Browse By Publication: Biological Chemistry
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Number of items: 15.
Batra, Jyotsna, O’Mara, Tracy, Patnala, Radhika, Lose, Felicity, & Clements, Judith A. (2012) Genetic polymorphisms in the human tissue kallikrein (KLK) locus and their implication in various malignant and non-malignant diseases. Biological Chemistry, 393(12), pp. 1365-1390.
Clements, Judith, Hooper, John D., Dong, Ying, & Harvey, Tracey (2005) The Expanded Human Kallikrein (KLK) gene family : genomic organisation, tissue specific expression and potential functions. Biological Chemistry, 382(1), pp. 5-14.
Clements, Judith A. (2008) Reflections on the tissue kallikrein and kallikrein-related peptidase family - from mice to men - what have we learnt in the last two decades? Biological Chemistry, 389(12), pp. 1447-1454.
De Veer, Simon J., Swedberg, Joakim E., Parker, Edward A., & Harris, Jonathan M. (2012) Non-combinatorial library screening reveals subsite cooperativity and identifies new high-efficiency substrates for kallikrein-related peptidase 14. Biological Chemistry, 393(5), pp. 331-341.
Dong, Ying, Harrington, Brittney S., Adams, Mark N., Wortmann, Andreas, Stephenson, Sally-Anne, Lisle, Jessica E., et al. (2014) Activation of membrane-bound proteins and receptor systems: A link between tissue kallikrein and the KLK-related peptidases. Biological Chemistry, 395(9), pp. 977-990.
Dong, Ying, Matigian, Nick, Harvey, Tracey J., Samaratunga, Hemamali, Hooper, John D., & Clements, Judith A. (2008) Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function. Biological Chemistry, 389(2), pp. 99-109.
Lai, John, An, Jiyuan, Nelson, Colleen C., Lehman, Melanie L., Batra, Jyotsna, & Clements, Judith A. (2014) Analysis of androgen and anti-androgen regulation of KLK-related peptidase 2, 3, and 4 alternative transcripts in prostate cancer. Biological Chemistry, 395(9), pp. 1127-1132.
Lai, John, An, Jiyuan, Srinivasan, Srilakshmi, Clements, Judith A., & Batra, Jyotsna (2016) A computational analysis of the genetic and transcript diversity at the kallikrein locus. Biological Chemistry. (In Press)
Lose, Felicity, Lawrence, Mitchell Graham, Srinivasan, Srilakshmi, O'Mara, Tracy, Marquart, Louise, Chambers, Suzanne, et al. (2012) Kallikrein 14 is down-regulated by androgen receptor signalling and harbours genetic variation that is associated with prostate tumour aggressiveness. Biological Chemistry, 393(5), pp. 403-412.
Lundwall, Ake, Band, Vimla, Blaber, Michael, Clements, Judith, Courty, Yves, Diamandis, Eleftherios, et al. (2006) A comprehensive nomenclature for serine proteases with homology to tissue kallikreins. Biological Chemistry, 387(6), pp. 637-641.
Ramsay, Andrew J., Reid, Janet C., Adams, Mark N., Samaratunga, Hemamali, Dong, Ying, Clements, Judith A., et al. (2008) Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs). Biological Chemistry, 389(6), pp. 653-668.
Reid, Janet C., Bennett, Nigel C., Stephens, Carson R., Carroll, Mekanie L., Magdolen, Viktor, Clements, Judith A., et al. (2016) In vitro evidence that KLK14 regulates the components of the HGF/Met axis, pro-HGF and HGF-activator inhibitor 1A and 1B. Biological Chemistry. (In Press)
Tan, Olivia, Whitbread, Astrid, Clements, Judith, & Dong, Ying (2006) Kallikrein-Related Peptidase (KLK) family mRNA variants and protein isoforms in hormone-related cancers : do they have a function? Biological Chemistry, 387(6), pp. 697-705.
Whitbread, Astrid, Veveris-Lowe, Tara, Lawrence, Mitchell, Nicol, David, & Clements, Judith (2006) The role of kallikrein-related peptidases in prostate cancer : potential involvement in an epithelial to mesenchymal transition. Biological Chemistry, 387(6), pp. 707-714.
de Veer, Simon J., Swedberg, Joakim E., Brattsand, Maria, Clements, Judith A., & Harris, Jonathan M. (2016) Exploring the active site binding specificity of kallikrein-related peptidase 5 (KLK5) guides the design of new peptide substrates and inhibitors. Biological Chemistry. (In Press)