Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

CAP-Gly Domain-Containing Linker Protein 1, human

Known as: Reed-Sternberg Microtubule-Associated Protein, CAP-Gly Domain-Containing Linker Protein 1, Cytoplasmic Linker Protein 170 
CAP-Gly domain-containing linker protein 1 (1427 aa, ~161 kDa) is encoded by the human CLIP1 gene. This protein plays a role in both centrosome… Expand
National Institutes of Health

Related topics

Related topics

12 relations
CLIP1 geneCLIP1 wt AlleleCell MovementCytokinesis
Expand

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2010
Highly Cited
2010
AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP-170 phosphorylation
AMP-activated protein kinase (AMPK) is an energy-sensing Ser/Thr protein kinase originally shown to be regulated by AMP. AMPK is… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
2010
Highly Cited
2010
Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments
CLIP‐170 is implicated in the formation of kinetochore–microtubule attachments through direct interaction with the dynein… Expand
Highly Cited
2007
Highly Cited
2007
Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1.
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule… Expand
  • figure 1
  • figure 2
  • table 1
  • figure 3
  • figure 4
Highly Cited
2005
Highly Cited
2005
Interactions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior.
CLIP-170 belongs to a group of proteins (+TIPs) with the enigmatic ability to dynamically track growing microtubule plus-ends… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
2004
Highly Cited
2004
Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization
Cytoplasmic linker protein (CLIP)-170, CLIP-115, and the dynactin subunit p150Glued are structurally related proteins, which… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
2002
Highly Cited
2002
The FKBP12‐rapamycin‐associated protein (FRAP) is a CLIP‐170 kinase
CLIP‐170/Restin belongs to a family of conserved microtubule (MT)‐associated proteins, which are important for MT organization… Expand
Highly Cited
1999
Highly Cited
1999
Antiangiogenic activity of restin, NC10 domain of human collagen XV: comparison to endostatin.
Based on a homology search with endostatin, the C-terminus 185 aa of collagen XVIII, we report the cloning, expression, and… Expand
Highly Cited
1999
Highly Cited
1999
Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends.
Cytoplasmic dynein is a minus end-directed microtubule motor responsible for centripetal organelle movement and several aspects… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
1998
Highly Cited
1998
Evidence for a Role of CLIP-170 in the Establishment of Metaphase Chromosome Alignment
CLIPs (cytoplasmic linker proteins) are a class of proteins believed to mediate the initial, static interaction of organelles… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Highly Cited
1994
Highly Cited
1994
Molecular characterization of two functional domains of CLIP-170 in vivo.
CLIP-170 is a microtubule-binding protein isolated from HeLa cells that is involved in the interaction of endosomes with… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE