Publications in 2009

Journal Articles

• Specificity versus catalytic potency: The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis.(Show details)
  

  Year:	2009
  Journal:	Biochimie
  Volume:	91
  Issue:	8
  Page numbers:	1036-44
  Author(s):
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• Specificity versus catalytic potency: The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis.(Show details)
  

  Year:	2009
  Journal:	Biochimie
  Volume:	91
  Issue:	8
  Page numbers:	1036-44
  Author(s):
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Publications in 2008

Journal Articles

• Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis

  (Show details)
  

  Year:	2008
  Journal:	Biochemical Journal
  Volume:	411
  Issue:	2
  Page numbers:	351-60
  Author(s):
  URL - restricted access	http://www.biochemj.org/bj/411/0351/bj4110351.htm
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• Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis

  (Show details)
  

  Year:	2008
  Journal:	Biochemical Journal
  Volume:	411
  Issue:	2
  Page numbers:	351-360
  Author(s):
  URL - restricted access	http://www.biochemj.org/bj/411/0351/bj4110351.htm
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• Conformationally constrained diketopimelic acid analogues as inhibitors of dihydrodipicolinate synthase(Show details)
  

  Year:	2008
  Journal:	Bioorganic and Medicinal Chemistry Letters
  Volume:	18
  Page numbers:	460-463
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• Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase. (Show details)
  

  Year:	2008
  Journal:	Protein Science
  Volume:	17
  Issue:	12
  Page numbers:	2080-90
  Author(s):
  URL - restricted access	http://www.ncbi.nlm.nih.gov/pubmed/18787203?ordinalpos=4&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum
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• Evolution of Quaternary Structure in a Homotetrameric Enzyme (Show details)
  

  Year:	2008
  Journal:	Journal of Molecular Biology
  Volume:	380
  Issue:	4
  Page numbers:	691-703
  Author(s):
  URL - restricted access	http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WK7-4SK07X4-5&_user=10&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=d6435c1ead9710cf6af1c431dc739e33
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• Federated repositories of X-ray diffraction images(Show details)
  

  Year:	2008
  Journal:	Acta Crystallographica Section D - Biological Crystallography
  Volume:	64
  Issue:	7
  Page numbers:	810-814
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• Inhibiting dihydrodipicolinate synthase across species: Towards specificity for pathogens?(Show details)
  

  Year:	2008
  Journal:	Bioorganic and Medicinal Chemistry Letters
  Volume:	18
  Page numbers:	842-844
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• Irreversible Inhibition of Dihydrodipicolinate Synthase by 4-oxo-heptenedioic acid analogues (Show details)
  

  Year:	2008
  Journal:	Bioorganic & Medicinal Chemistry
  Volume:	16
  Page numbers:	9975-9983
  Author(s):
  URL - open access	http://dx.doi.org/10.1016/j.bmc.2008.10.026
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• Mutating the tight-dimer interface of dihydrodipicolinate synthase disrupts the enzyme quaternary structure: toward a monomeric enzyme. (Show details)
  

  Year:	2008
  Journal:	Biochemistry
  Volume:	47
  Issue:	(46)
  Page numbers:	12108-17
  Author(s):
  URL - restricted access	http://www.ncbi.nlm.nih.gov/pubmed/18937497?ordinalpos=3&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum
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• Mutating the tight-dimer interface of dihydrodipicolinate synthase disrupts the enzyme quaternary structure: towards a monomeric enzyme.(Show details)
  

  Year:	2008
  Journal:	Biochemistry
  Volume:	47
  Page numbers:	12108-12117
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• Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen. (Show details)
  

  Year:	2008
  Journal:	Journal of Biological Chemistry
  Volume:	283
  Issue:	41
  Page numbers:	27598-27603
  Author(s):
  URL - restricted access	http://www.ncbi.nlm.nih.gov/pubmed/18684709?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum
  URL - restricted access	http://www.scopus.com.ezp.lib.unimelb.edu.au/scopus/record/display.url?fedsrfIntegrator=METALIB-SCOCIT&origin=fedsrf&view=basic&eid=2-s2.0-55549137411
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