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LINK . SPRINGER . COM {}

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  4. Monthly Traffic Estimate
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  6. Keywords
  7. Topics
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We are analyzing https://link.springer.com/chapter/10.1007/978-981-15-1025-0_3.

Title:
Assembly and Regulation of CRL Ubiquitin Ligases | SpringerLink
Description:
Cullin-RING ubiquitin ligases (CRLs) determine the substrate specificity of ubiquitination reactions, and substrates are recruited to the cullin core through binding to their cognate substrate receptor modules. Because a family of substrate receptors compete for the...
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Telecommunications
  • Business & Finance

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 5,000,016 visitors per month in the current month.

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

We can't see how the site brings in money.

Earning money isn't the goal of every website; some are designed to offer support or promote social causes. People have different reasons for creating websites. This might be one such reason. Link.springer.com could have a money-making trick up its sleeve, but it's undetectable for now.

Keywords {🔍}

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Topics {✒️}

appbp1-uba3-nedd8-atp complex reveals skp1-cul1-f-box tbp ubiquitin/proteasome-mediated protein degradation skp1-cul1-f-box protein sloper-mould ke month download article/chapter n-terminal acetylation acts scaffold-type e3 ligase cullin-ring catalytic core ran-nucleotide exchange catalyzed cullin–ring e3 networks 120-kda tbp-interacting protein stress-inducible dual e2 chapter cullin-ring ligases conserved protein dcn-1/dcn1p nedd8 recruits e2-ubiquitin ubiquitin c-terminal hydrolases ubiquitin-related protein rub1 unmodified cul1-interacting protein f-box protein expression deconjugating hyper-neddylated cul1 roc1-cul1 complex ubiquitin-activating enzyme e1 huang dt ubp-family deubiquitinating enzyme nedd-cul1 conjugate cleavage cullin-ring ligases skp1-f-box e2-ring expansion scf e3 ligase e2 binding domain ring e3 trapped scf ubiquitin-ligase ubiquitin ligase scf crl ubiquitin ligases ubiquitin pathway enzymes device instant download life sciences biomedical dual e3 mechanism cand1-dependent remodelling ubiquitin transfer cascade rub/nedd8 conjugation pathway privacy choices/manage cookies scf ubiquitin ligases c-terminal tail fischer es boh bk editor information editors heat-repeat protein cand1-mediated cycling

Schema {🗺️}

ScholarlyArticle:
      headline:Assembly and Regulation of CRL Ubiquitin Ligases
      pageEnd:46
      pageStart:33
      image:https://media.springernature.com/w153/springer-static/cover/book/978-981-15-1025-0.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Cullin-RING Ligases and Protein Neddylation
         isbn:
            978-981-15-1025-0
            978-981-15-1024-3
         type:Book
      publisher:
         name:Springer Singapore
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Kankan Wang
            affiliation:
                  name:Purdue University
                  address:
                     name:Department of Biochemistry, Purdue University, West Lafayette, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Raymond J. Deshaies
            affiliation:
                  name:Amgen, One Amgen Center Way
                  address:
                     name:Amgen, One Amgen Center Way, Thousand Oaks, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Xing Liu
            affiliation:
                  name:Purdue University
                  address:
                     name:Department of Biochemistry, Purdue University, West Lafayette, USA
                     type:PostalAddress
                  type:Organization
                  name:Center for Plant Biology, Purdue University
                  address:
                     name:Center for Plant Biology, Purdue University, West Lafayette, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:NEDD8, Neddylation, Cullin, CRLs, SCF, Cand1, Ubiquitination, F-box proteins
      description:Cullin-RING ubiquitin ligases (CRLs) determine the substrate specificity of ubiquitination reactions, and substrates are recruited to the cullin core through binding to their cognate substrate receptor modules. Because a family of substrate receptors compete for the same cullin core, the assembly and activity of CRLs are dynamically regulated to fulfill the needs of the cell to adapt to the changing pool of proteins demanding ubiquitination. Cullins are modified by NEDD8, a ubiquitin-like protein. This process, referred to as neddylation, promotes the E3 activity of CRLs by inducing conformational rearrangement in the Cullin-RING catalytic core. Cand1 is a cullin-associated protein whose binding is excluded by cullin neddylation. Although early biochemical studies suggested that Cand1 inhibits CRL activity, genetic studies revealed its positive role in ubiquitination. Emerging evidence from kinetic and quantitative proteomic studies demonstrated that Cand1 stimulates assembly of new Skp1-Cul1-F-box protein (SCF) complexes by exchanging the Skp1-F-box protein substrate receptor modules. Furthermore, aided by refined experimental design as well as computational simulation, an attractive model has been developed in which substrate, neddylation cycle and Cand1-mediated “adaptive exchange” collaborate to maintain the dynamics of the cellular SCF repertoire. Here, we review and discuss recent advances that have deepened our understanding of CRL regulation.
      datePublished:2020
      isAccessibleForFree:
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         type:WebPageElement
      context:https://schema.org
Book:
      name:Cullin-RING Ligases and Protein Neddylation
      isbn:
         978-981-15-1025-0
         978-981-15-1024-3
Organization:
      name:Springer Singapore
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Purdue University
      address:
         name:Department of Biochemistry, Purdue University, West Lafayette, USA
         type:PostalAddress
      name:Amgen, One Amgen Center Way
      address:
         name:Amgen, One Amgen Center Way, Thousand Oaks, USA
         type:PostalAddress
      name:Purdue University
      address:
         name:Department of Biochemistry, Purdue University, West Lafayette, USA
         type:PostalAddress
      name:Center for Plant Biology, Purdue University
      address:
         name:Center for Plant Biology, Purdue University, West Lafayette, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Kankan Wang
      affiliation:
            name:Purdue University
            address:
               name:Department of Biochemistry, Purdue University, West Lafayette, USA
               type:PostalAddress
            type:Organization
      name:Raymond J. Deshaies
      affiliation:
            name:Amgen, One Amgen Center Way
            address:
               name:Amgen, One Amgen Center Way, Thousand Oaks, USA
               type:PostalAddress
            type:Organization
      name:Xing Liu
      affiliation:
            name:Purdue University
            address:
               name:Department of Biochemistry, Purdue University, West Lafayette, USA
               type:PostalAddress
            type:Organization
            name:Center for Plant Biology, Purdue University
            address:
               name:Center for Plant Biology, Purdue University, West Lafayette, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Biochemistry, Purdue University, West Lafayette, USA
      name:Amgen, One Amgen Center Way, Thousand Oaks, USA
      name:Department of Biochemistry, Purdue University, West Lafayette, USA
      name:Center for Plant Biology, Purdue University, West Lafayette, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(386)

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