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1
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0025013883
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Components of the yeast spindle and spindle pole body
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Rout MP, Kilmartin JV Components of the yeast spindle and spindle pole body. J Cell Biol. 111:1990;1913-1927.
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Rout, M.P.1
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0027382276
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A spacer protein in the Saccharomyces cerevisiae spindle pole body whose transcript is cell cycle-regulated
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Kilmartin JV, Dyos SL, Kershaw D, Finch JT A spacer protein in the Saccharomyces cerevisiae spindle pole body whose transcript is cell cycle-regulated. J Cell Biol. 123:1993;1175-1184.
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Kilmartin, J.V.1
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Kershaw, D.3
Finch, J.T.4
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3
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0030683637
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Spc98p and Spc97p of the yeast γ-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p
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Knop M, Schiebel E Spc98p and Spc97p of the yeast γ-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p. EMBO J. 16:1997;6985-6995.
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Knop, M.1
Schiebel, E.2
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4
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0031830660
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A genetic analysis of interactions with Spc110p reveals distinct functions of Spc97p and Spc98p, components of the yeast γ-tubulin complex
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Spc98p binds more strongly to Spc110p than does Spc97p, suggesting the γ tubulin complex interacts with the SPB through a Spc110p-Spc98p linkage.
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Nguyen T, Vinh DBN, Crawford DK, Davis TN A genetic analysis of interactions with Spc110p reveals distinct functions of Spc97p and Spc98p, components of the yeast γ-tubulin complex. Mol Biol Cell. 9:1998;2201-2216. Spc98p binds more strongly to Spc110p than does Spc97p, suggesting the γ tubulin complex interacts with the SPB through a Spc110p-Spc98p linkage.
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Mol Biol Cell
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Nguyen, T.1
Vinh, D.B.N.2
Crawford, D.K.3
Davis, T.N.4
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5
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0030728492
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Stu2p: A microtubule-binding protein that is an essential component of the yeast spindle pole body
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Stu2p was isolated as a suppressor of the tub2-403 cold-sensitive β tubulin allele. The Stu2p protein binds laterally to microtubules in vitro and SPBs in vivo in the absence of microtubules. Stu2p may serve to increase the strength of the microtubule binding to the SPBs.
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Wang PJ, Huffaker TC Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body. J Cell Biol. 139:1997;1271-1280. Stu2p was isolated as a suppressor of the tub2-403 cold-sensitive β tubulin allele. The Stu2p protein binds laterally to microtubules in vitro and SPBs in vivo in the absence of microtubules. Stu2p may serve to increase the strength of the microtubule binding to the SPBs.
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J Cell Biol
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Wang, P.J.1
Huffaker, T.C.2
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6
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0031756101
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SPC72: A spindle pole component required for spindle orientation in the yeast Saccharomyces cerevisiae
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Spc72p was identified through monoclonal antibodies to purified SPBs. The protein is found on SPBs and the bridge. spc72 mutants have diminished cytoplasmic microtubules and spindle-positioning defects. The results add significantly to our understanding of how the SPB stabilizes microtubules after nucleation.
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Soues S, Adams IR SPC72: a spindle pole component required for spindle orientation in the yeast Saccharomyces cerevisiae. J Cell Sci. 111:1998;2809-2818. Spc72p was identified through monoclonal antibodies to purified SPBs. The protein is found on SPBs and the bridge. spc72 mutants have diminished cytoplasmic microtubules and spindle-positioning defects. The results add significantly to our understanding of how the SPB stabilizes microtubules after nucleation.
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(1998)
J Cell Sci
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Soues, S.1
Adams, I.R.2
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7
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0032527750
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Receptors determine the cellular localization of a γ-tubulin complex and thereby the site of microtubule formation
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The authors describe a cytoplasmic protein Spc72p which may function to link the γ-tubulin complex to the SPB on the cytoplasmic side. Both loss-of-function and overexpression studies suggest this protein is part of the pathway nucleating or stabilizing cytoplasmic microtubules.
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Knop M, Schiebel E Receptors determine the cellular localization of a γ-tubulin complex and thereby the site of microtubule formation. EMBO J. 17:1998;3952-3967. The authors describe a cytoplasmic protein Spc72p which may function to link the γ-tubulin complex to the SPB on the cytoplasmic side. Both loss-of-function and overexpression studies suggest this protein is part of the pathway nucleating or stabilizing cytoplasmic microtubules.
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(1998)
EMBO J
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Knop, M.1
Schiebel, E.2
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8
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0032100813
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The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly
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The Spc72p protein was identified using a two-hybrid screen from association with Stu2p. Loss of Spc72p produces both cytoplasmic and spindle microtubule defects. These results suggest a linkage between the microtubule binding protein Stu2p and the SPB.
