E. Korn

发表

Inhibition of actin polymerization by latrunculin A

S. Brenner, I. Spector, M. Coué, 1987, FEBS letters.

Structure of Biological Membranes

E. Korn, 1966, Science.

On the mechanism of actin monomer-polymer subunit exchange at steady state.

S. Brenner, E. Korn, 1983, The Journal of biological chemistry.

FILAMENTS OF AMOEBA PROTEUS

T. Pollard, E. Korn, 1971, The Journal of cell biology.

Acanthamoeba profilin. A protein of low molecular weight from Acanpthamoeba castellanii that inhibits actin nucleation.

E. Korn, E. Reichstein, 1979, The Journal of biological chemistry.

Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins.

E. Korn, H. Maruta, 1981, The Journal of biological chemistry.

Effect of Acanthamoeba profilin on the pre-steady state kinetics of actin polymerization and on the concentration of F-actin at steady state.

S. Brenner, E. Korn, L. Tobacman, 1983, The Journal of biological chemistry.

Properties of clearing factor obtained from rat heart acetone powder.

E. Korn, 1954, Science.

Clearing factor, a heparin-activated lipoprotein lipase. I. Isolation and characterization of the enzyme from normal rat heart.

E. Korn, 1955, The Journal of biological chemistry.

Lipoprotein lipase of chicken adipose tissue.

E. Korn, T. Quigley, 1957, The Journal of biological chemistry.

CLEARING FACTOR, A HEPARIN-ACTIVATED LIPOPROTEIN LIPASE*

E. Korn, 2003 .

Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium.

E. Korn, S. Shu, Xiong Liu, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain

J. Ferretti, J. Gruschus, E. Korn, 2007, Proceedings of the National Academy of Sciences.

Myosin I heavy chain kinase: cloning of the full-length gene and acidic lipid-dependent activation by Rac and Cdc42.

U. Knaus, E. Korn, H. Brzeska, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Acanthamoeba actin. Isolation and properties.

E. Korn, R. Weihing, 1971, Biochemistry.

THE FINE STRUCTURE OF ACANTHAMOEBA CASTELLANII (NEFF STRAIN)

B. Bowers, E. Korn, 1969, The Journal of cell biology.

Phagocytosis of latex beads by Acanthamoeba. I. Biochemical properties.

E. Korn, R. Weisman, 1967, Biochemistry.

Phagocytosis of latex beads by Acanthameba

E. Korn, R. Weisman, Ed Korn, 1967 .

Phagocytosis of latex beads by Acahamoeba castellanii (Neff). 3. Isolation of the phagocytic vesicles and their membranes.

E. Korn, M. Wetzel, 1969, The Journal of cell biology.

Differential localization of Acanthamoeba myosin I isoforms

E. Korn, I. Baines, H. Brzeska, 1992, The Journal of cell biology.

Swinholide A Is a Microfilament Disrupting Marine Toxin That Stabilizes Actin Dimers and Severs Actin Filaments (*)

A. Bershadsky, I. Spector, M. Bubb, 1995, The Journal of Biological Chemistry.

Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase.

J. Qin, J. Gruschus, J. Szczepanowska, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The Catalytic Domain of Acanthamoeba Myosin I Heavy Chain Kinase

E. Korn, H. Brzeska, Brian M. Martin, 1996, The Journal of Biological Chemistry.

Myosins of nonmuscle cells.

J. Hammer, E. Korn, 1988, Annual review of biophysics and biophysical chemistry.

Interaction of phospholipid vesicles with cells. Endocytosis and fusion as alternate mechanisms for the uptake of lipid-soluble and water-soluble molecules

E. Korn, S. Batzri, 1975, The Journal of cell biology.

Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin.

S. Brenner, E. Korn, 1979, The Journal of biological chemistry.

Acanthamoeba actin. Composition of the peptide that contains 3-methylhistidine and a peptide that contains N e -methyllysine.

E. Korn, R. Weihing, 1972, Biochemistry.

Structure‐function studies on Acanthamoeba myosins IA, IB, and II

J. Hammer, E. Korn, M. Atkinson, 1988, Journal of cellular biochemistry.

Ultrastructural characterization of F-actin isolated from Acanthamoeba castellanii and identification of cytoplasmic filaments as F-actin by reaction with rabbit heavy meromyosin.

