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3 edition of Protein kinase C and its brain substrates found in the catalog.

Protein kinase C and its brain substrates

International Meeting on Brain in Phosphoproteins (3rd 1990 Zeist, Netherlands)

Protein kinase C and its brain substrates

role in neuronal growth and plasticity : proceedings of the Third International Meeting on Brain Phosphoproteins, held at Zeist (The Netherlands) 24-26 August, 1990

by International Meeting on Brain in Phosphoproteins (3rd 1990 Zeist, Netherlands)

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  • 40 Currently reading

Published by Elsevier, Sole distributors for the U.S.A. and Canada, Elsevier Science Pub. Co. in Amsterdam, New York, New York, NY, U.S.A .
Written in English

    Subjects:
  • Protein kinase C -- Congresses.,
  • Neurochemistry -- Congresses.,
  • Neuroplasticity -- Congresses.

  • Edition Notes

    Includes bibliographical references and index.

    Statementedited by W.H. Gispen and A. Routtenberg.
    SeriesProgress in brain research ;, v. 89
    ContributionsGispen, Willem Hendrik., Routtenberg, Aryeh.
    Classifications
    LC ClassificationsQP376 .P7 vol. 89, QP606.P76 .P7 vol. 89
    The Physical Object
    Paginationxiii, 292 p. :
    Number of Pages292
    ID Numbers
    Open LibraryOL1767851M
    ISBN 100444814361
    LC Control Number92118992

      Mutations in PTEN-induced putative kinase 1 (PINK1) are a cause of autosomal recessive familial Parkinson's disease (PD). Efforts in deducing the PINK1 signaling pathway have been hindered by controversy around its subcellular and submitochondrial localization and the authenticity of its reported substrates. We show here that this mitochondrial protein exhibits a topology in which the kinase Missing: book. c-Abl has a unique myristoylated N-terminal region that negatively regulates its kinase activity 82 Several studies have shown the involvement of c-Abl in neurodegenerative diseases such as PD.

    Although the modification is often essential for the proper functioning of the modified protein, the mechanism by which the modification exerts its effects is still largely unknown. Brain-specific protein kinase C substrate, CAP/NAP, which is involved in the synaptogenesis and neuronal plasticity, binds calmodulin, but the protein lacks any canonical calmodulin-binding g: book. Discovery. The first mitogen-activated protein kinase to be discovered was ERK1 in ERK1 and its close relative ERK2 are both involved in growth factor signaling, the family was termed "mitogen-activated".With the discovery of other members, even from distant organisms (e.g. plants), it has become increasingly clear that the name is a misnomer, since most MAPKs are actually Missing: book.

    CEP4, GTPase, Mutants, Protein Kinase C, Rac, Substrate. Abstract. Aberrations in PKC signaling can lead to the development of multiple human diseases and the most prominent association of PKC with disease has been in tumor growth and metastasis. PKC and its related pathways have been recognized as promising targets for blocking the malignancy. As the number of known protein kinases has increased at an ever-accelerating pace, it has become more challenging to determine which protein kinases interact with which substrates in the cell. The determination of consensus phosphorylation site motifs by amino acid sequence alignment of known substrates has proven useful in this g: book.


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Protein kinase C and its brain substrates by International Meeting on Brain in Phosphoproteins (3rd 1990 Zeist, Netherlands) Download PDF EPUB FB2

Purchase Protein Kinase C and its Substrates, Volume 89 - 1st Edition. Print Book & E-Book. ISBN  Get this from a library. Protein kinase C and its brain substrates: role in neuronal growth and plasticity: proceedings of the Third International Meeting on Brain Phosphoproteins, held at Zeist (The Netherlands) August, [Willem Hendrik Gispen; Aryeh Routtenberg;].

Protein Kinase C Protocols covers fundamental methods for studying the structure, function, regulation, subcellular localization, and macromolecular interactions of PKC.

Protein Kinase C Protocols is divided into 11 sections representing the major aspects of PKC regulation and : Hardcover. Described in step-by-step detail, these methods can be easily used to explore the structure, function, regulation, subcellular localization, and macromolecular interactions of protein kinase C.

Included in this collection are easy-to-follow techniques to purify protein kinase C, to measure its activity and its membrane interaction in vivo and.

Protein kinase C and its brain substrates: role in neuronal growth and plasticity. Proceedings of the Third In ternational Meeting on Brain Phosphoproteins, the Netherlands, August Progress in Brain Research, 01 JanPMID: binding and the protein kinase C activities coeluted both upon partial purification (13—16)and with the homogeneously puri fled protein (17, 18).

