Biophysical Characterization of NleD: An effector protein from Escherichia coli O157:H7
Explore this paper's citation graph
Summary
The approach for improving the stability of the enzyme might facilitate its crystallization for structural work, while further mutagenesis studies may help identify the role of active site residues involved in catalysis.
- Type
- dissertation
- Published
- 2012-09-14
- Cited by
- 0
- References
- 75
- Access
- Open access
- OpenAlex
- https://openalex.org/W16358628
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:81919936
Keywords
Escherichia coli, Effector, Biochemistry, Active site, Biology
References
- An infrared and circular dichroism combined approach to the analysis of protein secondary structure.
- Size-exclusion chromatography.
- Dynamic Light Scattering: Applications of Photon Correlation Spectroscopy
- The stabilization of proteins by sucrose.
- A Brief Overview of Escherichia coli O157:H7 and Its Plasmid O157
- Metalloprotease type III effectors that specifically cleave JNK and NF‐κB
- Controlling injection: regulation of type III secretion in enterohaemorrhagic Escherichia coli.
- Pathogenic Escherichia coli
- Mass spectrometry for protein and peptide characterisation
- Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements.
- Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles.
- Arg(362) and Tyr(365) of the botulinum neurotoxin type a light chain are involved in transition state stabilization.
- Toward understanding tryptophan fluorescence in proteins.
- Use of high-speed size-exclusion chromatography for the study of protein folding and stability.
- Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions.
- Study of thermally and chemically unfolded conformations of bovine serum albumin by means of dynamic light scattering
- Molecular mechanisms of Escherichia coli pathogenicity
- Thermal Stability of Proteins
- Regulation and function of the JNK subgroup of MAP kinases.
- Application of dynamic light scattering to studies of protein folding kinetics
Cited by
No citing papers recorded for this paper.
Related papers
- Functional Characterization of the C-Terminus of YhaV in the Escherichia coli PrlF-YhaV Toxin-Antitoxin System.
- Characterisation of preYvaY export reveals differences in the substrate specificities of Bacillus subtilis and Escherichia coli leader peptidases.
- Switch of regulatory domains of P--protein and T--protein from E. coli
- X-Ray Structure and Site-Directed Mutagenesis Analysis of the Escherichia coli Colicin M Immunity Protein
- Characterization of a Hemoglobin Protease Secreted by the Pathogenic Escherichia coli Strain EB1
- EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli
- Evaluating the role of conserved amino acids in bacterial O-oligosaccharyltransferases by in vivo, in vitro and limited proteolysis assays.
- Site-specific proteolysis of the Escherichia coli SecA protein in vivo
- Secretion and processing of ribose-binding protein in Escherichia coli