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HMDB: the Human Metabolome Database
- D. Wishart, D. Tzur, +37 authors Lori Querengesser
- Biology, Computer Science
- Nucleic Acids Res.
- 1 January 2007
The Human Metabolome Database is designed to address the broad needs of biochemists, clinical chemists, physicians, medical geneticists, nutritionists and members of the metabolomics community. Expand
HMDB: a knowledgebase for the human metabolome
The most recent release of HMDB has been significantly expanded and enhanced over the previous release, with the number of fully annotated metabolite entries growing from 2180 to more than 6800, a 300% increase. Expand
Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs.
A structural approach is used in this review to examine the diversity of family members, and a biophysical perspective provides insight into the ability of the EF-hand motif to bind Ca2+ with a wide range of affinities. Expand
The expanding scope of antimicrobial peptide structures and their modes of action.
Several intact proteins or protein fragments are now being shown to have inherent antimicrobial activity, suggesting a better understanding of the structure-activity relationships of AMPs is required to facilitate the rational design of novel antimicrobial agents. Expand
Diversity of antimicrobial peptides and their mechanisms of action.
It is not likely that this diverse group of peptides has a single mechanism of action, but interaction of the peptides with membranes is an important requirement for most, if not all, antimicrobial peptides. Expand
Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.
In this review, the structures of a number of different Trp- and Arg-rich antimicrobial peptides are examined and some of the major mechanistic studies are presented. Expand
Structural biology of bacterial iron uptake.
Examination of the current three-dimensional structures of the outer membrane receptors, PBPs, and ABC transporters provides an overview of the structural biology of iron uptake in bacteria. Expand
Calmodulin’s flexibility allows for promiscuity in its interactions with target proteins and peptides
Novel structures have recently been reported where the conformation of CaM is highly dissimilar to these globular complexes, in some instances with less than a full compliment of bound calcium ions, as well as novel stoichiometries. Expand
The Solution Structures of the Human β-Defensins Lead to a Better Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus aureus *
- D. Schibli, H. Hunter, +5 authors H. Vogel
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 8 March 2002
The increased anti-Staphylococcalactivity of HBD3 may be explained by the capacity of the protein to form dimers in solution at low concentrations, an amphipathic dimer structure, and the increased positive surface charge compared with HBD1 and HBD2. Expand
Conformation of a Bactericidal Domain of Puroindoline a: Structure and Mechanism of Action of a 13-Residue Antimicrobial Peptide
A variety of biophysical and biochemical methods, including fluorescence spectroscopy and microcalorimetry, showed that puroA is located at the membrane interface, probably due to its high content of Trp residues that have a high propensity to partition into the membrane interfaces. Expand