T. Pollard, E. Shelton, E. Korn, 1970, Journal of molecular biology.

[32] Myosins from Acanthamoeba castellanii

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

Myosins from Acanthamoeba castellanii.

J. H. Collins, E. Korn, H. Maruta, 1982, Methods in enzymology.

The heavy chain of Acanthamoeba myosin IB is a fusion of myosin-like and non-myosin-like sequences.

J. Hammer, E. Korn, G. Jung, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Purification from Dictyostelium discoideum of a low-molecular-weight myosin that resembles myosin I from Acanthamoeba castellanii.

J. Hammer, J. Albanesi, E. Korn, 1985, The Journal of biological chemistry.

Acanthamoeba Myosin IC Colocalizes with Phosphatidylinositol 4,5-Bisphosphate at the Plasma Membrane Due to the High Concentration of Negative Charge*

E. Korn, H. Brzeska, K. Hwang, 2008, Journal of Biological Chemistry.

Structural invariance of constitutively active and inactive mutants of acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states.

B. Carragher, N. Cheng, J. Hammer, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Dictyostelium myosin 1F and myosin 1E inhibit actin waves in a lipid‐binding‐dependent and motor‐independent manner

M. Titus, E. Korn, H. Brzeska, 2020, Cytoskeleton.

Basic-hydrophobic sites are localized in conserved positions inside and outside of PH domains and affect localization of Dictyostelium myosin 1s

M. Titus, E. Korn, H. Brzeska, 2019, Molecular biology of the cell.

Calmodulin-binding and Autoinhibitory Domains ofAcanthamoeba Myosin I Heavy Chain Kinase, a p21-activated Kinase (PAK)*

J. Szczepanowska, E. Korn, Cristina A Tan, 2001, The Journal of Biological Chemistry.

I. Loss of lipids during preparation of amoebae for electron microscopy.

E. Korn, R. Weisman, E. D. Korn, 1966, Biochimica et biophysica acta.

The covalent structure of Acanthamoeba actobindin.

J. Vandekerckhove, K. Vancompernolle, J. Van Damme, 1990, The Journal of biological chemistry.

ε-N-Dimethyllysine in Amoeba Actin

E. Korn, R. Weihing, 1970, Nature.

Clearing factor, a heparin-activated lipoprotein lipase. II. Substrate specificity and activation of coconut oil.

E. Korn, 1955, The Journal of biological chemistry.

Studies on lipoprotein lipase of rat heart and adipose tissue.

E. Korn, T. Quigley, 1955, Biochimica et biophysica acta.

The lipoprotein lipase of cow's milk

E. Korn, 1962 .

The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization.

S. Brenner, E. Korn, 1980, The Journal of biological chemistry.

Biological, Biochemical, and Kinetic Effects of Mutations of the Cardiomyopathy Loop of Dictyostelium Myosin II

M. Kovács, E. Korn, S. Shu, 2005, Journal of Biological Chemistry.

Interaction of plasma gelsolin with ADP-actin.

M. Coué, E. Korn, 1986, The Journal of biological chemistry.

The critical concentration of actin in the presence of ATP increases with the number concentration of filaments and approaches the critical concentration of actin.ADP.

S. Brenner, A. Lal, M. Coué, 1984, The Journal of biological chemistry.

Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill.

S. Brenner, E. Korn, 1979, The Journal of biological chemistry.

Immunolocalization of myosin I heavy chain kinase in Acanthamoeba castellanii and binding of purified kinase to isolated plasma membranes

E. Korn, I. Baines, H. Brzeska, 1991, The Journal of cell biology.

Purification of myosin I and myosin I heavy chain kinase from Acanthamoeba castellanii.

E. Korn, T. Lynch, I. Baines, 1991, Methods in enzymology.

Identification by mass spectrometry of the phosphorylated residue responsible for activation of the catalytic domain of myosin I heavy chain kinase, a member of the PAK/STE20 family.

J. Qin, X. Zhang, J. Szczepanowska, 1997, Proceedings of the National Academy of Sciences of the United States of America.

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.

