We are analyzing https://link.springer.com/chapter/10.1007/978-1-4614-3229-6_4.

Title:
Death by Caspase Dimerization | SpringerLink
Description:
Controlled cell death, or apoptosis, occurs in response to many different environmental stimuli. The apoptotic cascade that occurs within the cell in response to these cues leads to morphological and biochemical changes that trigger the dismantling and packaging of...
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Keywords {🔍}

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Topics {✒️}

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Questions {❓}

Apoptosis in the treatment of cancer: a promise kept?
The death domain superfamily: a tale of two interfaces?

Schema {🗺️}

ScholarlyArticle:
      headline:Death by Caspase Dimerization
      pageEnd:73
      pageStart:55
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4614-3229-6.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Protein Dimerization and Oligomerization in Biology
         isbn:
            978-1-4614-3229-6
            978-1-4614-3228-9
         type:Book
      publisher:
         name:Springer New York
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Sarah H. MacKenzie
            affiliation:
                  name:North Carolina State University
                  address:
                     name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:A. Clay Clark
            affiliation:
                  name:North Carolina State University
                  address:
                     name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Adaptor Molecule, Central Cavity, Dime Interface, Protein Dimerization, Allosteric Site
      description:Controlled cell death, or apoptosis, occurs in response to many different environmental stimuli. The apoptotic cascade that occurs within the cell in response to these cues leads to morphological and biochemical changes that trigger the dismantling and packaging of the cell. Caspases are a family of cysteine-dependent aspartate-directed proteases that play an integral role in the cascade that leads to apoptosis. Caspases are grouped as either initiators or effectors of apoptosis, depending on where they enter the cell death process. Prior to activation, initiator caspases are present as monomers that must dimerize for full activation whereas effector caspases are present as dimeric zymogens that must be processed for full activation. The stability of the dimer may be due predominately to the interactions in the dimer interface as each caspase has unique properties in this region that lend to its specific mode of activation. Moreover, dimerization is responsible for active site formation because both monomers contribute residues that enable the formation of a fully functional active site. Overall, dimerization plays a key role in the ability of caspases to form fully functional proteases.
      datePublished:2012
      isAccessibleForFree:
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         type:WebPageElement
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Book:
      name:Protein Dimerization and Oligomerization in Biology
      isbn:
         978-1-4614-3229-6
         978-1-4614-3228-9
Organization:
      name:Springer New York
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:North Carolina State University
      address:
         name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
         type:PostalAddress
      name:North Carolina State University
      address:
         name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Sarah H. MacKenzie
      affiliation:
            name:North Carolina State University
            address:
               name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
               type:PostalAddress
            type:Organization
      name:A. Clay Clark
      affiliation:
            name:North Carolina State University
            address:
               name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
      name:Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

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