Name | protein is |
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Synonyms | ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2… |
Name | benomyl |
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CAS |
PubMed | Abstract | RScore(About this table) | |
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15023545 | Wysocka M, Rytka J, Kurlandzka A: Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex. Exp Cell Res. 2004 Apr 1;294(2):592-602. Deletion of CSM1 causes incorrect spore formation and meiotic chromosome missegregation together with increased sensitivity of vegetative cells to benomyl and |
0(0,0,0,0) | Details |
10087265 | Manning BD, Barrett JG, Wallace JA, Granok H, Snyder M: Differential regulation of the Kar3p kinesin-related protein by two associated proteins, Cik1p and Vik1p. J Cell Biol. 1999 Mar 22;144(6):1219-33. Disruption of VIK1 causes increased resistance to the microtubule depolymerizing drug benomyl and partially suppresses growth defects of cik1Delta mutants. |
0(0,0,0,0) | Details |
7916461 | Vinh DB, Drubin DG: A yeast TCP-1-like protein is required for actin function in vivo. Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):9116-20. We show that anc2-1 mutants contain abnormal and disorganized actin structures, are defective in cellular morphogenesis, and are hypersensitive to the microtubule inhibitor benomyl. |
1(0,0,0,1) | Details |
9483794 | Winkler AA, Bobok A, Zonneveld BJ, Steensma HY, Hooykaas PJ: The binding factor 5 (Cbf5) of Kluyveromyces lactis are not essential for function. Yeast. 1998 Jan 15;14(1):37-48. The main difference between both yeast proteins and the rat protein is the presence of -rich domain with KKE/D repeats in the C-terminal part of the protein. Deletion of the KKE/D domain in KlCbf5 however, has no discernible effect on growth on rich medium, sensitivity to the microtubule-destabilizing drug benomyl or segregation of a reporter plasmid. |
-rich C-terminal repeats of the centromere-1(0,0,0,1) | Details |
16624915 | Kim JM, Lu L, Shao R, Chin J, Liu B: Isolation of mutations that bypass the requirement of the septation initiation network for septum formation and conidiation in Aspergillus nidulans. Genetics. 2006 Jun;173(2):685-96. Epub 2006 Apr 19. They also rendered hypersensitivity to low doses of the microtubule-depolymerizing agent benomyl for conidiation. Mob1p, an evolutionarily conserved SIN protein, is associated with the most downstream kinase of this cascade in fission yeast. |
1(0,0,0,1) | Details |
10767562 | Shimizu Y, Akashi T, Okuda A, Kikuchi A, Fukui K: NBP1 (Nap1 binding protein 1), an essential gene for G2/M transition of Saccharomyces cerevisiae, encodes a protein of distinct sub-nuclear localization. Gene. 2000 Apr 4;246(1-2):395-404. This protein is also identified for its interaction with Clb2p in vitro. This mutant also confers resistance against benomyl, a microtubule-destabilizing agent. |
1(0,0,0,1) | Details |
12456004 | Schadick K, Fourcade HM, Boumenot P, Seitz JJ, Morrell JL, Chang L, Gould KL, Partridge JF, Allshire RC, Kitagawa K, Hieter P, Hoffman CS: Schizosaccharomyces pombe Git7p, a member of the Saccharomyces cerevisiae Sgtlp family, is required for In addition, git7 mutants are sensitive to the microtubule-destabilizing drug benomyl, although they do not display a chromosome stability defect. The Git7p protein is a member of the Saccharomyces cerevisiae Sgtlp protein family. |
and cyclic AMP signaling, cell wall integrity, and septation. Eukaryot Cell. 2002 Aug;1(4):558-67.1(0,0,0,1) | Details |
7836422 | Ouspenski II, Mueller UW, Matynia A, Sazer S, Elledge SJ, Brinkley BR: Ran-binding protein-1 is an essential component of the Ran/RCC1 molecular switch system in budding yeast. J Biol Chem. 1995 Feb 3;270(5):1975-8. Similar phenotypic consequences of overproduction of either Ran or RanBP1 indicate that the latter protein is a functional component of the Ran/RCC1 molecular switch system, which is implicated in the control of a number of nuclear functions. Our finding that overproduction of two components of this system results in mitotic chromosome nondisjunction and sensitivity to an anti-microtubule drug benomyl suggest their involvement in mitosis as well. |
1(0,0,0,1) | Details |