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Total synthesis and biological evaluation of aseries of macrocyclic hybrids and analogues of the antimitotic natural products Dictyostatin,Discodermolide, and Taxol
Title
Total synthesis and biological evaluation of aseries of macrocyclic hybrids and analogues of the antimitotic natural products Dictyostatin,Discodermolide, and Taxol.
Creator
Paterson, Ian, Naylor, G. J., Gardner, Nicola M., Guzman, Esther A., Wright, Amy E.
Date Issued
2011
PURL
http://purl.flvc.org/fau/fd/FA00007463
Subject Headings
Macrolides, Antimitotic Agents, Natural products, Tubulin
Format
Document (PDF)
Tubulin polymerizing activity of dictyostatin-1, a polyketide of marine sponge origin
Title
Tubulin polymerizing activity of dictyostatin-1, a polyketide of marine sponge origin.
Creator
Isbrucker, Richard A., Cummins, Jennifer, Pomponi, Shirley A., Longley, Ross E., Wright, Amy E.
Date Issued
2003
PURL
http://purl.flvc.org/FCLA/DT/2848313
Subject Headings
Tubulins, Cytotaxonomy, Antimitotic agents, Polyketides, Cells
Format
Document (PDF)
Total synthesis of a potent hybrid of the anticancer natural products dictyostatin and discodermolide.
Title
Total synthesis of a potent hybrid of the anticancer natural products dictyostatin and discodermolide.
Creator
Paterson, Ian, Naylor, G. J., Wright, Amy E.
Date Issued
2008
PURL
http://purl.flvc.org/fau/fd/FA00007062
Subject Headings
Antineoplastic agents, Macrolides, Polyketides, Tubulin Modulators, Marine natural products, Sponges
Format
Document (PDF)
Total synthesis of a library of designed hybrids of the microtubule-stabilising anticancer agents taxol, discodermolide and dictyostatin
Title
Total synthesis of a library of designed hybrids of the microtubule-stabilising anticancer agents taxol, discodermolide and dictyostatin.
Creator
Paterson, Ian, Naylor, G. J., Fujita, T., Guzman, Esther A., Wright, Amy E.
Date Issued
2010
PURL
http://purl.flvc.org/fau/fd/FA00007065
Subject Headings
Antineoplastic agents, Paclitaxel, Polyketides, Microtubules, Tubulin Modulators, Marine natural products
Format
Document (PDF)
The microtubule-stabilizing agent discodermolide competitively inhibits the binding of paclitaxel (Taxol) to tubulin polymers, enhances tubulin nucleation reactions more potently than paclitaxel, and inhibits the growth of paclitaxel-resistant cells.
Title
The microtubule-stabilizing agent discodermolide competitively inhibits the binding of paclitaxel (Taxol) to tubulin polymers, enhances tubulin nucleation reactions more potently than paclitaxel, and inhibits the growth of paclitaxel-resistant cells.
Creator
Kowalski, R. J., Giannakakou, P., Gunasekera, Sarath P., Longley, Ross E., Day, B. W., Hamel, E., Harbor Branch Oceanographic Institute
Date Issued
1997
PURL
http://purl.flvc.org/fau/fd/FA00007052
Subject Headings
Marine natural products, Cytotoxins, Tubulin Modulators, Paclitaxel, Lactones, Sponges
Format
Document (PDF)
Structure-activity relationship studies of Discodermolide and its semisynthetic acetylated analogs on microtubule function and cytotoxicity
Title
Structure-activity relationship studies of Discodermolide and its semisynthetic acetylated analogs on microtubule function and cytotoxicity.
Creator
Isbrucker, Richard A., Harbor Branch Oceanographic Institute
Date Issued
2001
PURL
http://purl.flvc.org/FCLA/DT/2783239
Subject Headings
Paclitaxel, Sponges --Research, Marine natural products, Tubulins, Cytotoxicity tests, Immunologic
Format
Document (PDF)
Stereochemical determination of dictyostatin, a novel microtubule-stabilising macrolide from the marine sponge Corallistidae sp.
Title
Stereochemical determination of dictyostatin, a novel microtubule-stabilising macrolide from the marine sponge Corallistidae sp.
Creator
Paterson, Ian, Britton, R., Delgado, Oscar, Wright, Amy E.
Date Issued
2004
PURL
http://purl.flvc.org/fau/fd/FA00007061
Subject Headings
Macrolides, Sponges, Tubulin Modulators, Stereochemistry, Microtubules, Polyketides, Antimitotic Agents
Format
Document (PDF)
Contributions of dynactin's p150[Glued] subunit's binding domains to microtubule anchoring at the centrosome
Title
Contributions of dynactin's p150[Glued] subunit's binding domains to microtubule anchoring at the centrosome.
Creator
Schneider, Rebecca., Harriet L. Wilkes Honors College
Abstract/Description
Intracellular transport carries out very important roles within the cell including mitosis, organization, and organelle function. In order for effective transport using the motor protein dynein, a cofactor named dynactin is required. Of dynactin's many subunits, p150[Glued] holds the most responsibility for effective microtubule organization throughout the cell and the necessary anchoring at the centrosome. P150[Glued] holds two areas of high binding potential, the CAP-Gly region and the...
