Search Results - "Madan, Lalima L"
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The Crystal Structure of a Quercetin 2,3-Dioxygenase from Bacillus subtilis Suggests Modulation of Enzyme Activity by a Change in the Metal Ion at the Active Site(s)
Published in Biochemistry (Easton) (11-01-2005)“…Common structural motifs, such as the cupin domains, are found in enzymes performing different biochemical functions while retaining a similar active site…”
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PeptideMine--a webserver for the design of peptides for protein-peptide binding studies derived from protein-protein interactomes
Published in BMC bioinformatics (22-09-2010)“…Signal transduction events often involve transient, yet specific, interactions between structurally conserved protein domains and polypeptide sequences in…”
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Modulation of catalytic activity in multi-domain protein tyrosine phosphatases
Published in PloS one (13-09-2011)“…Signaling mechanisms involving protein tyrosine phosphatases govern several cellular and developmental processes. These enzymes are regulated by several…”
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4
Conformational Basis for Substrate Recruitment in Protein Tyrosine Phosphatase 10D
Published in Biochemistry (Easton) (22-11-2011)“…The coordinated activity of protein tyrosine phosphatases (PTPs) is crucial for the initiation, modulation, and termination of diverse cellular processes. The…”
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Inter-domain interactions influence the stability and catalytic activity of the bi-domain protein tyrosine phosphatase PTP99A
Published in Biochimica et biophysica acta (01-08-2012)“…The two protein tyrosine phosphatase (PTP) domains in bi-domain PTPs share high sequence and structural similarity. However, only one of the two PTP domains is…”
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6
Addition of a polypeptide stretch at the N-terminus improves the expression, stability and solubility of recombinant protein tyrosine phosphatases from Drosophila melanogaster
Published in Protein expression and purification (01-02-2008)“…The production of recombinant proteins in Escherichia coli involves substantial optimization in the size of the protein and over-expression strategies to avoid…”
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7
The Crystal Structure of a Quercetin 2,3-Dioxygenase from Bacillus subtilis Suggests Modulation of Enzyme Activity by a Change in the Metal Ion at the Active Site(s)
Published in Biochemistry (Easton) (10-11-2010)“…Common structural motifs, such as the cupin domains, are found in enzymes performing different biochemical functions while retaining a similar active site…”
Get full text
Journal Article