D. Hackney

发表

GTP hydrolysis promotes disassembly of the atlastin crossover dimer during ER fusion

Tina H Lee, J. Winsor, Ursula Machi, 2018, The Journal of cell biology.

The crossover conformational shift of the GTPase atlastin provides the energy driving ER fusion

Tina H Lee, J. Winsor, D. Hackney, 2017, The Journal of cell biology.

The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP.

D. Hackney, David D Hackney, 2005, Proceedings of the National Academy of Sciences of the United States of America.

The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition

D. Hackney, F. Kozielski, H. Kaan, 2011, Science.

Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization.

Ting Huang, D. Hackney, T. Huang, 1994, The Journal of biological chemistry.

Nucleotide-free kinesin motor domains reversibly convert to an inactive conformation with characteristics of a molten globule.

D. Hackney, M. McGoff, 2016, Archives of biochemistry and biophysics.

Formation of the Compact Confomer of Kinesin Requires a COOH-terminal Heavy Chain Domain and Inhibits Microtubule-stimulated ATPase Activity*

Ting Huang, M. F. Stock, D. Hackney, 1999, The Journal of Biological Chemistry.

Characterization of α2β2 and α2 forms of kinesin

D. Hackney, J. D. Levitt, D. D. Wagner, 1991 .

Kinesin undergoes a 9 S to 6 S conformational transition.

D. Hackney, J. Suhan, J. D. Levitt, 1992, The Journal of biological chemistry.

Interaction of the mitotic inhibitor monastrol with human kinesin Eg5.

P. Gans, J. Simorre, R. Cross, 2003, Biochemistry.

Myosin and kinesin: mother and child reunited.

D. Hackney, 1996, Chemistry & biology.

Interaction of mant-adenosine nucleotides and magnesium with kinesin.

D. Hackney, J. Cheng, W. Jiang, 1998, Biochemistry.

Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli.

D. Hackney, J. Suhan, T. Huang, 1994, The Journal of biological chemistry.

Assays for kinesin microtubule-stimulated ATPase activity.

D. Hackney, W. Jiang, 2001, Methods in molecular biology.

Kinesin tail domains and Mg2+ directly inhibit release of ADP from head domains in the absence of microtubules.

M. F. Stock, D. Hackney, 2008, Biochemistry.

Jump-starting kinesin

D. Hackney, 2007, The Journal of cell biology.

P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of Protein 5 (Dbp5).

Y. Modis, W. Cao, D. Hackney, 2016 .

Anomalous oxygen-18 exchange during ATP synthesis in oxidative phosphorylation.

D. Hackney, J. Sines, 1986, Biochemistry.

Mechanistic implications of 18O exchange during ATP synthesis in oxidative phosphorylation.

D. Hackney, 1984, Current topics in cellular regulation.

Photodynamic action of bilirubin on the inner mitochondrial membrane. Implications for the organization of the mitochondrial ATPase.

D. Hackney, 1980, Biochemical and biophysical research communications.

Oxygen-18 probes of enzymic reactions of phosphate compounds.

P. Boyer, D. Hackney, K. Stempel, 1980, Methods in enzymology.

Characterization of phosphate oxygen exchange reactions catalyzed by myosin through measurement of the distribution of 18-O-labeled species.

P. Boyer, D. Hackney, J. Sleep, 1978, The Journal of biological chemistry.

Subunit interaction during catalysis. Implications of concentration dependency of oxygen exchanges accompanying oxidative phosphorylation for alternating site cooperativity.

P. Boyer, D. Hackney, 1978, The Journal of biological chemistry.

Dynamic reversal of enzyme carboxyl group phosphorylation as the basis of the oxygen exchange catalyzed by sarcoplasmic reticulum adenosine triphosphatase.

P. Boyer, D. Hackney, L. de Meis, 1977, Biochemistry.

Half-site inhibition of dimeric kinesin head domains by monomeric tail domains.

D. Hackney, Avin C. Snyder, Nahyeon Baek, 2009, Biochemistry.

Fluorometric methods for analysis of acid and alkaline phosphatase.

G. Guilbault, D. Hackney, A. Vaughan, 1971, Analytical chemistry.

Targeted movement of cell end factors in fission yeast

P. Nurse, D. Hackney, H. Browning, 2003, Nature Cell Biology.

Implications of diffusion-controlled limit for processivity of dimeric kinesin head domains.

D. Hackney, 1995, Biophysical journal.

When is weaker better? Design of an ADP sensor with weak ADP affinity, but still selective against ATP.

D. Hackney, 2010, ACS chemical biology.

Evaluation of the partitioning of bound inorganic phosphate during medium and intermediate phosphate in equilibrium water oxygen exchange reactions of yeast inorganic pyrophosphatase.

P. Boyer, D. Hackney, 1978, Proceedings of the National Academy of Sciences of the United States of America.

Analysis of positional isotope exchange in ATP by cleavage of the beta P-O gamma P bond. Demonstration of negligible positional isotope exchange by myosin.

D. Hackney, D D Hackney, M. P. Dale, 1987, Biochemistry.

The kinetic cycles of myosin, kinesin, and dynein.