Biochemistry of actomyosin-dependent cell motility (a review).

E. Korn, 1978, Proceedings of the National Academy of Sciences of the United States of America.

Functional consequences of the proteolytic removal of regulatory serines from the nonhelical tailpiece of Acanthamoeba myosin II.

V. Sathyamoorthy, B. Bowers, E. Korn, 1990, Biochemistry.

Characterization of cytoplasmic actin isolated from Acanthamoeba castellanii by a new method.

E. Eisenberg, E. Korn, D. J. Gordon, 1976, The Journal of biological chemistry.

Endocytosis and exocytosis: Role of microfilaments and involvement of phospholipids in membrane fusion

S. R. Simmons, B. Bowers, E. Korn, 1974 .

LOCALIZATION OF LIPOPHOSPHONOGLYCAN ON BOTH SIDES OF ACANTHAMOEBA PLASMA MEMBRANE

B. Bowers, E. Korn, 1974, The Journal of cell biology.

The Discovery of Unconventional Myosins: Serendipity or Luck?

E. Korn, 2004, Journal of Biological Chemistry.

Reinvestigation of the inhibition of actin polymerization by profilin.

A. Lal, E. Korn, 1985, The Journal of biological chemistry.

Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate.

E. Korn, S. Mockrin, 1980, Biochemistry.

Autophosphorylation-independent activation of Acanthamoeba myosin I heavy chain kinase by plasma membranes.

E. Korn, I. Baines, H. Brzeska, 1993, The Journal of biological chemistry.

Acanthamoeba myosin I heavy chain kinase is activated by phosphatidylserine-enhanced phosphorylation.

E. Korn, T. Lynch, H. Brzeska, 1990, The Journal of biological chemistry.

Effect of actin filament length and filament number concentration on the actin-activated ATPase activity of Acanthamoeba myosin I.

J. Albanesi, M. Coué, E. Korn, 1985, The Journal of biological chemistry.

Comparative biochemistry of non-muscle actins.

J. Boyer, E. Korn, J. Boyer, 1977, The Journal of biological chemistry.

ATP hydrolysis by the gelsolin-actin complex and at the pointed ends of gelsolin-capped filaments.

M. Coué, E. Korn, 1986, The Journal of biological chemistry.

Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin.

E. Korn, D. J. Gordon, Y. Yang, 1976, The Journal of biological chemistry.

Kinetic Characterization of the ATPase and Actin-activated ATPase Activities of Acanthamoeba castellanii Myosin-2

J. Sellers, Sarah M. Heissler, E. Korn, 2013, The Journal of Biological Chemistry.

The amino acid sequence of Acanthamoeba profilin.

J. Vandekerckhove, C. Ampe, S. Brenner, 1985, The Journal of biological chemistry.

The regulation of actin polymerization and the inhibition of monomeric actin ATPase activity by Acanthamoeba profilin.

E. Korn, L. Tobacman, E. Korn, 1982, The Journal of biological chemistry.

The amino acid sequence of the light chain of Acanthamoeba myosin IC

J. Sellers, P. Matsudaira, Zhen-Yuan Wang, 1997, Journal of Muscle Research & Cell Motility.

Structure and function of the plasma membrane. A biochemical perspective.

E. Korn, E. D. Korn, 1968, The Journal of general physiology.

A CHROMATOGRAPHIC AND SPECTROPHOTOMETRIC STUDY OF THE PRODUCTS OF THE REACTION OF OSMIUM TETROXIDE WITH UNSATURATED LIPIDS

E. Korn, 1967, The Journal of cell biology.

Interaction of plasma gelsolin with G-actin and F-actin in the presence and absence of calcium ions.

M. Coué, E. Korn, 1985, The Journal of biological chemistry.

The localization and sequence of the phosphorylation sites of Acanthamoeba myosins I. An improved method for locating the phosphorylated amino acid.

B. Martin, E. Korn, T. Lynch, 1989, The Journal of biological chemistry.

PHAGOCYTOSIS OF LATEX BEADS BY ACANTHAMOEBA CASTELLANII (NEFF)

E. Korn, M. Wetzel, 1969, The Journal of cell biology.

Single bilayer liposomes.

