditions whereas renin, a structural homologue of pepsin, is fully stable and optimally active in the...
3.
Zhao X, Tian J, Yu H, Bryksa B, Dupuis J, Ou X, et al.
J Biol Chem
. 2020 Jul;
295(43):14548-14562.
PMID: 32651232
In plants, many natural defense mechanisms include cellular membrane fusion as a way to resist infection by external pathogens. Several plant proteins mediate membrane fusion, but the detailed mechanism by...
4.
Cheung L, Dupuis J, Dee D, Bryksa B, Yada R
Trends Plant Sci
. 2020 Jun;
25(7):682-694.
PMID: 32526173
Ubiquitously expressed in plants, the plant-specific insert (PSI) of typical plant aspartic proteases (tpAPs) has been associated with plant development, stress response, and defense processes against invading pathogens. Despite sharing...
5.
Bryksa B, Yada R
Sci Rep
. 2017 Dec;
7(1):16911.
PMID: 29208977
Many plant aspartic proteases contain a saposin-like domain whose principal functions are intracellular sorting and host defence. Its structure is characterised by helical segments cross-linked by three highly conserved cystines....
6.
Bryksa B, Grahame D, Yada R
Biochim Biophys Acta Biomembr
. 2017 Feb;
1859(5):1008-1018.
PMID: 28212860
The present study characterized the aspartic protease saposin-like domains of four plant species, Solanum tuberosum (potato), Hordeum vulgare L. (barley), Cynara cardunculus L. (cardoon; artichoke thistle) and Arabidopsis thaliana, in...
7.
Jaafar A, Xiao H, Dee D, Bryksa B, Bhaumik P, Yada R
Biochim Biophys Acta
. 2016 Jul;
1864(10):1356-62.
PMID: 27378574
Plasmepsin II is a malarial pepsin-like aspartic protease produced as a zymogen containing an N-terminal prosegment domain that is removed during activation. Despite structural similarities between active plasmepsin II and...
8.
Xiao H, Bryksa B, Bhaumik P, Gustchina A, Kiso Y, Yao S, et al.
Mol Biochem Parasitol
. 2014 Dec;
197(1-2):56-63.
PMID: 25447707
Plasmepsin V, a membrane-bound aspartic protease present in Plasmodium falciparum, is involved in the export of malaria parasite effector proteins into host erythrocytes and therefore is a potential target for...
9.
De Moura D, Bryksa B, Yada R
PLoS One
. 2014 Sep;
9(9):e104315.
PMID: 25188221
The plant-specific insert is an approximately 100-residue domain found exclusively within the C-terminal lobe of some plant aspartic proteases. Structurally, this domain is a member of the saposin-like protein family,...
10.
Bryksa B, Bhaumik P, Magracheva E, De Moura D, Kurylowicz M, Zdanov A, et al.
J Biol Chem
. 2011 Jun;
286(32):28265-75.
PMID: 21676875
Many plant aspartic proteases contain an additional sequence of ~100 amino acids termed the plant-specific insert, which is involved in host defense and vacuolar targeting. Similar to all saposin-like proteins,...