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Biochemistry|May 12, 1992
Anion binding by human lactoferrin: results from crystallographic and physicochemical studiesM S Shongwe, C A Smith, E W Ainscough, et al.
Biochemistry|October 7, 1998
Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrinP D Jeffrey, M C Bewley, R T MacGillivray, et al.
Structure (London, England : 1993)|December 24, 1998
Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenasesS A Moore, H M Baker, T J Blythe, et al.
FEBS Letters|February 24, 1992
Human melanotransferrin (p97) has only one functional iron-binding siteE N Baker, H M Baker, C A Smith, et al.
Chemical Communications (Cambridge, England)|January 14, 2017
Harnessing ester bond chemistry for protein ligationP G Young, Y Yosaatmadja, P W R Harris, et al.
Journal of Molecular Biology|September 21, 2001
The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin bindingS A Moore, R L Kingston, K M Loomes, et al.
FEBS Letters|July 26, 2000
A direct photo-activated affinity modification of tetracycline transcription repressor protein TetR(D) with tetracycline(1)M M Beliakova, M M Anokhina, V A Spiridonov, et al.
Biopolymers|January 29, 2016
Total Chemical Synthesis of an Orf Virus Protein, ORFV002, an Inhibitor of the Master Gene Regulator NF-κBS J Son, P W R Harris, C J Squire, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 26, 2001
Expression, crystallization and preliminary characterization of methylmalonyl coenzyme A epimerase from Propionibacterium shermaniiA A McCarthy, H M Baker, S C Shewry, et al.
Biochemistry|May 1, 2001
Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrinD Nurizzo, H M Baker, Q Y He, et al.
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