A. Bangham, E. Korn, S. M. Johnson, 1971, Biochimica et biophysica acta.

THE LIPOPROTEIN LIPASE OF MAMMARY GLAND AND THE CORRELATION OF ITS ACTIVITY TO LACTATION.

O. Mcbride, E. Korn, O. McBride, 1963, Journal of lipid research.

Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro

E. Korn, S. Shu, Xiong Liu, 2020, Proceedings of the National Academy of Sciences.

Polymerization pathway of mammalian nonmuscle myosin 2s

E. Korn, S. Shu, Xiong Liu, 2018, Proceedings of the National Academy of Sciences.

Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II

J. Sellers, G. Piszczek, N. Billington, 2017, Proceedings of the National Academy of Sciences.

Mammalian Nonmuscle Myosin II Binds to Anionic Phospholipids with Concomitant Dissociation of the Regulatory Light Chain*

J. Sellers, J. Donaldson, N. Billington, 2016, The Journal of Biological Chemistry.

Myosin-I nomenclature

J. R. Holt, A. Hudspeth, T. Pollard, 2001, The Journal of cell biology.

The fatty acids of Euglena gracilis.

E. Korn, 1964, Journal of lipid research.

Electron microscopic identification of actin associated with isolated amoeba plasma membranes.

T. Pollard, E. Korn, 1973, The Journal of biological chemistry.

Choline esterase activity in the tissues of the snail Helix Aspersa

E. Korn, 1969 .

The fatty acid and positional specificities of lipoprotein lipase.

E. Korn, 1961, The Journal of biological chemistry.

Inactivation of lipoprotein lipase by heparinase.

E. Korn, 1957, The Journal of biological chemistry.

The “Contractile” Proteins of Acanthamoeba castellanii

T. Pollard, E. Korn, 1973 .

II. Synthesis of bis(methyl 9,10-dihydroxystearate)osmate from methyl oleate and osmium tetroxide under conditions used for fixation of biological material.

E. Korn, E. D. Korn, 1966, Biochimica et biophysica acta.

3. Modification of oleic acid during fixation of Amoebae by osmium tetroxide.

E. Korn, E. D. Korn, 1966, Biochimica et biophysica acta.

Bacterial Degradation of Heparin

E. Korn, A. N. Payza, A. NAIL PAYZA, 1956, Nature.

7-Dehydrostigmasterol and ergosterol: the major sterols of an amoeba.

E. Korn, F. Smith, E. D. Korn, 1968, Journal of lipid research.

Enzymic degradation of heparin.

E. Korn, A. N. Payza, 1956, Biochimica et biophysica acta.

Ca2+ bound to the high affinity divalent cation-binding site of actin enhances actophorin-induced depolymerization of muscle F-actin but inhibits actophorin-induced depolymerization of Acanthamoeba F-actin

M. Mossakowska, E. Korn, 1996, Journal of Muscle Research & Cell Motility.

Single bilayer liposomes prepared without sonication.

E. Korn, E D Korn, S Batzri, 1973, Biochimica et biophysica acta.

Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin.

E. Sausville, A. Senderowicz, M. Bubb, 1994, The Journal of biological chemistry.

Phosphonoglycan. A major polysaccharide constituent of the amoeba plasma membrane contains 2-aminoethylphosphonic acid and 1-hydroxy-2-aminoethylphosphonic acid.

D. Dearborn, H. Fales, E. Korn, 1973, The Journal of biological chemistry.

Cell membranes: structure and synthesis.

E. Korn, 1969, Annual Review of Biochemistry.

BIOCHEMISTRY OF THE MAMMALIAN PLASMA MEMBRANE

E. Korn, 1974 .

[26] Purines and pyrimidines

E. Korn, 1957 .

FATTY ACID AND PHOSPHOLIPID COMPOSITION OF THE CELLULAR SLIME MOLD, DICTYOSTELIUM DISCOIDEUM. THE OCCURRENCE OF PREVIOUSLY UNDESCRIBED FATTY ACIDS.

F. Davidoff, E. Korn, 1963, The Journal of biological chemistry.

Lipids of dictyostelium discoideum: Phospholipid composition and the presence of two new fatty acids: cis,cis-5,11-octadecadienoic and cis,cis-5,9-hexadecadienoic acids

F. Davidoff, E. Korn, 1962 .

Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin.