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Chen XP, Yin H, Huffaker TC The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly. J Cell Biol. 141:1998;1169-1179. The Spc72p protein was identified using a two-hybrid screen from association with Stu2p. Loss of Spc72p produces both cytoplasmic and spindle microtubule defects. These results suggest a linkage between the microtubule binding protein Stu2p and the SPB.
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J Cell Biol
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Chen, X.P.1
Yin, H.2
Huffaker, T.C.3
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9
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0016731336
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Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae
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Byers B, Goetsch L Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae. J Bacteriol. 124:1975;511-523.
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Byers, B.1
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0031669666
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Saccharomyces cerevisiae cells with defective spindle pole body outer plaques accomplish nuclear migration via half-bridge-organized microtubules
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The identification of Cnm67p, a protein required for formation or stability of the outer plaque of the SPB. In yeast cells with cnm67 mutations, the half-bridge retains cytoplasmic microtubule nucleating capacity.
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Brachat A, Kilmartin JV, Wach A, Philippsen P Saccharomyces cerevisiae cells with defective spindle pole body outer plaques accomplish nuclear migration via half-bridge-organized microtubules. Mol Biol Cell. 9:1998;977-991. The identification of Cnm67p, a protein required for formation or stability of the outer plaque of the SPB. In yeast cells with cnm67 mutations, the half-bridge retains cytoplasmic microtubule nucleating capacity.
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Brachat, A.1
Kilmartin, J.V.2
Wach, A.3
Philippsen, P.4
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11
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0032053785
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The fission yeast SPB component Cut12 links bipolar spindle formation to mitotic control
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The identification of Cut12, an inner SPB component required for spindle assembly. The cut12+ gene is allelic with stf1+ a bypass suppressor of cdc25 mutants and Cut12 may be a substrate of the Cdc2 kinase.
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Bridge AJ, Morphew M, Bartlett R, Hagan IM The fission yeast SPB component Cut12 links bipolar spindle formation to mitotic control. Genes Dev. 12:1998;927-942. The identification of Cut12, an inner SPB component required for spindle assembly. The cut12+ gene is allelic with stf1+ a bypass suppressor of cdc25 mutants and Cut12 may be a substrate of the Cdc2 kinase.
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Genes Dev
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Bridge, A.J.1
Morphew, M.2
Bartlett, R.3
Hagan, I.M.4
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12
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0031750102
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Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry
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Purified SPB preparations were analyzed by mass spectrographic analysis, identifying many new SPB components. Localization was confirmed by epitope-tagging. Some proteins are apparently unique to the SPB, others are also found throughout the spindle.
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Wigge PA, Jensen ON, Holmes S, Soues S, Mann M, Kilmartin JV Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. J Cell Biol. 141:1998;967-977. Purified SPB preparations were analyzed by mass spectrographic analysis, identifying many new SPB components. Localization was confirmed by epitope-tagging. Some proteins are apparently unique to the SPB, others are also found throughout the spindle.
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(1998)
J Cell Biol
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Wigge, P.A.1
Jensen, O.N.2
Holmes, S.3
Soues, S.4
Mann, M.5
Kilmartin, J.V.6
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13
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0030933383
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The Saccharomyces cerevisiae kinesin-related motor Kar3p acts at pre-anaphase spindle poles to limit the number and length of cytoplasmic microtubules
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Saunders W, Hornack D, Lengyel V, Deng C The Saccharomyces cerevisiae kinesin-related motor Kar3p acts at pre-anaphase spindle poles to limit the number and length of cytoplasmic microtubules. J Cell Biol. 137:1997;417-431.
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Saunders, W.1
Hornack, D.2
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Deng, C.4
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14
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0028245510
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Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends
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Endow S, Kang S, Satterwhite L, Rose M, Skeen V, Salmon E Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends. EMBO J. 13:1994;2708-2713.
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Endow, S.1
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Satterwhite, L.3
Rose, M.4
Skeen, V.5
Salmon, E.6
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15
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0032539526
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X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg ADP to 2.3 Å resolution
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The first X-ray crystallographic structure of a minus-end-directed kinesin motor. Structural variation between Kar3p and plus-end-directed motors suggest possible mechanisms for microtubule destabilization and minus-end-directed movement.
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Gulick AM, Song H, Endow SA, Rayment I X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg ADP to 2.3 Å resolution. Biochemistry. 37:1998;1769-1776. The first X-ray crystallographic structure of a minus-end-directed kinesin motor. Structural variation between Kar3p and plus-end-directed motors suggest possible mechanisms for microtubule destabilization and minus-end-directed movement.
