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Tuesday, August 4, 2020 | History

4 edition of Calreticulin (Molecular Biology Intelligence Unit) (Molecular Biology Intelligence Unit) found in the catalog.

Calreticulin (Molecular Biology Intelligence Unit) (Molecular Biology Intelligence Unit)

  • 135 Want to read
  • 22 Currently reading

Published by Springer .
Written in English

    Subjects:
  • Metabolism,
  • Proteins,
  • Science,
  • Science/Mathematics,
  • Biochemistry,
  • Life Sciences - Biochemistry,
  • Science / Biological Sciences,
  • Science / Biochemistry,
  • Life Sciences - Biology - General,
  • Calreticulin

  • Edition Notes

    ContributionsPaul Eggleton (Editor), Marek Michalak (Editor)
    The Physical Object
    FormatHardcover
    Number of Pages304
    ID Numbers
    Open LibraryOL9898301M
    ISBN 100306478455
    ISBN 109780306478451

    Today's Deals Best Sellers Find a Gift Customer Service New Releases Registry Books Gift Cards Kindle Books AmazonBasics Sell Amazon Home Amazon Fashion Toys & Games Coupons Computers Whole Foods Automotive Beauty & Personal Care Home Improvement Health & Household TV & Video Smart Home Food & Grocery Baby Handmade Amazon Launchpad Free. The calreticulin Mi-CRT is a protein synthesized in the esophageal glands of the root-knot nematode Meloidogyne incognita. After three-dimensional modeling of the Mi-CRT protein, a surface peptide.

    In the present study, we focused on Calreticulin (CALR) which is one of those 11 proteins. CALR is a 46 kDa protein which acts as a molecular chaperone and a major Ca (2+)-binding (storage) protein in the endoplasmic reticulum (ER) that ensures proper folding of glycoproteins (9 – 11). The book focuses on the latest discoveries on calreticulin, calnexin and other endoplasmic reticulum proteins. Calreticulin has been implicated to affect diverse cellular function and play a role in many pathologies including protein folding disorders, ca.

      Calreticulin is an essential protein present in the endoplasmic reticulum of cells, which is capable of binding to calcium and has some vital nuclear functions as well as functions that are wholly. Calreticulin is a ubiquitous Ca 2+ binding protein, located in the endoplasmic reticulum lumen, which has been implicated in many diverse functions including: regulation of intracellular Ca 2+ homeostasis, chaperone activity, steroid-mediated gene regulation, and cell adhesion. To understand the physiological function of calreticulin we used gene targeting to create a knockout mouse for.


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Calreticulin (Molecular Biology Intelligence Unit) (Molecular Biology Intelligence Unit) Download PDF EPUB FB2

Calreticulin also known as calregulin, CRP55, CaBP3, calsequestrin-like protein, and endoplasmic reticulum resident protein 60 (ERp60) is a protein that in humans is encoded by the CALR gene. Calreticulin is a multifunctional soluble protein that binds Ca 2+ ions (a second messenger in signal transduction), rendering it Ca 2+ is bound with low affinity, but high capacity, and can Aliases: CALR, CRT, HEL-Sn, RO, SSA, cC1qR.

The book focuses on the latest discoveries on calreticulin, calnexin and other endoplasmic reticulum proteins. Calreticulin has been implicated to affect diverse cellular function and play a role in many pathologies including protein folding disorders, cardiac pathologies, cancer and autoimmunity.

Calreticulin and the Modulation of Gene Expression \/ Nasrin Mesaeli -- 7. Role of Calreticulin in Rubella Virus Replication \/ Chintamani D. Atreya, Gregory P. Pogue, Nishi K. Singh and Hira L. Nakhasi -- 8. Calreticulin and Autoimmunity \/ Richard D. Sontheimer, Tho Q. Nguyen, Shih-Tsung Cheng, Tsu-San Lieu and J.

Donald Capra -- 9. Calreticulin and the Action of 1,25(OH) 2 D 3 on the PTH Gene. Calreticulin is a calcium-binding protein present in the endoplasmic reticulum of cells that may also have a nuclear function. It regulates gene transcription via its ability to bind a protein motif in the DNA-binding domain of nuclear hormone receptors of sterol hormones.

This book is about calreticulin, a multifunctional calcium binding protein first discovered over 20 years ago. The protein has been described in various locations: endoplasmic reticulum, nuclear envelope, cytoplasmic granules, nucleus, cell surface and even secreted into the blood stream.

This book is about calreticulin, a multifunctional calcium binding protein first discovered over 20 years ago. The protein has been described in various locations: endoplasmic reticulum, nuclear envelope, cytoplasmic granules, nucleus, cell surface and even secreted into the blood stream.

This. Calreticulin is an abundant 46 kDa, high capacity Ca 2+-binding protein found (with the Calreticulin book of erythrocytes) in every cell of higher ural predictions for calreticulin suggest that it has at least three structural and functional domains ().The protein has an N-terminal signal sequence that is processed cotranslationally (R.

