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Versatility of Aminoglycosides and Prospects for Their Future
The most recent knowledge about the mechanism of aminoglycoside action and the mechanisms of resistance to these antibiotics are reviewed.
Matrix metalloproteinases: structures, evolution, and diversification
- I. Massova, L. Kotra, R. Fridman, S. Mobashery
- Biology, MedicineFASEB journal : official publication of the…
- 1 September 1998
Analysis indicates that a retrograde structure simplification may have accounted for the evolution of MMPs with simple domain constituents, such as matrilysin, from the larger and more elaborate enzymes.
Kinetic Analysis of the Binding of Human Matrix Metalloproteinase-2 and -9 to Tissue Inhibitor of Metalloproteinase (TIMP)-1 and TIMP-2*
- M. Olson, D. Gervasi, S. Mobashery, R. Fridman
- Chemistry, MedicineThe Journal of Biological Chemistry
- 21 November 1997
Investigation of surface plasmon resonance and enzyme inhibition studies demonstrate that TIMPs are slow binding inhibitors with monophasic inhibition kinetics, suggesting that a single binding event results in enzyme inhibition.
Kinship and Diversification of Bacterial Penicillin-Binding Proteins and β-Lactamases
The catalytic function of β-lactamases is the primary cause of bacterial resistance to β-lactam antibiotics (e.g., penicillins and cephalosporins). β-Lactamases show diversity in both structure and…
How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function
- L. H. Otero, A. Rojas-Altuve, +12 authors J. Hermoso
- Biology, MedicineProceedings of the National Academy of Sciences
- 1 October 2013
The identification of an allosteric binding domain—a remarkable 60 Å distant from the dd-transpeptidase active site—discovered by crystallographic analysis of a soluble construct of PBP2a opens an unprecedented realm for β-lactam antibiotic structure-based design.
Three-dimensional structure of the bacterial cell wall peptidoglycan.
- S. Meroueh, Krisztina Z. Bencze, +4 authors S. Mobashery
- Biology, MedicineProceedings of the National Academy of Sciences…
- 21 March 2006
The 3D solution structure as determined by NMR of the 2-kDa NAG-NAM(pentapeptide)-NAG-Nam(pentAPEptide) synthetic fragment of the cell wall is reported and a model for the bacterial cell wall has been proposed.
Cell surface association of matrix metalloproteinase-9 (gelatinase B)
- R. Fridman, M. Tóth, Irina Chvyrkova, S. Meroueh, S. Mobashery
- Biology, MedicineCancer and Metastasis Reviews
- 1 June 2003
Evidence shows that association of MMP-9 with the cell surface is mediated by a distinct array of surface proteins that serve to regulate multiple aspects of the enzyme function including localization, inhibition and internalization.
Discoidin Domain Receptors: Unique Receptor Tyrosine Kinases in Collagen-mediated Signaling*
- H. Fu, Rajeshwari R. Valiathan, +8 authors R. Fridman
- Biology, MedicineThe Journal of Biological Chemistry
- 18 January 2013
This minireview provides an overview of these areas of DDR research with the goal of fostering further investigation of these intriguing and unique receptors.
Bacterial Resistance to β‐Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity
Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2).
A novel mechanism of activation of progelatinase B mediated by gelatinase A species that may be localized in the surface of tumor cells and enhance matrix degradation during cancer metastasis is suggested.