Show moreIntracellular transport carries out very important roles within the cell including mitosis, organization, and organelle function. In order for effective transport using the motor protein dynein, a cofactor named dynactin is required. Of dynactin's many subunits, p150[Glued] holds the most responsibility for effective microtubule organization throughout the cell and the necessary anchoring at the centrosome. P150[Glued] holds two areas of high binding potential, the CAP-Gly region and the Basic region. Each of these binding domains have different binding potentials and affinities for microtubules. The CAP-Gly region binds tightly the microtubules for a longer period of tiem ; the Basic region binds loosely to microtubules. Throughout the course of my research, I manipulated these two regions binding affinity for microtubules and evaluated the resulting cells ability to effectively organize microtubules and anchor them properly at the centrosome.
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Date Issued
2012
PURL
http://purl.flvc.org/FAU/3359326
Subject Headings
Cytoskeletal proteins, Microtubules, Centrosomes, Cell organelles, Formation, Molecular biology, Tubulins
Format
Document (PDF)
Differential functionality of microtubule binding motifs in the p150[Glued] subunit of dynactin
Title
Differential functionality of microtubule binding motifs in the p150[Glued] subunit of dynactin.
Creator
Mallen, Michael Luis., Harriet L. Wilkes Honors College
Abstract/Description
Dynactin is a multi-subunit protein complex that is the required cofactor for the cytoplasmic motor protein, dynein. Dynactin is critical for cytoplasmic activities such as vesicle transport, cytoskeletal organization, membrane organization and mitotic progression as it serves to increase processivity of dynein. The main subunit in focus for this study is the sidearm extension p150Glued. On the exposed end (N-terminus) lie two different microtubule binding motifs: CAP-Gly and Basic. CAP-Gly...
Show moreDynactin is a multi-subunit protein complex that is the required cofactor for the cytoplasmic motor protein, dynein. Dynactin is critical for cytoplasmic activities such as vesicle transport, cytoskeletal organization, membrane organization and mitotic progression as it serves to increase processivity of dynein. The main subunit in focus for this study is the sidearm extension p150Glued. On the exposed end (N-terminus) lie two different microtubule binding motifs: CAP-Gly and Basic. CAP-Gly has a high binding affinity for microtubules, while Basic binds the microtubules quite weakly. It is at this location that dynactin is proposed to assist in the processivity of transporting cargo long distances in the cell, by providing additional support for the dynein molecule as it progresses along the microtubule. Analysis of the effects of overexpression of these motifs, alone or in tandem, suggested that there was no disruption of the dynein/dynactin interaction, but its ability to act in a processive manner had been perturbed. Effects on non-dynamic processes, such as Golgi localization and microtubule organization were generally weak, but effects were greater on y-tubulin organization. While this could suggest a defect in centrosome organization, we propose that it instead shows that cargo motility in the affected cells is defective, and that transport of centrosomal proteins to the centrosome is interrupted, suggesting a broader cargo-transport defect may be evident in these cells.
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Date Issued
2007
PURL
http://purl.flvc.org/FAU/11613
Subject Headings
Cytoskeletal proteins, Tubulins, Microtubules, Centrosomes, Cell organelles, Formation
Format
Document (PDF)
Centrosome recruitment
Title
Centrosome recruitment: analysis of protein changes during S phase.
Creator
Raborn, Erik., Harriet L. Wilkes Honors College
Abstract/Description
The centrosome is a dynamic and highly active organelle within the cell. It plays a pivotal role in mitosis driving several of the physical changes that are taking place. The centrosome self-replicates before mitosis in order to set up two spindle poles on opposite sides of the cell. This leads to the creation of a mother and daughter centrosomes within a cell that have distinct components. This project will examine the recruitment of proteins to the centrosome as a cell progresses through...
Show moreThe centrosome is a dynamic and highly active organelle within the cell. It plays a pivotal role in mitosis driving several of the physical changes that are taking place. The centrosome self-replicates before mitosis in order to set up two spindle poles on opposite sides of the cell. This leads to the creation of a mother and daughter centrosomes within a cell that have distinct components. This project will examine the recruitment of proteins to the centrosome as a cell progresses through the cell cycle. The proteins examined are (Sd(B-tubulin, (Sf(B-tubulin, Nek 2, Centrin2, p150Glued, EB-1, and dynein intermediate chain. In addition, chromosome arrangement was determined. By examining these proteins we hope to establish a logical order for the interactions of these proteins and their key contributions to cell cycle progression and completion, specifically dealing with the development of the mother and daughter centrosomes.
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Date Issued
2009
PURL
http://purl.flvc.org/FAU/3325085
Subject Headings
Cell organelles, Formation, Cytoskeletal proteins, Cell division, Tubulins, Microtubules
Format
Document (PDF)