Publications

Külzer, S., Rug, M., Brinkman, K., Cannon, P., Cowman, A., Lingelbach, K., Blatch, G.L., Maier, A.G., and Przyborski, J.M. 2010. Parasite encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum infected erythrocyte. Cell. Microbiol. (doi:10.1111/j.1462-5822.2010.01477.x).

Pesce, E.-R. , Cockburn, I.L., Goble, J.L., Stephens, L.L., and Blatch, G.L. 2010. Malaria heat shock proteins: Drug targets that chaperone other drug targets. Infect. Disord. Drug Targets. 10: 147-157.

Setati, M.M., Prinsloo, E., Longshaw, V. M., Murray, P.A., Edgar, D.H., and Blatch, G.L. 2010. Leukemia inhibitory factor promotes Hsp90 association with STAT3 in mouse embryonic stem cells. IUBMB Life. 62: 61-66.

Goble, J.L., Adendorff, M.R., de Beer, T.A.P. Stephens, L.L., and Blatch, G.L. 2010. The malarial drug target Plasmodium falciparum 1-deoxy-D-xylulose-5-phosphate reductoisomerase (PfDXR): development of a 3-D model for identification of novel, structural and functional features and for inhibitor screening. Protein Pept. Lett. 17: 109-120.

Louw, C.A., Ludewig, M.H., and Blatch, G.L. 2010. Overproduction, purification and characterisation of Tbj1, a novel Type III Hsp40 from Trypanosoma brucei, the African sleeping sickness parasite. Prot. Exp. Purif. 69: 168-177.

Lawson, J.C., Blatch, G.L., and Edkins, A.L. 2009. Cancer stem cells in breast cancer and metastasis. Breast Cancer Res. Treat. 118: 241-254.

Modisakeng, K.W., Jiwaji, M., Robert, J., Amemiya, C.T., Dorrington, R.A., and Blatch, G.L. 2009. Isolation of a Latimeria menadoensis heat shock protein 70 (Lmhsp70) that has all the features of an inducible gene and encodes a functional molecular chaperone. Mol. Genet. Genom. 282: 185-196.

Mutorwa, M., Salisu, S., Blatch, G.L., Kenyon, C., and Kaye, P.T. 2009. 3-Substituted aniline as scaffolds for the construction of glutamine synthetase and DXP-reductoisomerase inhibitors. Synthetic Commun. 39: 2723-2736.

Pesce, E.-R., and Blatch, G.L. 2009. The Hsp40-Hsp70 chaperone machinery of Plasmodium falciparum. AJBR. 3: 154-163.

Longshaw, V.M., Stephens, L.L., Daniel, S., and Blatch, G.L. 2009. The TPR2B domain of the Hsp70/Hsp90 organizing protein (Hop) may contribute towards its dimerization. Protein Pept. Lett. 16: 402-407.

Zimmermann, R., and Blatch, G.L. 2009. A novel twist to protein secretion in eukaryotes. Trends Parasitol. 25: 147-150.

Prinsloo, E.A.G., Setati, M.M., and Blatch G.L. 2009. Chaperoning stem cells: a role for hear shock proteins in the regulation of embryonic stem cell self-renewal, maintenance and differentiation? BioEssays. 31:370-377.

Parfitt, D.A., Michael, G.J., Vermeulen, E., Prodromou, N.V., Webb, T.R., Gallo, J-M., Cheetham, M.E. Nicoll, W.S., Blatch, G.L., and Chapple, P. 2009. The ataxia protein sacsin is a functional cochaperone that that modifies the cellular fate of polyglutamine expanded ataxin-1. Hum. Mol. Genet. 18: 1556-1565.

Longshaw, V.M., Baxter, M., Prewitz, M., and Blatch, G.L. 2009. Knockdown of the co-chaperone Hop promotes extra-nuclear accumulation of STAT3 in mouse embryonic stem cells. Eur. J. Cell Biol. 88:153-166.

Gentz, P.M., Blatch, G.L., and Dorrington, R.A. 2009. Dimerisation of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent. FEBS J. 276: 695-706.

Birkholtz, L.-M., Blatch, G.L., Coetzer, T.L., Hoppe, H.C., Human, E., Morris, J.E., Ngcete, Z., Oldfield, L., Roth, R., Shonhai, A., Stephens L., and Louw, A.I. 2008. Heterologous expression of plasmodial proteins for structural studies and functional annotation. Malaria J. 7: 197 (doi:10.1186/1475-2875-7-197).

Pesce E.-R., Acharya P., Tatu U., Nicoll W. S., Shonhai A., Hoppe H. C., and Blatch, G.L. 2008. The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns. Int. J. Biochem. Cell Biol. 40: 2914-2926.

Zimmermann, R., and Blatch G.L. 2008. Chaperones. In: Offermanns, S. and Rosenthal, W, eds. Encyclopedia of Molecular Pharmacology. Springer (ISBN: 978-3-540-38921-7).

Shonhai, A., Botha, M., de Beer, T.A.P., Boshoff, A., and Blatch, G.L. 2008. Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses. Protein and Peptide Letters. 15: 1117-1125.

Gordon AK, Blatch GL, Daniel S, Muller WJ. 2008. Stress protein responses in South African freshwater invertebrates exposed to detergent surfactant linear alkylbenzene sulfonate (LAS). Water Air Soil Pollut. 193: 123-130.

Daniel, S., Bradley, G., Longshaw, V., Söti, C., Csermely, P., and Blatch, G.L. 2008. Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding. BBA Mol Cell Res. 1783: 1003-1014.