T. Pollard, E. Korn, 1973, The Journal of biological chemistry.

Methods in membrane biology

E. Korn, 2013, Springer US.

THE REACTIONS OF TRANS-ALPHA, BETA-HEXADECENOYL COENZYME A AND CIS- AND TRANS-BETA, GAMMA-HEXADECENOYL COENZYME A CATALYZED BY ENZYMES FROM GUINEA PIGS LIVER MITOCHONDRIA.

F. Davidoff, E. Korn, 1965, The Journal of biological chemistry.

Ameba actin: the presence of 3-methylhistidine.

E. Korn, R. Weihing, 1969, Biochemical and biophysical research communications.

Uptake of fatty acids by Acanthamoeba.

E. Korn, R. Weisman, E. D. Korn, 1966, Biochimica et biophysica acta.

Further studies on the biosynthesis of fatty acids in the cellular slime mold.

F. Davidoff, E. Korn, 1962, Biochemical and biophysical research communications.

Separation of positional isomers of long-chain unsaturated fatty acid methyl esters by thin-layer chromatography and presence of mono-trans, di-cis isomers in commerical linolenic acid.

E. Korn, A. M. Lees, 1966, Biochimica et biophysica acta.

The sterols of Trypanosoma cruzi and Crithidia fasciculata.

E. Korn, T. von Brand, E. J. Tobie, 1969, Comparative biochemistry and physiology.

Physical and chemical properties of polysaccharides and glycoproteins of the yeast-cell wall.

D. Northcote, E. Korn, BY E. D. Korn, 1960, The Biochemical journal.

Composition of an amoeba plasma membrane.

T. Olivecrona, E. Korn, 1971, Biochemical and biophysical research communications.

The enzymatic aromatization of the b ring of Δ5,7-sterols

E. Korn, R. Weihing, M. Wetzel, 1969 .

The degradation of heparin by bacterial enzymes. III. A comparison of the degradation of heparin, hyaluronic acid, and chondroitin sulfate.

E. Korn, 1957, The Journal of biological chemistry.

The degradation of hyaluronate, the chondroitin sulfates and heparin by bacterial enzymes (flavobacterium).

E. Korn, A. Linker, K. Meyer, 1957, Biochimica et biophysica acta.

The degradation of heparin by bacterial enzymes. I. Adaptation and lyophilized cells.

E. Korn, A. N. Payza, 1956, The Journal of biological chemistry.

PLASMA AND PHAGOSOME MEMBRANES OF ACANTHAMOEBA CASTELLANII

E. Korn, M. Wetzel, A. Ulsamer, 1971, The Journal of cell biology.

CYTOCHEMICAL IDENTIFICATION OF PHOSPHATASE ACTIVITY IN THE CONTRACTILE VACUOLE OF ACANTHAMOEBA CASTELLANII

B. Bowers, E. Korn, Edward D. Korn, 1973, The Journal of cell biology.

Presence of glycerokinase in guinea pig mammary gland and the incorporation of glycerol into glycerides.

O. Mcbride, E. Korn, 1964, Journal of lipid research.

THE CONVERSION OF LONG CHAIN SATURATED FATTY ACIDS TO THEIR ALPHA, BETA-UNSATURATED, BETA, GAMMA-UNSATURATED, AND BETA-HYDROXY DERIVATIVES BY ENZYMES FROM THE CELLULAR SLIME MOLD, DICTYOSTELIUM DISCOIDEUM.

F. Davidoff, E. Korn, 1964, The Journal of biological chemistry.

Methods in Membrane Biology

N. Gershfeld, E. Korn, L. Bergelson, 1978, Springer US.

The Assay of Lipoprotein Lipase in Vivo and in Vitro

E. Korn, 2006 .

Acanthamoeba castellanii: methods and perspectives for study of cytoskeleton proteins.

E. Korn, 1982, Methods in cell biology.

Lipophosphonoglycan of the plasma membrane of A canthamoeba castellanii. Inositol and phytosphingosine content and general structural features.

