The Experts below are selected from a list of 321 Experts worldwide ranked by ideXlab platform
Wolf Dietrich Heyer - One of the best experts on this subject based on the ideXlab platform.
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a role of sep1 kem1 xrn1 as a microtubule associated protein in saccharomyces cerevisiae
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
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A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae.
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
H Interthal - One of the best experts on this subject based on the ideXlab platform.
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a role of sep1 kem1 xrn1 as a microtubule associated protein in saccharomyces cerevisiae
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
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A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae.
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
C Bellocq - One of the best experts on this subject based on the ideXlab platform.
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a role of sep1 kem1 xrn1 as a microtubule associated protein in saccharomyces cerevisiae
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
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A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae.
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
Jurg Bahler - One of the best experts on this subject based on the ideXlab platform.
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a role of sep1 kem1 xrn1 as a microtubule associated protein in saccharomyces cerevisiae
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
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A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae.
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
Vladimir I Bashkirov - One of the best experts on this subject based on the ideXlab platform.
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a role of sep1 kem1 xrn1 as a microtubule associated protein in saccharomyces cerevisiae
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
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A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae.
The EMBO Journal, 1995Co-Authors: H Interthal, C Bellocq, Jurg Bahler, Vladimir I Bashkirov, S Edelstein, Wolf Dietrich HeyerAbstract:Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy Defect, impaired spindle pole body separation, and Defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a Structural Defect accounting for the benomyl hypersensitivity, rather than a regulatory Defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of porcine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
