Structural Biology of the Separase–Securin Complex with Crucial Roles in Chromosome Segregation

Luo, S., & Tong, L. (2018). Structural Biology of the Separase–Securin Complex with Crucial Roles in Chromosome Segregation. Current Opinion in Structural Biology, 114-122.

Type

Journal article

Intellectual base

Primary research

Year

2018

Pages

114-122

DOI

10.1016/j.sbi.2018.01.012

DOI registrant

Elsevier

Link

https://pubmed.ncbi.nlm.nih.gov/29452922/

Cited by

1 citation across 1 artifact.

Domain-specific

• Securin
  • Securin is a conserved protein regulator of the metaphase-to-anaphase transition.

    Supported in partVerified against the work's full text

    Establishes securin as a natively unfolded protein that inhibits and chaperones separase, holding it in a complex until anaphase onset, but does not state that securin is conserved.

    “Securin, a natively unfolded protein in solution [ 24 , 25 ], is the first reported regulator of separase and acts as both a chaperone and an inhibitor [ 26 – 33 ]. Securin binds to nascent separase protein co-translationally to help its proper folding and forms a stable complex with separase until the onset of anaphase.”

    Read by an automated reader; not a human review. How support was checked

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Registry ID ref:9fa733c37679 · see in the full table