- Sabato D'Auria, CNR
- Chris Grant, University of Manchester
- John Honek, University of Waterloo
- Albert Jeltsch, Universität Stuttgart
- Tom Rowles, BioMed Central
An isolated form of N-terminal acidic extension of Heparin cofactor II (HCII 1-75) binds thrombin with a higher affinity than glycosaminoglycans (GAGs), suggesting that this region of Heparin cofactor II (HCII) is required for binding of thrombin exosite 1.
RTKB2 kinase from the unicellular choanoflagellate Monosiga brevicollis demonstrates regulatory functions as complex as those performed by mammalian receptor tyrosine kinases (RTKs), showing that complex signal transduction circuitry predates the evolution of metazoans.
Arginine-188 of the plant sucrose uptake transporter OsSUT1 is required for substrate translocation but not interaction, implicating the involvement of an alternative substrate binding site in substrate recognition.
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BMC Biochemistry 2011, 12:58
BMC Biochemistry is an open access, peer-reviewed journal that considers articles on all aspects of biochemical processes, including the structure, function and dynamics of metabolic pathways, supramolecular complexes, enzymes, proteins, nucleic acids and small molecular components of organelles, cells and tissues.
It is journal policy to publish work deemed by peer reviewers to be a coherent and sound addition to scientific knowledge and to put less emphasis on interest levels, provided that the research constitutes a useful contribution to the field.
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Section Editor's profile
John F. Honek is currently Professor and Chair of the Department of Chemistry at the University of Waterloo, Ontario, Canada.
Dr. Honek’s laboratory focuses on the structure and function of enzymes involved in methionine biochemistry, the Glyoxalase metalloenzymes and several protein targets of potential importance in medicinal chemistry. Recently Dr. Honek’s group has extended their investigations to the application of multisubunit protein systems to bionanomaterial fabrication.
"BMC Biochemistry is an important publication outlet for useful biochemistry research. The journal was created to provide an open access forum for leading edge investigations and provides freely available literature to the scientific community. This open forum provides anyone, regardless of their professional associations or financial capabilities, immediate access to world-class research investigations in biochemistry. We believe this accessible knowledge will stimulate many new ideas for future biochemical research among scientists throughout the world."