We are analyzing https://link.springer.com/chapter/10.1007/978-94-007-3012-0_7.

Title:
Phosphoinositide Phosphatases: Just as Important as the Kinases | SpringerLink
Description:
Phosphoinositide phosphatases comprise several large enzyme families with over 35 mammalian enzymes identified to date that degrade many phosphoinositide signals. Growth factor or insulin stimulation activates the phosphoinositide 3-kinase that phosphorylates...
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
Health & Fitness

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We're unsure how the site profits.

While profit motivates many websites, others exist to inspire, entertain, or provide valuable resources. Websites have a variety of goals. And this might be one of them. Link.springer.com might be earning cash quietly, but we haven't detected the monetization method.

Keywords {🔍}

google, scholar, pubmed, cas, article, phosphatase, cell, inositol, biol, ship, cancer, chem, polyphosphate, gene, human, res, mol, protein, expression, phosphoinositide, syndrome, cells, regulates, mitchell, synaptojanin, signaling, sci, usa, phosphatidylinositol, genet, ptdinsp, role, proc, acad, phosphatases, sac, natl, lowe, function, analysis, membrane, majerus, prex, type, ocrl, breast, regulation, activation, factor, zhang,

Topics {✒️}

fmet-leu-phe-induced superoxide production sh3p4/sh3p8/sh3p13 protein family guanine-nucleotide exchange factor leukaemic t-cell line platelet-derived growth factor muscle-eye-brain disease gene exchange factor p-rex2a bcr-mediated blys receptor regulates fcgammar-mediated phagocytosis month download article/chapter regulates clathrin-mediated endocytosis bcr-abl-mediated transformation sphingosine-1-phosphate receptor s1p1 carcinogen-induced murine model oliveira-dos-santos aj inhibits immunoglobulin e-mediated common ocrl-binding motif promote tnfalpha-dependent growth insulin-induced metabolic actions inositol pyrophosphates 5pp-insp5 akt proto-oncogene product k-ras transformation independent neuregulin-erbb signal transduction mnb/dyrk1a phosphorylation regulates constitutively tyrosine phosphorylated encoding inositol polyphosphate-5-phosphatase 75-kda inositol polyphosphate-5-phosphatase undergoes stimulation-dependent dephosphorylation genome-wide molecular profiles fas-mediated death pathway cell growth-dependent coordination mammalian inositol-polyphosphate 5-phosphatases microrna-205-directed transcriptional activation inositol-5-phosphatase knockout mice kidney-enriched inositol phosphatase feed-forward proinflammatory mechanism tyrosine-phosphorylated beta subunit cerebellar long-term potentiation macrophage rac1 activation van netten-thomas cj x-ray crystallographic analysis chemokine receptor expression coated endocytic intermediates growth factor signaling onco-mir-155 targets ship1 inhibits pi3k signaling stress-induced phosphatidylinositol 3 hoopes rr jr rac-gef p-rex1 fcgammar-stimulated phagocytosis

Questions {❓}

Astle MV, Horan KA, Ooms LM, Mitchell CA (2007) The inositol polyphosphate 5-phosphatases: traffic controllers, waistline watchers and tumour suppressors?
Bisgaard AM, Kirchhoff M, Nielsen JE, Brandt C, Hove H, Jepsen B, Jensen T, Ullmann R, Skovby F (2007) Transmitted cytogenetic abnormalities in patients with mental retardation: pathogenic or normal variants?
Orchard TJ, Chang YF, Ferrell RE, Petro N, Ellis DE (2002) Nephropathy in type 1 diabetes: a manifestation of insulin resistance and multiple genetic susceptibilities?

