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Kinetic stabilization of microtubule dynamic instability in vitro by vinblastine

Biochemistry (Easton), 1993-02, Vol.32 (5), p.1285-1293

1993

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The Arc of War: Origins, Escalation, and Transformation by Jack S. Levy and William R. Thompson (review)

Journal of world history, 2013-03, Vol.24 (1), p.179-181

Farrell, Kevin W

2013

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Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae

Biochemistry (Easton), 1993-08, Vol.32 (34), p.8823-8835

1993

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Mutation in the β-Tubulin Signature Motif Suppresses Microtubule GTPase Activity and Dynamics, and Slows Mitosis

Biochemistry (Easton), 2001-12, Vol.40 (51), p.15725-15732

2001

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Taxol stabilization of microtubules in vitro: dynamics of tubulin addition and loss at opposite microtubule ends

Biochemistry (Easton), 1985-09, Vol.24 (19), p.5254-5262

1985

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Microtubule Dynamics Modulated by Guanosine Triphosphate Hydrolysis Activity of β-Tubulin

Science (American Association for the Advancement of Science), 1994-05, Vol.264 (5160), p.839-842

1994

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Role of GTP hydrolysis in microtubule polymerization: evidence for a coupled hydrolysis mechanism

Biochemistry (Easton), 1990-07, Vol.29 (27), p.6489-6498

1990

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Proposed mechanism for colchicine poisoning of microtubules reassembled in vitro from Strongylocentrotus purpuratus sperm tail outer doublet tubulin

Biochemistry (Easton), 1980-06, Vol.19 (13), p.3048-3054

1980

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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

Biochemistry (Easton), 1998-08, Vol.37 (31), p.10861-10865

1998

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Site-Directed Mutagenesis of Putative GTP-Binding Sites of Yeast .beta.-Tubulin: Evidence That .alpha.-, .beta.-, and .gamma.-Tubulins Are Atypical GTPases

Biochemistry (Easton), 1995-06, Vol.34 (22), p.7409-7419

1995

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Drawdown: The American Way of Postwar

1, 2016

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Tubulin-colchicine complexes differentially poison opposite microtubule ends

Biochemistry (Easton), 1984-07, Vol.23 (16), p.3741-3748

1984

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Epilogue

Drawdown, 2020, Vol.8, p.291-294

2020

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EPILOGUE

Drawdown, 2016, p.291

2016

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The Arc of War: Origins, Escalation, and Transformation

Journal of World History, 2013, Vol.24 (1), p.179-181

FARRELL, KEVIN W.

2013

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Getting to the heart of β-tubulin

Trends in cell biology, 1996-08, Vol.6 (8), p.297-303

1996

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Detection of GTP and P i in Wild-Type and Mutated Yeast Microtubules: Implications for the Role of the GTP/GDP−P i Cap in Microtubule Dynamics

Biochemistry (Easton), 1998-08, Vol.37 (31), p.10861-10865

1998

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Characterization of the in vitro reassembly of tubulin derived from stable Strongylocentrotus purpuratus outer doublet microtubules

Biochemistry (Easton), 1979-03, Vol.18 (5), p.905-911

1979

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Outer doublet tubulin reassembly: evidence for opposite end assembly-disassembly at steady state and a disassembly end equilibrium

Biochemistry (Easton), 1979-06, Vol.18 (12), p.2642-2647

1979

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Operation Enduring Freedom: The United States in Afghanistan

The Routledge Handbook of American Military and Diplomatic History, 2013, p.354-361

1, 2013

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Phase Dynamics at Microtubule Ends: The Coexistence of Microtubule Length Changes and Treadmilling

The Journal of cell biology, 1987-04, Vol.104 (4), p.1035-1046

1987

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Kinetics and Steady State Dynamics of Tubulin Addition and Loss at Opposite Microtubule Ends: The Mechanism of Action of Colchicine

Annals of the New York Academy of Sciences, 1986, Vol.466 (1), p.690-708

1986

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Kinetics and Steady State Dynamics of Tubulin Addition and Loss at Opposite Microtubule Ends: The Mechanism of Action of Colchicinea

Annals of the New York Academy of Sciences, 1986-06, Vol.466 (1), p.690-708

1986

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Commercial [ 3H]Glutamate Contains a Contaminant That Labels Tubulin Covalently

Analytical biochemistry, 1995-09, Vol.230 (2), p.350-353

1995

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[37] Isolation of tubulin from nonneural sources

Methods in Enzymology, 1982, Vol.85, p.385-393

Farrell, Kevin W.

1982

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Kinetic stabilization of microtubule dynamic instability in vitro by vinblastine

The Arc of War: Origins, Escalation, and Transformation by Jack S. Levy and William R. Thompson (review)

Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae

Mutation in the β-Tubulin Signature Motif Suppresses Microtubule GTPase Activity and Dynamics, and Slows Mitosis

Taxol stabilization of microtubules in vitro: dynamics of tubulin addition and loss at opposite microtubule ends

Microtubule Dynamics Modulated by Guanosine Triphosphate Hydrolysis Activity of β-Tubulin

Role of GTP hydrolysis in microtubule polymerization: evidence for a coupled hydrolysis mechanism

Proposed mechanism for colchicine poisoning of microtubules reassembled in vitro from Strongylocentrotus purpuratus sperm tail outer doublet tubulin

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

Site-Directed Mutagenesis of Putative GTP-Binding Sites of Yeast .beta.-Tubulin: Evidence That .alpha.-, .beta.-, and .gamma.-Tubulins Are Atypical GTPases

Drawdown: The American Way of Postwar

Tubulin-colchicine complexes differentially poison opposite microtubule ends

Epilogue

EPILOGUE

The Arc of War: Origins, Escalation, and Transformation

Getting to the heart of β-tubulin

Detection of GTP and P i in Wild-Type and Mutated Yeast Microtubules: Implications for the Role of the GTP/GDP−P i Cap in Microtubule Dynamics

Characterization of the in vitro reassembly of tubulin derived from stable Strongylocentrotus purpuratus outer doublet microtubules

Outer doublet tubulin reassembly: evidence for opposite end assembly-disassembly at steady state and a disassembly end equilibrium

Operation Enduring Freedom: The United States in Afghanistan

Phase Dynamics at Microtubule Ends: The Coexistence of Microtubule Length Changes and Treadmilling

Kinetics and Steady State Dynamics of Tubulin Addition and Loss at Opposite Microtubule Ends: The Mechanism of Action of Colchicine

Kinetics and Steady State Dynamics of Tubulin Addition and Loss at Opposite Microtubule Ends: The Mechanism of Action of Colchicinea

Commercial [ 3H]Glutamate Contains a Contaminant That Labels Tubulin Covalently

[37] Isolation of tubulin from nonneural sources

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