J. Collins

发表

Ca2+ stimulates the Mg2(+)-ATPase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound.

H. Swanljung-Collins, J. Collins, 1991, The Journal of biological chemistry.

Rapid, high-yield purification of intestinal brush border myosin I.

J. H. Collins, H. Swanljung-Collins, J. Collins, 1991, Methods in enzymology.

Actin activation of Ca2+-sensitive Mg2+-ATPase activity of Acanthamoeba myosin II is enhanced by dephosphorylation of its heavy chains.

E. Korn, J. Collins, 1980, The Journal of biological chemistry.

Peptide maps of the myosin isoenzymes of Acanthamoeba castellanii.

E. Korn, H. Gadasi, H. Maruta, 1979, The Journal of biological chemistry.

Multiple forms of Acanthamoeba myosin I.

E. Korn, H. Gadasi, H. Maruta, 1979, The Journal of biological chemistry.

The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity.

J. H. Collins, E. Korn, H. Gadasi, 1978, The Journal of biological chemistry.

Brush border myosin heavy chain phosphorylation is regulated by calcium and calmodulin

H. Swanljung-Collins, J. Montibeller, J. Rieker, 1987, FEBS letters.

Localization of the three phosphorylation sites on each heavy chain of Acanthamoeba myosin II to a segment at the end of the tail.

E. Korn, G. Côté, J. Collins, 1982, The Journal of biological chemistry.

Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.

E. Korn, G. Côté, J. Collins, 1981, The Journal of biological chemistry.

Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border.

H. Swanljung-Collins, J. Rieker, J. Collins, 1987, The Journal of biological chemistry.

Comparison of the actin binding and filament formation properties of phosphorylated and dephosphorylated Acanthamoeba myosin II.

J. Kuźnicki, B. Bowers, E. Korn, 1982, Biochemistry.

Phosphorylation of brush border myosin by brush border calmodulin‐dependent myosin heavy and light chain kinases

J. Rieker, J. Collins, 1987, FEBS letters.

Purification and characterization of actin-activatable, Ca2+-sensitive myosin II from Acanthamoeba.

E. Korn, J. Collins, 1981, The Journal of biological chemistry.

Type-1 transforming growth factor-beta differentially modulates tumoricidal activity of murine peritoneal macrophages against metastatic variants of the B16 murine melanoma.

J. H. Collins, I. Fidler, E. Kruzel, 2002, Journal of experimental therapeutics & oncology.

Phosphorylation of brush border myosin at threonine on its 20 kDa light chains by a calmodulin‐independent kinase activates its ATPase

H. Swanljung-Collins, J. Rieker, J. Collins, 1988, FEBS letters.

Calcium regulation of myosin I--a motor for membrane movement.

J. H. Collins, H. Swanljung-Collins, J. Collins, 1992, Advances in experimental medicine and biology.

Purification and characterization of the 110-kDa actin- and calmodulin-binding protein from intestinal brush border: a myosin-like ATPase.

H. Swanljung-Collins, J. Montibeller, J. Collins, 1987, Methods in Enzymology.

[32] Myosins from Acanthamoeba castellanii

J. H. Collins, E. Korn, H. Maruta, 1982 .

Brush border myosin I has a calmodulin/phosphatidylserine switch and tail actin-binding.

H. Swanljung-Collins, J. Collins, 1994, Advances in experimental medicine and biology.

Phosphorylation of brush border myosin I by protein kinase C is regulated by Ca(2+)-stimulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation.

H. Swanljung-Collins, J. Collins, 1992, The Journal of biological chemistry.

Sequence similarities between chicken intestinal 110-kDa ATPase and myosin I-like enzymes

M. Atkinson, J. Collins, 1989, Journal of protein chemistry.