Results 241 to 250 of about 30,178 (280)
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Molecular and Cellular Biochemistry, 2004
Calreticulin is a Ca2+ binding/storage chaperone resident protein of the endoplasmic reticulum. This protein plays a key role in the calreticulin/calnexin cycle and the quality control pathways in the endoplasmic reticulum. Calreticulin deficiency is lethal due to impaired cardiac development.
Marek, Michalak +4 more
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Calreticulin is a Ca2+ binding/storage chaperone resident protein of the endoplasmic reticulum. This protein plays a key role in the calreticulin/calnexin cycle and the quality control pathways in the endoplasmic reticulum. Calreticulin deficiency is lethal due to impaired cardiac development.
Marek, Michalak +4 more
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Trends in Cell Biology, 2000
The workshop organizers thank the following organizations for financial support, making possible the provision of bursaries to PhD students and junior post-doctoral workers: the Wellcome Trust, Amersham Pharmacia Biotech, Promega UK, Novus and abcam.
D H, Llewellyn, S, Johnson, P, Eggleton
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The workshop organizers thank the following organizations for financial support, making possible the provision of bursaries to PhD students and junior post-doctoral workers: the Wellcome Trust, Amersham Pharmacia Biotech, Promega UK, Novus and abcam.
D H, Llewellyn, S, Johnson, P, Eggleton
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Calreticulin in Vector Arthropods—The Secreted Calreticulin
1996One of the most unusual places calreticulin has been found is the saliva of ticks.1 Most calreticulins are located intracellularly. Our work objective was to characterize and clone salivary secretions that induce host immunity to tick feeding.2,3 Host immune response to tick feeding was demonstrated in domesticated animals as early as 1918.4 Trager5 ...
Deborah C. Jaworski, Glen R. Needham
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Characterization of the autoantigen calreticulin
The Journal of Immunology, 1991Abstract Anti-Ro/SS-A antibodies are commonly found in the sera of patients with Sjögren’s syndrome and SLE. These antibodies also occur in the mothers of children with neonatal lupus and congenital heart block. Ro/SS-A is a ribonucleoprotein complex whose cellular function remains unknown.
L A, Rokeach +6 more
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1996
Abstract Calreticulin is a ubiquitous and highly conserved Ca2+-bindinglstorage protein associated with endo(sarco)plasmic reticulum membranes. Calreticulin is a multifunctional protein implicated to play a role in a variety of cellular functions ranging from Ca2+homeostasis to the control of gene expression. Rabbit calreticulin has a
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Abstract Calreticulin is a ubiquitous and highly conserved Ca2+-bindinglstorage protein associated with endo(sarco)plasmic reticulum membranes. Calreticulin is a multifunctional protein implicated to play a role in a variety of cellular functions ranging from Ca2+homeostasis to the control of gene expression. Rabbit calreticulin has a
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Calreticulin Exposure in Mitotic Catastrophe
2021Mitotic catastrophe is a modality of cell death (or occasionally senescence) that occurs after cells enter, and fail to resolve, abnormal mitosis, for instance after DNA damage or perturbations of the cell cycle. Mitotic catastrophe can avoid the generation of neoplastic cells from premalignant precursors, yet may also occur in cancer cells as a result
Lucillia, Bezu +2 more
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Calreticulin and Calreticulin Fragments Are Endothelial Cell Inhibitors That Suppress Tumor Growth
Blood, 1999Several angiogenesis inhibitors are fragments of larger proteins that are themselves not active as angiogenesis inhibitors. Vasostatin, the N-terminal domain of calreticulin inclusive of amino acids 1-180, is an angiogenesis inhibitor that exerts antitumor effects in vivo.
S E, Pike +12 more
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1996
The human calreticulin amino acid sequence has been shown to be associated with the immune response in several ways. In addition, calreticulin is now widely accepted to be the target of autoantibody production in several autoimmune diseases including systemic lupus erythematosus (SLE).
Richard D. Sontheimer +4 more
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The human calreticulin amino acid sequence has been shown to be associated with the immune response in several ways. In addition, calreticulin is now widely accepted to be the target of autoantibody production in several autoimmune diseases including systemic lupus erythematosus (SLE).
Richard D. Sontheimer +4 more
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Calreticulin mutations in myeloproliferative neoplasms
2021Calreticulin (CALR) is a chaperone present in the endoplasmic reticulum, which is involved in the quality control of N-glycosylated proteins and storage of calcium ions. In 2013, the C-terminal mutation in CALR was identified in half of the patients with essential thrombocythemia and primary myelofibrosis who did not have a JAK2 or MPL mutation.
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2003
Over 30 years ago calreticulin, then known as the high affinity calcium binding protein (HACBP), was identified and purified from isolated skeletal muscle sarcoplasmic reticulum vesicles.1,2 Surprisingly, it took almost 20 years to realize that the protein is a major component of the endoplasmic reticulum (ER) in non-muscle cells3.
Paul Eggleton, Marek Michalak
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Over 30 years ago calreticulin, then known as the high affinity calcium binding protein (HACBP), was identified and purified from isolated skeletal muscle sarcoplasmic reticulum vesicles.1,2 Surprisingly, it took almost 20 years to realize that the protein is a major component of the endoplasmic reticulum (ER) in non-muscle cells3.
Paul Eggleton, Marek Michalak
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