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1 CENP-F is a nonmotor microtubule-binding protein that pa
2 CENP-F is important for the formation of proper kinetoch
3 CENP-F, hBUBR1, and CENP-E assembled onto kinetochores i
4 CENP-F-driven mitochondrial transport is linked to growi
5 HC module (comprised of BUB-1(Bub1), HCP-1/2(CENP-F) and CLS-2(CLASP))-dependent pushing acts redunda
6 CP-4 are both required for localization of a CENP-F-like protein, HCP-1, indicating an ordered assemb
7 t throughout the mitotic delay some aligned, CENP-F depleted kinetochores continuously recruit Mad1.
8 f dynein at G2/M that facilitates BICD2- and CENP-F-mediated anchoring of dynein to nuclear pore comp
10 f these, the centromeric proteins CENP-E and CENP-F are preferentially expressed during mitosis and a
11 RhoB and the centromere proteins CENP-E and CENP-F are relevant targets of farnesylation inhibition;
12 rom the COOH-terminal CAAX box of CENP-E and CENP-F are substrates for farnesyl transferase but not g
13 t preventing the farnesylation of CENP-E and CENP-F by treatment with the farnesyl transferase inhibi
14 of the outer kinetochore proteins CENP-E and CENP-F, which are involved in chromosome congression and
19 lization of RanGAP1, Mad1, Mad2, CENP-E, and CENP-F, as well as loss of cold-stable kinetochore-MT in
21 rotubule tips can transport mitochondria and CENP-F-coated artificial cargoes over micrometer-long di
23 ch as anti-p53, anti-p62, anti-Koc, and anti-CENP-F, auto-antibodies to p90 represent a new marker fo
24 ted the dynamic association of LANA and Bub1/CENP-F and the colocalization between Bub1, LANA, and th
26 at included the kinetochore proteins CENP-E, CENP-F, and hBUBR1, a BUB1-related kinase that was found
31 ociation of LANA with centromeric protein F (CENP-F) prompted us to further study whether LANA target
32 crotubule (MT)-binding centromere protein F (CENP-F) was previously shown to play a role exclusively
33 lated association with centromere protein F (CENP-F), allowing ATR to engage replication protein A (R
34 novel and critical localization and role for CENP-F at the centrosome, the major MT organizing center
35 ivation and silencing and a crucial role for CENP-F in efficient assembly of a stable microtubule-kin
38 ata, we hypothesize that chicken CMF1, human CENP-F, mitosin, and mouse LEK1 are members of an emergi
40 murine cDNA, LEK1, that is related to human CENP-F and mitosin and more distantly to chicken CMF1.
42 d 3-5 pN but could exceed 10 pN, identifying CENP-F as a highly effective coupler to shortening MTs.
44 ber of outer kinetochore proteins, including CENP-F [1, 2] and the widely conserved microtubule-assoc
46 Here we show that the absence of nuclear CENP-F does not affect cell cycle progression in S and G
49 (-/-) cells, we demonstrate that ablation of CENP-F protein function eliminates MT repolymerization a
51 research demonstrating the strong binding of CENP-F to the MT network, support the conclusion that CE
52 olymerization block shows that disruption of CENP-F function impacts MT nucleation and anchoring rath
53 how that the N-terminal MT-binding domain of CENP-F prefers curled oligomers of tubulin relative to M
54 the amino- and carboxyl-terminal domains of CENP-F as well as the carboxyl-terminal (non-kinesin) do
56 als a major new localization and function of CENP-F at the centrosome that is likely to impact a broa
65 F" pathways act sequentially, with Nup133 or CENP-F RNAi arresting nuclei close to the ventricular su
66 on between LANA and the kinetochore proteins CENP-F and Bub1 is important for KSHV genome tethering a
67 rised of the kinase BUB-1, the two redundant CENP-F orthologs HCP-1/2, and the CLASP family member CL
68 relationship between HCP-1/2, two redundant CENP-F-like proteins, and CLASP(CLS-2) in Caenorhabditis
69 the MT network, support the conclusion that CENP-F is a powerful regulator of MT dynamics during int
71 r novel genetic deletion model, we show that CENP-F also regulates a broader range of cellular functi
73 e and previous observations, we suggest that CENP-F might act as a transporter of mitochondria and ot
75 show that the conserved kinesin CeMCAK, the CENP-F-related proteins HCP-1 and HCP-2, and the core ki