S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature).
- I. Marenholz, C. Heizmann, G. Fritz
- BiologyBiochemical and Biophysical Research…
- 1 October 2004
Binding of S100 proteins to RAGE: an update.
- E. Leclerc, G. Fritz, S. Vetter, C. Heizmann
- BiologyBiochimica et Biophysica Acta
- 1 June 2009
The S100 family of EF-hand calcium-binding proteins: functions and pathology.
- B. Schäfer, C. Heizmann
- BiologyTIBS -Trends in Biochemical Sciences. Regular ed
- 1 April 1996
S100 proteins: structure, functions and pathology.
- C. Heizmann, G. Fritz, B. Schäfer
- BiologyFrontiers in Bioscience
- 1 May 2002
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
- H. Kita, T. Kosaka, C. Heizmann
- BiologyBrain Research
- 17 December 1990
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
- I. Laing, A. Todd, C. Heizmann, H. Schmidt
- BiologyNeuroscience
- 1 July 1994
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.
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