Considerable recent effort has been directed at characterizing the substrate specificity of protein kinase C, its interaction with lipids and its subcellular localization (10, 19). A major im. Alexandra C. Newton, in Handbook of Cell Signaling (Second Edition), Downregulation of Protein Kinase C.

Protein kinase C isozymes are degraded by multiple mechanisms. In the absence of activation, conventional isozymes have an unusually long half-life (days), but in the membrane-bound conformation they are rapidly dephosphorylated and shunted to degradation pathways.

Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to g: book.

Structure. Members of the protein kinase C family are a single polypeptide, comprised of an N-terminal regulatory region (approximately kDa) and a C-terminal catalytic region (approximately 45 kDa) ().Cloning of the first isozymes in the mids revealed four conserved domains: C1-C4().Each is a functional module, and many unrelated proteins have one or the other().Missing: book.

Protein kinase C, commonly abbreviated to PKC (EC ), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family.

PKC enzymes in turn are activated by signals such as increases in the concentration of Missing: book. protein kinase C substrates of bovine brain. To better characterize p43 and p17, the further purification of both proteins was desirable and this was achieved by two.

A.C. Newton, in Encyclopedia of Biological Chemistry (Second Edition), PKC Signaling. PKC phosphorylates an abundance of substrates, including membrane proteins, cytoskeletal proteins, cytosolic proteins, and nuclear proteins.

It plays key roles in diverse biological processes, many involving cell-survival pathways. Neurogranin, formerly designated p17 (Baudier, J., Bronner, C., Kligman, D., and Cole, R. D.) () J. Biol. Chem.), a brain-specific in vitro substrate for protein kinase C (PKC), has been purified to homogeneity from bovine forebrain.

The epsilon isoform of protein kinase C (PKCε) has important roles in the function of the cardiac, immune and nervous systems. As a result of its diverse actions, PKCε is the target of active drug discovery programs. A major research focus. The myristoylated alanine-rich C-kinase substrate (MARCKS) was identified by Greengard and colleagues in as a protein highly enriched in brain that is heavily phosphorylated by PKC [47,48].

It has since become one of the most robust and well characterized read-outs of conventional and novel PKC signaling [ 49 ].Missing: book. Abstract. Protein kinases play diverse and essential roles in the regulation of cell growth, survival, and differentiation, and in other critical biological functions, for example, neurotransmission (1, 2).Substrate selectivity is a major factor in the division of labor among the members of the protein kinase superfamily ().Typically, local sequences surrounding phospho-acceptor residues are.

the phosphorylation of protein substrates in the active site of a protein kinase is complex and involves structural changes. While the simple core structure is shared within the protein kinase family, the core frequently interacts with regulatory proteins or domains that either enhance or repress catalytic g: book.

Abstract. Ca 2+, phospholipid-dependent protein kinase (PKC) was first described as a proteolytically activated protein kinase (1).Only later its reversible activation was demonstrated to be synergistically induced by membrane acidic phospholipids in the presence of diacylglycerol (DAG) and physiological concentration of calcium (2, 3), thus implicating PCK as a mediator of the effects of a.

C c-Jun human % (SDS-PAGE), recombinant, expressed in E. coli, truncated human c-Jun sequence-GST fusion protein GST, soluble: Substrate for SAPK1/JNK2. Purified protein transcription factor which binds the AP1 gene to activate g: book. Immobilized proteins were eluted using M Glycine pH for 10 min in RT, corresponding volume of 1 M Tris pH was added to adjust the pH to and eluted proteins were used as a substrate in kinase reaction.

The kDa protein, a major specific substrate for protein kinase C, has been purified fold to apparent homogeneity from bovine forebrain supernatant. The purification procedure included batch adsorption to DE (DEAE-cellulose), (NH4)2SO4 precipitation, and chromatography on DEAE-Sephacel, Bio-Gel HTP (hydroxylapatite), Sephacryl S, and fast protein liquid chromatography Missing: book.

Protein phosphorylation is a common posttranslational modification and is involved in many physiological and pathophysiological processes. Among other diseases, the deregulation of protein kinase activities can lead to cellular transformation and cancer. Thus, kinases are good drug targets.

Understanding how kinases interact with their substrates may elucidate processes that lead to .Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth.

Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been g: book.