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Biochemistry
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Gulick, A.M.1
Song, H.2
Endow, S.A.3
Rayment, I.4
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16
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0032584067
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Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha, beta)methylenediphosphonate
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Muller-Reichert T, Chretien D, Severin F, Hyman AA Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha, beta)methylenediphosphonate. Proc Natl Acad Sci USA. 95:1998;3661-3666.
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Muller-Reichert, T.1
Chretien, D.2
Severin, F.3
Hyman, A.A.4
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17
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0030931849
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Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins
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Cottingham FR, Hoyt MA Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins. J Cell Biol. 138:1997;1041-1053.
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Cottingham, F.R.1
Hoyt, M.A.2
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18
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0031908741
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The Kar3p and Kip2p motors function antagonistically at the spindle poles to influence cytoplasmic microtubule numbers
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Loss of Kar3p stimulates cytoplasmic microtubule growth whereas loss of Kip2p greatly reduces the length of cytoplasmic microtubules. Both of these motors function at the SPB and when both are deleted the microtubules levels return to near normal suggesting a balanced antagonism of these proteins acting at the minus ends of the microtubules.
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Huyett A, Kahana J, Silver P, Zeng X, Saunders W The Kar3p and Kip2p motors function antagonistically at the spindle poles to influence cytoplasmic microtubule numbers. J Cell Sci. 111:1998;295-301. Loss of Kar3p stimulates cytoplasmic microtubule growth whereas loss of Kip2p greatly reduces the length of cytoplasmic microtubules. Both of these motors function at the SPB and when both are deleted the microtubules levels return to near normal suggesting a balanced antagonism of these proteins acting at the minus ends of the microtubules.
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(1998)
J Cell Sci
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Huyett, A.1
Kahana, J.2
Silver, P.3
Zeng, X.4
Saunders, W.5
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19
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0031878092
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The kinesin-related proteins, Kip2p and Kip3p, function differently in nuclear migration in yeast
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Miller RK, Heller KK, Frisen L, Wallack DL, Loayza D, Gammie AE, Rose MD The kinesin-related proteins, Kip2p and Kip3p, function differently in nuclear migration in yeast. Mol Biol Cell. 9:1998;2051-2068.
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Miller, R.K.1
Heller, K.K.2
Frisen, L.3
Wallack, D.L.4
Loayza, D.5
Gammie, A.E.6
Rose, M.D.7
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20
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0030668938
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Astral microtubule dynamics in yeast: A microtubule-based searching mechanism for spindle orientation and nuclear migration into the bud
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Green fluorescent protein (GFP)-labeled dynein was used to visualize nuclear movement with respect to cytoplasmic microtubule growth. These observations suggest a pushing mechanism for nuclear movement from growth of cytoplasmic microtubules.
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Shaw SL, Yeh E, Maddox P, Salmon ED, Bloom K Astral microtubule dynamics in yeast: a microtubule-based searching mechanism for spindle orientation and nuclear migration into the bud. J Cell Biol. 139:1997;985-994. Green fluorescent protein (GFP)-labeled dynein was used to visualize nuclear movement with respect to cytoplasmic microtubule growth. These observations suggest a pushing mechanism for nuclear movement from growth of cytoplasmic microtubules.
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Shaw, S.L.1
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Bloom, K.5
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0027097142
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A low copy number central sequence with strict symmetry and unusual chromatin structure in fission yeast centromere
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Takahashi K, Murakami S, Chikashige Y, Funabiki H, Niwa O, Yanagida M A low copy number central sequence with strict symmetry and unusual chromatin structure in fission yeast centromere. Mol Biol Cell. 3:1992;819-835.
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Yanagida, M.6
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0027305680
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Centromeres of the fission yeast Schizosaccharomyces pombe are highly variable genetic loci
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Steiner NC, Hahnenberger KM, Clarke L Centromeres of the fission yeast Schizosaccharomyces pombe are highly variable genetic loci. Mol Cell Biol. 13:1993;4578-4587.
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Steiner, N.C.1
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0026013226
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A 240kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere
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Lechner J, Carbon J A 240kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere. Cell. 64:1991;717-725.
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Factors required for the binding of reassembled yeast kinetochores to microtubules in vitro
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Sorger PK, Severin FF, Hyman AA Factors required for the binding of reassembled yeast kinetochores to microtubules in vitro. J Cell Biol. 127:1994;995-1008.
