The conserved KMN network constitutes the core microtubule-binding site of the kinetochore.
By I. Cheeseman, J. Chappie, E. Wilson-Kubalek, A. Desai. Cell, 2006
1,069 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/d7991f0fe8194162f75fa3abb7f5a3a83125f450
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Citations in the corpus
- Microtubule attachment and spindle assembly checkpoint signaling at the kinetochore (2012, background): “relative to the outer kinetochore is unchanged (2).”
- The spindle-assembly checkpoint in space and time (2007, background): “Before mitosis, other evolutionarily conserved proteins, including Spc105 (KNL-1 in Caenorhabditis elegans ) and the Mtw1 (MIS12 in humans), Ndc80 (HEC1 in humans) and minichromosome maintenance protein-21 (MCM21) complexes, are recruited to the kinetochore outer plate to form attachment sites for ”
- Shared and separate functions of polo-like kinases and aurora kinases in cancer (2010, background): “In this conformation, it can phosphorylate several kinetochore-associated proteins, such as highly expressed in cancer (HEC1; also known as NDC80), DSN1 (also known as KNL3) and KNL1 (also known as CASC5 or blinkin) thereby modifying the microtubule binding affinity of the KMN network”
- Kinetochore microtubule dynamics and attachment stability are regulated by Hec1. (2006, positive): “In support of this, recent evidence from C. elegans and human cells suggests that the Ndc80 complex directly binds MTs, and this binding is regulated, in part, by Aurora B kinase (Cheeseman et al., 2006 [this issue of Cell]).”
- Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling (2013, background): “In a few well-characterized cases, phosphorylation negatively regulates protein interactions at the kinetochore (e.g., Cheeseman et al., 2006; DeLuca et al., 2006; Meadows et al., 2011; Rosenberg et al., 2011).”