5 edition of Calcium Binding Proteins in Normal and Transformed Cells (Advances in Experimental Medicine and Biology) found in the catalog.
Calcium Binding Proteins in Normal and Transformed Cells (Advances in Experimental Medicine and Biology)
March 31, 1990
Written in English
|Contributions||R. Pochet (Editor), D. Eric M. Lawson (Editor), Claus W. Heizmann (Editor)|
|The Physical Object|
|Number of Pages||224|
2) Binds regulatory proteins and alters movement of contractile or cytoskeletal proteins-microtubules. Ca2+ binding to TROPONIN, initiating a muscle contraction 3) binds to regulatory proteins to trigger exocytosis of secretory vesicles ->ex insulin from B cells pancreas occurs in response to calcium signal. Calmodulin and Calmodulin-Binding Proteins in Normal and Virus-Transformed Fibroblasts: Levels, Subcellular Distribution, and Regulation Calcium-Binding Proteins and Cell Proliferation Extracellular Calcium Regulates Growth and Terminal Differentiation of Book Edition: 1.
CP Cooperates with Two Calcium-binding Proteins to Regulate Cytokinesis and Genome Stability. This in vivo interaction was also observed using both normal diploid and transformed cells (HeLa, T98G, Saos2, and IMR90). Molecular Biology of the Cell is published by . The 10th European Symposium on Calcium-Binding Proteins in Normal and Transformed Cells The 10th European Symposium on Calcium-Binding Proteins in Normal and Transformed Cells was held at K.U. Leuven, one of the oldest University in Europe, from 17th–20th of September The meeting was organized by our Belgian colleagues Humbert De.
The plant hormone auxin is a central regulator of plant development. In Arabidopsis, the PINOID (PID) protein serine/threonine kinase is a key component in the signaling of this phytohormone. To further investigate the biological function of PID, we performed a screen for PID-interacting proteins using the yeast two-hybrid system. Here, we show that PID interacts with two calcium-binding. Proteins are not stored for later use, so excess proteins must be converted into glucose or triglycerides, and used to supply energy or build energy reserves. Although the body can synthesize proteins from amino acids, food is an important source of those amino acids, especially because humans cannot synthesize all of the 20 amino acids used to.
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Calcium Binding Proteins in Normal and Transformed Cells. Editors: Pochet, R., Lawson, D. Eric M., Heizmann, Claus W. (Eds.) Free PreviewBrand: Springer US. Calcium Binding Proteins in Normal and Transformed Cells.
Editors (view affiliations) Calcium Binding Proteins in Transformed Cells. Oncomodulin in Normal and Transformed Cells. John P. MacManus, Linda M. Brewer, Denis Banville. Pages Calcium Binding Proteins in Normal and Transformed Cells (Advances in Experimental Medicine and Biology): Medicine & Health Science Books @ mat: Paperback.
"Proceedings of the First European Symposium on Calcium Binding Proteins in Normal and Transformed Cells, held Aprilin Brussels, Belgium"--Title page verso. Description: pages: illustrations ; 26 cm. Contents: Calcium and Steady States.- Genes of Calcium Binding Protein Family Calcium and Steady States --Genes of Calcium Binding Protein Family --Evolution of the "ef-Hand" Family of Calcium-Binding Proteins --Functional Analysis of the Promoter Region of the Gene Encoding Chicken Calbindin-D28K --Structure of the Human cDNAs and Genes coding for Calbindin-D28K and Calretinin --Calbindin-D9K (CaBP9K) Gene: a Model for.
Calcium- binding sites in proteins coordinate the calcium ion by protein oxygen atoms and water molecules in a roughly octahedral arrangement. The prototypic EF-hand presumably gained calcium-binding ability in a similar way by modification of a protein or a protein fragment, which originally had some other function.
Several tumor cells (transformed by chemicals or viruses) contain increased concentrations of Ca 2+-binding proteins. The multifunctional Ca 2+-binding protein calmodulin was found to be 2 to 10 fold higher in some transformed cells as compared to normal cells (Chafouleas et al., ; Zendegui et al., ).Cited by: 1.