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Sorger, P.K.1
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Hyman, A.A.3
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26
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0032482756
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Detection of GTP and Pi in wild-type and mutated yeast microtubules: Implications for the role of the GTP/GDP-Pi cap in microtubule dynamics
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GTP hydrolysis was measured in brain and yeast microtubules and the GTP in yeast was found to be relatively small. Yeast tubulin mutants with increased dynamic instability did not have reduced cap size implying additional mechanisms governing microtubule dynamics at the plus ends.
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Dougherty CA, Himes RH, Wilson L, Farrell KW Detection of GTP and Pi in wild-type and mutated yeast microtubules: implications for the role of the GTP/GDP-Pi cap in microtubule dynamics. Biochemistry. 37:1998;10861-10865. GTP hydrolysis was measured in brain and yeast microtubules and the GTP in yeast was found to be relatively small. Yeast tubulin mutants with increased dynamic instability did not have reduced cap size implying additional mechanisms governing microtubule dynamics at the plus ends.
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Biochemistry
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Dougherty, C.A.1
Himes, R.H.2
Wilson, L.3
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27
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0031451181
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Probing the architecture of a simple kinetochore using DNA-protein crosslinking
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The DNA-binding properties of the CBF3 centromere binding activity was examined. Three proteins Ctf13p, Cep3p and Ndc10p make direct contact with the CDEIII DNA. Ndc10p also forms an asymmetrical extended association with the DNA to one side of the CDEIII region.
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Espelin CW, Kaplan KB, Sorger PK Probing the architecture of a simple kinetochore using DNA-protein crosslinking. J Cell Biol. 139:1997;1383-1396. The DNA-binding properties of the CBF3 centromere binding activity was examined. Three proteins Ctf13p, Cep3p and Ndc10p make direct contact with the CDEIII DNA. Ndc10p also forms an asymmetrical extended association with the DNA to one side of the CDEIII region.
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Espelin, C.W.1
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The chromatin structure of centromeres from fission yeast: Differentiation of the central core that correlates with function
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Polizzi C, Clarke L The chromatin structure of centromeres from fission yeast: differentiation of the central core that correlates with function. J Cell Biol. 112:1991;191-201.
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Chromatin conformation of yeast centromeres
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Bloom KS, Amaya E, Carbon J, Clarke L, Hill A, Yeh E Chromatin conformation of yeast centromeres. J Cell Biol. 99:1984;1559-1568.
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0028104174
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Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere
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Sullivan KF, Hechenberger M, Masri K Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere. J Cell Biol. 127:1994;581-592.
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0028946805
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A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis
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Stoler S, Keith KC, Curnick KE, Fitzgerald-Hayes M A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. Genes Dev. 9:1995;573-586.
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0032483564
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Cse4p is a component of the core centromere of Saccharomyces cerevisiae
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Cse4p is found at the centromere suggesting a specialized nucleosomal structure. A centrosomal nucleosomal fold model is presented. These results help to elucidate how the chromatin structure becomes specialized to support attatchment of the microtubule.
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Meluh PB, Yang P, Glowczewski L, Koshland D, Smith MM Cse4p is a component of the core centromere of Saccharomyces cerevisiae. Cell. 94:1998;607-613. Cse4p is found at the centromere suggesting a specialized nucleosomal structure. A centrosomal nucleosomal fold model is presented. These results help to elucidate how the chromatin structure becomes specialized to support attatchment of the microtubule.
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Cell
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Meluh, P.B.1
Yang, P.2
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Smith, M.M.5
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33
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0031459979
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Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres
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Trichostatin A treatment increased chromosomal loss and misplaced the transcriptional inhibitor Swi6. These results support a model with histone acetylation and transcriptional repression playing a key linked role in centromere function.
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Ekwall K, Olsson T, Turner BM, Cranston G, Allshire RC Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres. Cell. 91:1997;1021-1032. Trichostatin A treatment increased chromosomal loss and misplaced the transcriptional inhibitor Swi6. These results support a model with histone acetylation and transcriptional repression playing a key linked role in centromere function.
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Ekwall, K.1
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0029859275
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Mutations in the fission yeast silencing factors clr4+ and rik1+ disrupt the localisation of the chromo domain protein Swi6p and impair centromere function
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Ekwall K, Nimmo ER, Javerzat JP, Borgstrom B, Egel R, Cranston G, Allshire R Mutations in the fission yeast silencing factors clr4+ and rik1+ disrupt the localisation of the chromo domain protein Swi6p and impair centromere function. J Cell Sci. 109:1996;2637-2648.
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Ekwall, K.1
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Borgstrom, B.4
Egel, R.5
Cranston, G.6
Allshire, R.7
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