D. Dearborn, E. Korn, S. Smith, 1976, The Journal of biological chemistry.

Plasma membrane and soluble lysophospholipases of Acanthamoeba castellanii.

E. Korn, E. J. Victoria, 1975, Archives of biochemistry and biophysics.

Enzymes of phospholipid metabolism in the plasma membrane of Acanthamoeba castellanii.

E. Korn, E. J. Victoria, 1975, Journal of lipid research.

Lipophosphonoglycan of the plasma membrance of Acanthamoeba castellanii. Isolation from whole amoebae and identification of the water-soluble products of acid hydrolysis.

D. Dearborn, E. Korn, P. L. Wright, 1974, Journal of Biological Chemistry.

Lipophosphonoglycan of the plasma membrane of Acanthamoeba castellanii. Fatty acid composition.

D. Dearborn, E. Korn, 1974, The Journal of biological chemistry.

Macromolecular composition of an amoeba plasma membrane.

E. Korn, P. L. Wright, 1973, Journal of Biological Chemistry.

PHAGOCYTOSIS OF LATEX BEADS BY ACANTHAMOEBA

E. Korn, R. Weisman, 1967, The Journal of cell biology.

Immunological characterization of phosphoprotein phosphatases.

E. Shacter, J. McClure, E. Korn, 1985, Archives of biochemistry and biophysics.

The isolation of the amoeba plasma membrane and the use of latex beads for the isolation of phagocytic vacuole (phagosome) membranes from amoebae including the culture techniques for amoebae.

E. Korn, 1974, Methods in enzymology.

Dictyostelium and Acanthamoeba myosin II assembly domains go to the cleavage furrow of Dictyostelium myosin II-null cells

E. Korn, S. Shu, Xiong Liu, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Dynamic localization of myosin-I to endocytic structures in Acanthamoeba.

Thomas D Pollard, E Michael Ostap, T. Pollard, 2003, Cell motility and the cytoskeleton.

Flexibility of Acanthamoeba myosin rod minifilaments.

M. Zółkiewski, A. Ginsburg, J. Hammer, 1999, Biochemistry.

Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis.

J. Sellers, J. Hammer, E. Korn, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Isolation of a non-muscle myosin heavy chain gene from Acanthamoeba.

B. Paterson, J. Hammer, E. Korn, 1986, The Journal of biological chemistry.

Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in the rodlike tail

B. Paterson, J. Hammer, B. Bowers, 1987, The Journal of cell biology.

Proteolytic separation of the actin-activatable ATPase site from the phosphorylation site on the heavy chain of Acanthamoeba myosin IA.

E. Korn, H. Maruta, 1981, The Journal of biological chemistry.

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.

Evidence for differential intracellular localization of the Acanthamoeba myosin isoenzymes

E. Korn, H. Gadasi, 1980, Nature.

Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. Evidence for oligomeric actin in the erythrocyte cytoskeleton.

S. Brenner, E. Korn, 1980, The Journal of biological chemistry.

Immunochemical analysis of Acanthamoeba myosins IA, IB, and II.

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

Cooperative binding of tropomyosin to muscle and Acanthamoeba actin.

E. Eisenberg, E. Korn, Y. Yang, 1979, 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.

Binding of tropomyosin to copolymers of Acanthamoeba actin and muscle actin.

E. Eisenberg, E. Korn, Y. Yang, 1979, The Journal of biological chemistry.

Acanthamoeba cofactor protein is a heavy chain kinase required for actin activation of the Mg2+-ATPase activity of Acanthamoeba myosin I.

E. Korn, H. Maruta, 1977, The Journal of biological chemistry.

Acanthamoeba myosin II.

E. Korn, H. Maruta, 1977, The Journal of biological chemistry.

Interaction between Acanthamoeba actin and rabbit skeletal muscle tropomyosin.

E. Eisenberg, E. Korn, D. J. Gordon, 1977, The Journal of biological chemistry.

Purification from Acanthamoeba castellanii of proteins that induce gelation and syneresis of F-actin.

E. Korn, H. Maruta, 1977, The Journal of biological chemistry.

Acanthamoeba myosin. II. Interaction with actin and with a new cofactor protein required for actin activation of Mg 2+ adenosine triphosphatase activity.

