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Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum.
- M. Michalak, J. Groenendyk, E. Szabó, L. Gold, M. Opas
- Chemistry, Medicine
- The Biochemical journal
- 1 February 2009
Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The protein is involved in regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity. The protein impacts on… Expand
Calreticulin: one protein, one gene, many functions.
- M. Michalak, E. Corbett, N. Mesaeli, K. Nakamura, M. Opas
- Biology, Medicine
- The Biochemical journal
- 1 December 1999
The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of membrane-associated and secreted proteins. The membrane is also an important site of Ca(2+) storage and… Expand
Quality control in the endoplasmic reticulum.
- M. Michalak
- Biology, Medicine
- Seminars in cell & developmental biology
- 1 July 2010
Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57*
- A. Zapun, N. Darby, D. Tessier, M. Michalak, J. Bergeron, David Y. Thomas
- Biology, Medicine
- The Journal of Biological Chemistry
- 13 March 1998
The endoplasmic reticulum is the site of folding, disulfide bond formation, and N-glycosylation of secretory proteins. Correctly folded proteins are exported from the endoplasmic reticulum, whereas… Expand
Modulation of gene expression by calreticulin binding to the glucocorticoid receptor
- K. Burns, B. Duggan, +4 authors M. Michalak
- Biology, Medicine
- Nature
- 3 February 1994
CALRETICULIN is a multifunctional protein that acts as a major Ca2+-binding (storage) protein in the lumen of the endoplasmic reticulum1. It is also found in the nucleus2, suggesting that it may have… Expand
Calreticulin: non‐endoplasmic reticulum functions in physiology and disease
- L. Gold, P. Eggleton, +5 authors J. Murphy-Ullrich
- Biology, Medicine
- FASEB journal : official publication of the…
- 1 March 2010
Calreticulin (CRT), when localized to the endoplasmic reticulum (ER), has important functions in directing proper conformation of proteins and glycoproteins, as well as in homeostatic control of… Expand
Characterization of monoclonal antibody to DNA.RNA and its application to immunodetection of hybrids.
- S. Boguslawski, D. E. Smith, +4 authors R. Carrico
- Biology, Medicine
- Journal of immunological methods
- 1 May 1986
Monoclonal antibodies were raised to a DNA.RNA heteropolymer duplex prepared by transcription of phi X174 single-stranded DNA with DNA-dependent RNA polymerase. A monoclonal antibody with the highest… Expand
Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum.
- L. Fliegel, K. Burns, D. Maclennan, R. Reithmeier, M. Michalak
- Biology, Medicine
- The Journal of biological chemistry
- 25 December 1989
A cDNA clone encoding the high affinity Ca2+-binding protein (HACBP) of rabbit skeletal muscle sarcoplasmic reticulum was isolated and sequenced. The cDNA encoded a protein of 418 amino acids, but a… Expand
Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum.
- M. Michalak, J. M. Robert Parker, M. Opas
- Biology, Medicine
- Cell calcium
- 1 November 2002
The endoplasmic reticulum is a centrally located organelle which affects virtually every cellular function. Its unique luminal environment consists of Ca(2+) binding chaperones, which are involved in… Expand
Calcium, a signaling molecule in the endoplasmic reticulum?
- E. Corbett, M. Michalak
- Chemistry, Medicine
- Trends in biochemical sciences
- 1 July 2000
For many years now, it has been known that Ca2+ is an important signaling molecule in the cytosol of the cell, but emerging evidence suggests that Ca2+ might also play a signaling role in the… Expand
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