D. Hackney, D D Hackney, 1996, Annual review of physiology.

Kinesin and myosin ATPases: variations on a theme.

D. Hackney, 1992, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

The EB1 Homolog Mal3 Stimulates the ATPase of the Kinesin Tea2 by Recruiting It to the Microtubule*

D. Hackney, H. Browning, 2005, Journal of Biological Chemistry.

The Kinesin Family Member BimC Contains a Second Microtubule Binding Region Attached to the N terminus of the Motor Domain*

M. F. Stock, D. Hackney, J. Chu, 2003, Journal of Biological Chemistry.

Expression of kinesin in Escherichia coli.

M. F. Stock, D. Hackney, 2001, Methods in molecular biology.

Influence of the Kinesin Neck Domain on Dimerization and ATPase Kinetics*

Wei Jiang, M. F. Stock, Wei Jiang, 1997, The Journal of Biological Chemistry.

S-Trityl-L-cysteine Is a Reversible, Tight Binding Inhibitor of the Human Kinesin Eg5 That Specifically Blocks Mitotic Progression*

R. Cross, L. Lebeau, D. Hackney, 2006, Journal of Biological Chemistry.

Interaction of Mg+2 with beef heart mitochondrial ATPase (F1).

D. Hackney, 1979, Biochemical and biophysical research communications.

Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.

D. Hackney, D D Hackney, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Kinesin’s IAK tail domain inhibits initial microtubule-stimulated ADP release

M. F. Stock, D. Hackney, Maryanne F. Stock, 2000, Nature Cell Biology.

Biochemical characterization of Escherichia coli DNA helicase I

P. Dash, D. Hackney, E. Minkley, 1992, Molecular microbiology.

The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA.

W. Cao, E. M. De La Cruz, D. Hackney, 2008, Journal of molecular biology.

Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O]ATP species formation.

P. Boyer, D. Hackney, G. Rosen, 1979, Proceedings of the National Academy of Sciences of the United States of America.

Motor proteins of the kinesin superfamily

D. Hackney, 2003 .

Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains

D. Hackney, David D. Hackney, 1995, Nature.

Kinesin ATPase: rate-limiting ADP release.

D. Hackney, D D Hackney, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Steady state kinetics at high enzyme concentration. The myosin MgATPase.

D. Hackney, P. Clark, 1985, The Journal of biological chemistry.

Processive Motor Movement

D. Hackney, David D Hackney, 2007, Science.

Energy coupling and molecular motors

F. Tamanoi, D. Hackney, D. Sigman, 2004 .

Monomeric Kinesin Head Domains Hydrolyze Multiple ATP Molecules before Release from a Microtubule*

W. Jiang, D. Hackney, 1997, The Journal of Biological Chemistry.

Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)

Y. Modis, W. Cao, E. M. De La Cruz, 2016, Journal of molecular biology.

Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA

W. Cao, E. M. De La Cruz, D. Hackney, 2010, Proceedings of the National Academy of Sciences.

Catalytic consequences of oligomeric organization: kinetic evidence for "tethered" acto-heavy meromyosin at low ATP concentrations.

D. Hackney, P. Clark, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Theoretical analysis of distribution of [18O]Pi species during exchange with water. Application to exchanges catalyzed by yeast inorganic pyrophosphatase.

D. Hackney, 1980, The Journal of biological chemistry.

The Tail Domain of Myosin Va Modulates Actin Binding to One Head*

Adrian O. Olivares, E. M. De La Cruz, Wakam Chang, 2006, Journal of Biological Chemistry.

Oxygen isotopic exchange probes of ATP hydrolysis by RNA helicases.

D. Hackney, 2012, Methods in enzymology.

Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins.

A. Pyle, W. Cao, E. M. De La Cruz, 2011, Journal of molecular biology.

Structural insights into a unique inhibitor binding pocket in kinesin spindle protein.

O. Rath, A. Pannifer, D. Hackney, 2013, Journal of the American Chemical Society.

Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli.

D. Hackney, J. Suhan, T. Huang, 1994, The Journal of biological chemistry.

Modulation of kinesin half-site ADP release and kinetic processivity by a spacer between the head groups.

M. F. Stock, D. Hackney, David D Hackney, 2003, Biochemistry.

Characterization of alpha 2 beta 2 and alpha 2 forms of kinesin.

D. Hackney, J. D. Levitt, D. D. Wagner, 1991, Biochemical and biophysical research communications.

Nucleotide-free kinesin hydrolyzes ATP with burst kinetics.

D. Hackney, K. Wright, A. S. Malik, 1989, Journal of Biological Chemistry.

Isolation of kinesin using initial batch ion exchange.

D. Hackney, 1991, Methods in enzymology.

The equivalence of phosphate oxygens for exchange and the hydrolysis characteristics revealed by the distribution of [18O]Pi species formed by myosin and actomyosin ATPase.

P. Boyer, D. Hackney, J. Sleep, 1980, The Journal of biological chemistry.

The rate-limiting step in microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains occurs while bound to the microtubule.

D. Hackney, 1994, The Journal of biological chemistry.