Schema {🗺️}

ScholarlyArticle:
      headline:Phosphoinositide Phosphatases: Just as Important as the Kinases
      pageEnd:279
      pageStart:215
      image:https://media.springernature.com/w153/springer-static/cover/book/978-94-007-3012-0.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Phosphoinositides I: Enzymes of Synthesis and Degradation
         isbn:
            978-94-007-3012-0
            978-94-007-3011-3
         type:Book
      publisher:
         name:Springer Netherlands
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Jennifer M. Dyson
            affiliation:
                  name:Monash University
                  address:
                     name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Clare G. Fedele
            affiliation:
                  name:Monash University
                  address:
                     name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Elizabeth M. Davies
            affiliation:
                  name:Monash University
                  address:
                     name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Jelena Becanovic
            affiliation:
                  name:Monash University
                  address:
                     name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Christina A. Mitchell
            affiliation:
                  name:Monash University
                  address:
                     name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Inositol polyphosphate 5-phosphatases, Inositol polyphosphate 4-phosphatases, Sac phosphatases, Trafficking, Hematopoietic system
      description:Phosphoinositide phosphatases comprise several large enzyme families with over 35 mammalian enzymes identified to date that degrade many phosphoinositide signals. Growth factor or insulin stimulation activates the phosphoinositide 3-kinase that phosphorylates phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to form phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P3], which is rapidly dephosphorylated either by PTEN (phosphatase and tensin homologue deleted on chromosome 10) to PtdIns(4,5)P2, or by the 5-phosphatases (inositol polyphosphate 5-phosphatases), generating PtdIns(3,4)P2. 5-phosphatases also hydrolyze PtdIns(4,5)P2 forming PtdIns(4)P. Ten mammalian 5-phosphatases have been identified, which regulate hematopoietic cell proliferation, synaptic vesicle recycling, insulin signaling, and embryonic development. Two 5-phosphatase genes, OCRL and INPP5E are mutated in Lowe and Joubert syndrome respectively. SHIP [SH2 (Src homology 2)-domain inositol phosphatase] 2, and SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) negatively regulate insulin signaling and glucose homeostasis. SHIP2 polymorphisms are associated with a predisposition to insulin resistance. SHIP1 controls hematopoietic cell proliferation and is mutated in some leukemias. The inositol polyphosphate 4-phosphatases, INPP4A and INPP4B degrade PtdIns(3,4)P2 to PtdIns(3)P and regulate neuroexcitatory cell death, or act as a tumor suppressor in breast cancer respectively. The Sac phosphatases degrade multiple phosphoinositides, such as PtdIns(3)P, PtdIns(4)P, PtdIns(5)P and PtdIns(3,5)P2 to form PtdIns. Mutation in the Sac phosphatase gene, FIG4, leads to a degenerative neuropathy. Therefore the phosphatases, like the lipid kinases, play major roles in regulating cellular functions and their mutation or altered expression leads to many human diseases.
      datePublished:2012
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Phosphoinositides I: Enzymes of Synthesis and Degradation
      isbn:
         978-94-007-3012-0
         978-94-007-3011-3
Organization:
      name:Springer Netherlands
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Monash University
      address:
         name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
         type:PostalAddress
      name:Monash University
      address:
         name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
         type:PostalAddress
      name:Monash University
      address:
         name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
         type:PostalAddress
      name:Monash University
      address:
         name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
         type:PostalAddress
      name:Monash University
      address:
         name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Jennifer M. Dyson
      affiliation:
            name:Monash University
            address:
               name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
               type:PostalAddress
            type:Organization
      name:Clare G. Fedele
      affiliation:
            name:Monash University
            address:
               name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
               type:PostalAddress
            type:Organization
      name:Elizabeth M. Davies
      affiliation:
            name:Monash University
            address:
               name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
               type:PostalAddress
            type:Organization
      name:Jelena Becanovic
      affiliation:
            name:Monash University
            address:
               name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
               type:PostalAddress
            type:Organization
      name:Christina A. Mitchell
      affiliation:
            name:Monash University
            address:
               name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
      name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
      name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
      name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
      name:Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(1116)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js

7.14s.

LINK . SPRINGER . COM {}