T. Pollard, E. Korn, 1973, The Journal of biological chemistry.

LIPIDS OF ACANTHAMOEBA CASTELLANII

E. Korn, A. Ulsamer, F. Smith, 1969, The Journal of cell biology.

Plasma membrane association of Acanthamoeba myosin I

B. Bowers, E. Korn, H. Miyata, 1989, The Journal of cell biology.

Isolation and partial characterization of a 110-kD dimer actin-binding protein

E. Korn, T. Ueno, 1986, The Journal of cell biology.

Cytoplasmic actin and myosin

E. Korn, 1976 .

The enzymatic sulfation of heparin.

E. Korn, 1959, The Journal of biological chemistry.

Biosynthesis of the purines. VII. Synthesis of nucleotides from bases by partially purified enzymes.

E. Korn, J. M. Buchanan, C. Remy, 1955, The Journal of biological chemistry.

The formation of unsaturated disacharides from mucopoly-saccharides and their cleavage to alpha-keto acid by bacterial enzymes.

E. Korn, A. Linker, K. Meyer, 1960, The Journal of biological chemistry.

S-adenosylhomocysteine hydrolase is localized at the front of chemotaxing cells, suggesting a role for transmethylation during migration

C. Parent, Wenli Liu, E. Korn, 2006, Proceedings of the National Academy of Sciences.

SYNTHESIS OF UNSATURATED FATTY ACIDS IN THE SLIME MOLD PHYSARUM POLYCEPHALUM AND THE ZOOFLAGELLATES LEISHMANIA TARENTOLAE, TRYPANOSOMA LEWISI, AND CRITHIDIA SP.: A COMPARATIVE STUDY.

C. Greenblatt, E. Korn, A. M. Lees, 1965, Journal of lipid research.

Biosynthesis of the purines. VI. Purification of liver nucleoside phosphorylase and demonstration of nucleoside synthesis from 4-amino-5-imidazolecarboxamide, adenine, and 2, 6-diaminopurine.

E. Korn, J. M. Buchanan, 1955, The Journal of biological chemistry.

Properties of Acanthamoeba Myosin I Heavy Chain Kinase Bound to Phospholipid Vesicles (*)

E. Korn, I. Baines, H. Brzeska, 1995, The Journal of Biological Chemistry.

The Polymerization of Actin

E. Korn, 1981 .

FILAMENTS OF AMOEBA PROTEUS II. Binding of Heavy Meromyosin by Thin Filaments in Motile Cytoplasmic Extracts

T. Pollard, E. Korn, 2003 .

Actin polymerization and its regulation by proteins from nonmuscle cells.

E. Korn, E D Korn, 1982, Physiological reviews.

Expression of Y53A-Actin in Dictyostelium Disrupts the Cytoskeleton and Inhibits Intracellular and Intercellular Chemotactic Signaling*

C. Parent, P. Kriebel, E. Korn, 2010, The Journal of Biological Chemistry.

Monomeric Acanthamoeba myosins I support movement in vitro.

J A Hammer, M. Sheetz, J. Hammer, 1985, The Journal of biological chemistry.

Myosin I is located at the leading edges of locomoting Dictyostelium amoebae

Y. Fukui, E. Korn, T. Lynch, 1989, Nature.

ATPase activities and actin-binding properties of subfragments of Acanthamoeba myosin IA.

J. Albanesi, B. Bowers, E. Robinson, 1986, The Journal of biological chemistry.

Kinetic model for the inhibition of actin polymerization by actobindin.

M. Bubb, E. Korn, 1995, Biochemistry.

Amino acid sequence of a segment of the Acanthamoeba myosin II heavy chain containing all three regulatory phosphorylation sites.

E. Appella, E. Robinson, E. Korn, 1984, The Journal of biological chemistry.

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.

Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essential in vivo function(s)

N. Osherov, G. May, E. Korn, 2001, Proceedings of the National Academy of Sciences of the United States of America.

p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I.