Oncomodulin has three domains composed of helix:metal-binding loop:helix arranged in a similar way to parvalbumin (Moews and Kretsinger ).
This was not unexpected because it was known that oncomodulin and parvalbumin share 50% identical amino acid sequence, and an additional 30% conservative residue replacement (MacManus et al., ).Cited by: 9.
Discover Book Depository's huge selection of D M Lawson books online. Free delivery worldwide on over 20 million titles. Section III Novel Members of the EF-Hand Calcium-Binding Protein Family in Normal and Transformed Cells.- 13 Calretinin.- 14 Purification, Identification And Regional Localization of a Brain-Specific Calretinin-Like Calcium-Binding Protein (Protein 10).- 15 Lsp1 is a New Lymphocyte-Specific Ca2+-Binding Protein Which Co-Caps With Surface.
Language: English ISBN:LCCN: MeSH: Calcium-Binding Proteins/genetics*Calcium-Binding Proteins/physiology* Publication Type(s): Congresses Notes: "Proceedings of the First European Symposium on Calcium Binding Proteins in Normal and Transformed Cells, held Aprilin Brussels, Belgium"--T.p.
verso. Purchase Calcium-Binding Proteins in Health and Disease - 1st Edition. Print Book & E-Book. ISBNThe content of the book delves into 48 chapters including subjects such as data analysis and modern technologies to study calcium-binding and signaling in cells, the superfamily of calcium-binding proteins characterized by the EF-hand structural motif, as well as their use as diagnostic and prognostic biomarkers in Laboratory Medicine and novel.
Together, EF-hand calcium-binding proteins serve in the critical process of converting the ionic signal into activation of intracellular signalling pathways. Key Concepts: The EF-hand is a helix. Members of the Arabidopsis calcineurin B–like Ca2+ binding protein (AtCBL) family are differentially regulated by stress conditions.
One AtCBL plays a role in salt stress; another is implicated in response to other stress signals, including drought, cold, and wounding. In this study, we identified a group of novel protein kinases specifically associated with AtCBL-type Ca2+ by: The enormous and varied role of calcium in living systems is now widely appreciated by both cell biologists and clinicians.
The identification and characterisation of new calcium binding proteins and regulatory pathways is matched by the recognition of the involvement of calcium binding proteins in a growing number of disease states. This book is intended to introduce clinicians to fundamental.
Download Calcium Binding Proteins in Normal and Transformed Cells by R Pochet Valedictory Address to the Graduating Class of Hahnemann Medical College, Delivered February 15th, (Classic Reprint).
Separation of various calmodulins, calmodulin tryptic fragments, and different homologous Ca2+-binding proteins by reversed-phase, hydrophobic interaction, and ion-exchange high-performance liquid. Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.
Annexin 2 is involved in diverse cellular processes such as cell motility (especially that of the epithelial cells), linkage of membrane-associated protein complexes to the actin cytoskeleton, endocytosis, fibrinolysis, ion channel formation, and cell matrix s: ANXA2, ANX2, ANX2L4, CAL1H, HEL-S.
Calcium signals are transduced into cellular responses via Ca 2+-binding proteins, of which calmodulin (CaM) is the most common (Zielinski, ). Changes in intracellular Ca 2+ and signaling via Ca 2+ are well-documented features of legume-rhizobia interactions and root nodule development (Lévy et al., ).Cited by:.
DEFINITION. Hypercalcemia can be defined as a serum calcium greater than 2 standard deviations above the normal mean in a reference laboratory.
Calcium in the blood is normally transported partly bound to plasma proteins (about 45%), notably albumin, partly bound to small anions such as phosphate and citrate (about 10%) and partly in the free or ionized state (about 45%) (1).Cited by: 6.
Cambridge 8 th European symposium on calcium-binding proteins in normal and transformed cells Cambridge, Wednesday July 28 th to Saturday J Program ; Abstract book ; Photos; Poster Prizes and ECS Grants.
Among the salt-responsive microsomal proteins, two spots that increased upon salt treatment on a two-dimensional gel were identified as the same protein, designated annexin 1 (AnnAt1).
Annexins comprise a multigene family of Ca2+-dependent membrane binding proteins and have been extensively studied in animal by: