S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature).
Binding of S100 proteins to RAGE: an update.
The S100 family of EF-hand calcium-binding proteins: functions and pathology.
S100 proteins: structure, functions and pathology.
S100 proteins have received increasing attention due to their close association with several human diseases including cardiomyopathy, neurodegenerative disorders and cancer, and are considered having a potential as drug targets to improve therapies.
Parvalbumin-immunoreactive neurons in the rat neostriatum: a light and electron microscopic study
Chemically defined neuron groups and their subpopulations in the glomerular layer of the rat main olfactory bulb
S100B and S100A6 Differentially Modulate Cell Survival by Interacting with Distinct RAGE (Receptor for Advanced Glycation End Products) Immunoglobulin Domains*
- E. Leclerc, G. Fritz, M. Weibel, C. Heizmann, A. Galichet
- BiologyJournal of Biological Chemistry
- 26 October 2007
Comparison of the interaction of two S100 proteins, S100B and S100A6, with RAGE by in vitro assay and in culture of human SH-SY5Y neuroblastoma cells suggests that the receptor for advanced glycation end products (RAGE) plays important roles in mediating S100 protein-induced cellular signaling.
Subpopulations of gabaergic neurons in laminae i–iii of rat spinal dorsal horn defined by coexistence with classical transmitters, peptides, nitric oxide synthase or parvalbumin
Correlation of parvalbumin concentration with relaxation speed in mammalian muscles.
- C. Heizmann, M. Berchtold, A. Rowlerson
- BiologyProceedings of the National Academy of Sciences…
- 1 December 1982
It is suggested that parvalbumin is involved directly in the relaxation process in fast muscles in a variety of muscles and species.
Parvalbumin and calbindin D‐28k in the human motor system and in motor neuron disease
- P. Ince, N. Stout, K. Baimbridge
- Biology, MedicineNeuropathology and Applied Neurobiology
- 1 August 1993
The distribution of calbindin D‐28k and parvalbumin was surveyed in the normal human motor system and in motor neuron disease (MND) using immunocytochemistry in formalin fixed post‐mortem tissues.