Boshoff, A., Stephens, L.L., and Blatch G.L. 2008. The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state, and chaperone properties. Int. J. Biochem. Cell Biol. 40: 804-812.

Botha, M., Pesce, E.-R., and Blatch G.L. (2007) The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. Int. J. Biochem. Cell Biol. 39: 1781-1803.

Shonhai, A., Boshoff, A., and Blatch, G.L. (2007) The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum. Protein Science. 16: 1803-1818.

Nicoll, W.S., Botha, M., McNamara, C., Schlange, M., Pesce, E., Boshoff, A., Ludewig, M.H., Zimmermann, R., Cheetham, M.E., Chapple, J.P., and Blatch, G.L. (2007) Cytosolic and ER J-domains of mammalian and parasite origin can interact with DnaK. Int. J. Biochem. Cell Biol. 39: 736-751.

Csermely, P., Söti, C., and Blatch, G.L. (2007) Chaperones as parts of cellular networks. In: Csermely, P. and Vígh L., eds. Molecular aspects of the stress response: chaperones, membranes and networks, Advances in Experimental Medicine and Biology vol. 594. Austin: Landes Bioscience; New York: Springer Science+Business Media, 55-63 (publication date 27-11-06; ISBN: 0-387-39974-7)

Daniel, S., Söti, C., Csermely, P., Bradley, G., and Blatch, G.L. (2007) Hop: an Hsp70/90co-chaperone that functions within and beyond Hsp70-Hsp90 protein folding pathways. In: Blatch G.L., ed. Networking of Chaperones by Co-Chaperones. Austin: Landes Bioscience; New York: Springer Science + Business Media, 26-37 (publication date 04-12-06; ISBN: 978-0-387-49308-4).

Modisakeng, K.W., Amemiya, C.T., Dorrington, R.A., and Blatch, G.L. (2006) Molecular Biology studies on the coelacanth: a review. Special Coelacanth Issue of S. Afr. J. Sci. 102: 479-485.

Longshaw, V.M., Nicoll, W.S. , Botha, M., Ludewig, M.H., Shonhai, A., Stephens, L.L., and Blatch G.L. (2006) Getting practical with molecular chaperones. Biotechnology International. 18: 24-27

Nicoll, W.S., Boshoff, A., Ludewig, M.H., Hennessy, F., Jung, M., and Blatch, G.L. (2006) Approaches to the isolation and characterization of molecular chaperones. Prot. Exp. Purif. 46: 1-15.

Sinclair, B.J., Terblanche, J.S., Scott, M.B., Blatch, G.L., Klok, J., and Chown, S.L. (2006) Environmental physiology of three species of collembola at Cape Hallett, North Victoria Land, Antarctica. Journal of Insect Physiology. 52: 29-52.

Shonhai, S., Boshoff, A., and Blatch, G.L. (2005) Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain. Mol Genet Genom. 274: 70-78.

Hennessy, F., Nicoll, W.S., Zimmermann, R., Cheetham, M.E., and Blatch, G.L. (2005) Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Science. 14: 1697-1709.

Hennessy, F., Boshoff, A., and Blatch, G.L. (2005) Rational mutagenesis of the J domain identifies residues critical to the in vivo function of the Agrobacterium tumefaciens DnaJ. Int. J. Biochem. Cell Biol. 37: 177-191.

Modisakeng, K.W., Dorrington, R.A., Blatch, G.L. (2004) Isolation of genes encoding heat shock protein 70 (hsp70s) from the coelacanth, Latimeria chalumnae. Special Rhodes University Centenary Issue of S. Afr. J. Sci. 100: 683-686.

Limson, J., Odunuga, O.O., Green, H., Höök, F., and Blatch G.L. (2004) The use of Quartz Crystal Microbalance with Dissipation (QCM-D) for the measurement of protein-protein interactions: a qualitative and quantitative analysis of the interactions between molecular chaperones. Special Rhodes University Centenary Issue of S. Afr. J. Sci. 100: 678-682.

Boshoff, A., Nicoll, W.S., Hennessy, F., Ludewig, M.H., Daniel, S., Modisakeng, K.W., Shonhai, A., McNamara, C., Bradley, G., and Blatch. G.L. (2004) Molecular chaperones in biology, medicine and protein biotechnology. Special Rhodes University Centenary Issue of S. Afr. J. Sci. 100: 665-677.

Boshoff, A., Hennessy, F., and Blatch, G.L. (2004) The in vivo and in vitro characterization of DnaK from Agrobacterium tumefaciens RUOR. Prot. Exp. Purif. 38: 161-169.

Odunuga, O.O., Longshaw, V.M., and Blatch, G.L. (2004) Hop: more than an Hsp70/Hsp90 adaptor protein. BioEssays. 26: 1058-1068.

Edkins, A.L., Ludewig, M.H., and Blatch G.L. (2004) A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40. Int. J. Biochem. Cell Biol. 36: 1585-1598.

Longshaw, V.M., Chapple, J.P., Balda, M.S., Cheetham, M.E. and Blatch, G.L. (2004) The nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases. J. Cell Sci. 117:701-710

Matambo, T.S., Odunuga, O.O., Boshoff, A., and Blatch, G.L. (2004) Over-production, purification and characterization of the Plasmodium falciparum heat shock protein 70. Prot.Exp.Purif. 33: 214-222

Odunuga, O.O., Hornby, J.A., Bies, C., Zimmerman, R., Pugh, D.J. and Blatch, G.L. (2003) Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction: molecular characterization of the critical contacts for successful binding and specificity. J. Biol. Chem. 278: 6896-6904.