Clark, University of Texas Health Science. Calreticulin has been implicated to affect diverse cellular function and play a role in many pathologies including protein folding disorders, cardiac pathologies, cancer and autoimmunity.

This book contains contributions from the world leaders in the area of endoplasmic reticulum function, protein folding, Calcium homeostasis and autoimmunity.

Calreticulin (CALR) Mutation Analysis - This DNA-based assay tests leukocytes from blood or bone marrow aspirate for mutations in exon 9 of calreticulin (CALR), using an advanced DNA sequencing method. Frameshift mutations in this region of CALR are associated with myeloproliferative neoplasms, particularly essential thrombocythemia and primary myelofibrosis.

Andy van Hateren, Tim Elliott, in Encyclopedia of Immunobiology, Calreticulin. Calreticulin is a 60 kDa homologue of calnexin, and like calnexin contains a globular glycan-binding site with specificity for (GlcNAc) 2 (Man) 9 Glc and an elongated P-domain that binds ERp57 at its tip (Frickel et al., ), and is thus important for holding together the PLC.

Calreticulin is a multi-functional chaperone protein involved in protein folding, maturation, and trafficking. However, evidence has been accumulating that calreticulin can also negatively regulate the surface expression of certain receptors and channels.

In these instances, depletion of calreticulin enhances cell-surface expression and function. The book focuses on the latest discoveries on calreticulin, calnexin and other endoplasmic reticulum proteins.

Calreticulin has been implicated to affect diverse cellular function and play a role in many pathologies including protein folding Author: Paul Eggleton. The book focuses on the latest discoveries on calreticulin, calnexin and other endoplasmic reticulum proteins.

Calreticulin has been implicated to affect diverse cellular function and play a role in many pathologies including protein folding disorders, cardiac pathologies, cancer and autoimmunity. This book contains contributions from the world leaders in the area of endoplasmic reticulum. Calreticulin (CRT) and calnexin (CNX) are members of a family of endoplasmic reticulum (ER) chaperones that fold newly synthesized polypeptides.

Aside from their role as foldases in the ER, our laboratory has shown that all members of this family of proteins modulate Ca2+ oscillations. In Xenopus oocytes and other cells, stimulation by G-protein and tyrosine coupled receptors results in Ca2. Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle.

This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Calreticulin is a highly conserved endoplasmic reticulum chaperone protein which participates in various cellular processes.

It was first identified as a Ca 2+ -binding protein in Accumulated evidences indicate that calreticulin has great impacts for the development of different cancers and the effect of calreticulin on tumor formation and progression may depend on cell types and.

Calnexin and calreticulin are homologous molecular chaperones of the endoplasmic reticulum. Their binding to newly synthesized glycoproteins is mediated, at least in part, by a lectin site that recognizes the early N-linked oligosaccharide processing intermediate, Glc1Man9GlcNAc2.

We compared the oligosaccharide binding specificities of calnexin and calreticulin in an effort to determine the. ISBN: OCLC Number: Description: pages: illustrations ; 24 cm.

Contents: Introduction to Calreticulin / Paul Eggleton, Marek Michalak --Biochemical and Molecular Properties of Calreticulin / Steven J. Johnson, Kjell O. Hakansson --A Chaperone System for Glycoprotein Folding: The Calnexin/Calreticulin Cycle / Lars Ellgaard, Ari Helenius --Calnexin, an ER.

Calreticulin is a highly conserved chaperone protein which resides primarily in the endoplasmic reticulum, and is involved in a variety of cellular processes, among them, cell adhesion. Additionally, it functions in protein folding quality control and calcium homeostasis.

Calreticulin is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin is an ancient and highly conserved protein. It is intensively studied and has been assigned multiple functions, the scope and variety of which are exceptionally wide for a single protein.

Calreticulin (CALR) is a multifaceted protein primarily involved in intracellular protein control processes. The identification of CALR mutations in essential thrombocythemia (ET) and primary myelofibrosis that are mutually exclusive with the JAK2 VF mutation has stirred an intensive research interest about the molecular functions of CALR and its mutants in myeloproliferative neoplasms.Calreticulin is a Ca 2+-binding chaperone in the endoplasmic reticulum (ER), and calreticulin gene knockout is embryonicwe used calreticulin-deficient mouse embryonic fibroblasts to examine the function of calreticulin as a regulator of Ca 2+ homeostasis.

In cells without calreticulin, the ER has a lower capacity for Ca 2+ storage, although the free ER luminal Ca 2+ concentration.Along with other endoplasmic reticulum (ER) Ca 2+-binding proteins, notably the glucose-response proteins grp78 and grp94, expression of calreticulin is induced in response to perturbation of normal ER has yet to be clearly defined how this stress is signaled from the ER to the nucleus in mammalian cells, particularly with regard to its initiation.