G. Bokoch, U. Knaus, E. Korn, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The Catalytic Domain of Acanthamoeba Myosin I Heavy Chain Kinase

J. Szczepanowska, E. Korn, H. Brzeska, 1996, The Journal of Biological Chemistry.

Regulation of Class I and Class II Myosins by Heavy Chain Phosphorylation*

E. Korn, H. Brzeska, 1996, The Journal of Biological Chemistry.

Inhibition of contractile vacuole function in vivo by antibodies against myosin-I

T. Pollard, E. Korn, S. Doberstein, 1993, Nature.

Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides.

B. Martin, E. Korn, T. Lynch, 1990, The Journal of biological chemistry.

Purification and characterization of a third isoform of myosin I from Acanthamoeba castellanii.

E. Korn, T. Lynch, H. Miyata, 1989, The Journal of biological chemistry.

A kinetic model for the molecular basis of the contractile activity of Acanthamoeba myosins IA and IB.

J. Albanesi, E. Korn, H. Fujisaki, 1985, The Journal of biological chemistry.

Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii.

J. Hammer, J. Albanesi, E. Korn, 1983, The Journal of biological chemistry.

The isolation of heparin from mouse mast cell tumor.

E. Korn, 1959, The Journal of biological chemistry.

Interaction of cytochalasin D with actin filaments in the presence of ADP and ATP.

E. Korn, D. Pantaloni, M. Carlier, 1986, The Journal of biological chemistry.

The polyunsaturated 20-carbon and 22-carbon fatty acids of Euglena.

E. Korn, 1963, Biochemical and biophysical research communications.

The kinetics of the inhibition of lipoprotein lipase by polyanions and polycations.

E. Korn, 1962, 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.

Supramolecular regulation of the actin-activated ATPase activity of filaments of Acanthamoeba Myosin II.

J. Kuźnicki, J. Albanesi, E. Korn, 1983, Journal of Biological Chemistry.

Coevolution of head, neck, and tail domains of myosin heavy chains.

E. Korn, E. D. Korn, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Nucleotides Increase the Internal Flexibility of Filaments of Dephosphorylated Acanthamoeba Myosin II (*)

D. Rau, E. Korn, M. Rędowicz, 1996, The Journal of Biological Chemistry.

The regulation of actin and myosin by ATP.

E. Korn, 1985, Current topics in cellular regulation.

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

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

Regulation of the filament structure and assembly of Acanthamoeba myosin II by phosphorylation of serines in the heavy-chain nonhelical tailpiece

E. Korn, S. Shu, Xiong Liu, 2012, Proceedings of the National Academy of Sciences.

Regulation of the actin-activated MgATPase activity of Acanthamoeba myosin II by phosphorylation of serine 639 in motor domain loop 2

R. Levine, S. Cai, E. Korn, 2012, Proceedings of the National Academy of Sciences.

Localization of myosin IC and myosin II in Acanthamoeba castellanii by indirect immunofluorescence and immunogold electron microscopy

E. Korn, I. Baines, 1990, The Journal of cell biology.

Electric birefringence study of the solution structure of chymotrypsin-cleaved Acanthamoeba myosin II.

S. Wijmenga, D. Rau, E. Korn, 1987, The Journal of biological chemistry.

Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II.

J. Kuźnicki, B. Bowers, E. Korn, 1985, The Journal of biological chemistry.

Chimeras of Dictyostelium myosin II head and neck domains with Acanthamoeba or chicken smooth muscle myosin II tail domain have greatly increased and unregulated actin-dependent MgATPase activity.

E. Korn, Y. Xu, S. Shu, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Structure and Function of the Plasma Membrane

E. Korn, 1968, The Journal of general physiology.

BIOSYNTHESIS OF UNSATURATED FATTY ACIDS IN ACANTHAMOEBA SP.

E. Korn, 1964, The Journal of biological chemistry.

A model for actin polymerization and the kinetic effects of ATP hydrolysis.

T. L. Hill, E. Korn, D. Pantaloni, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Mutation of Actin Tyr-53 Alters the Conformations of the DNase I-binding Loop and the Nucleotide-binding Cleft*

Bin Yu, E. Korn, S. Shu, 2010, The Journal of Biological Chemistry.

Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding

R. Dominguez, E. Korn, F. Ferron, 2008, Proceedings of the National Academy of Sciences.

Detection of Rho-family proteins in Acanthamoeba castellanii.

E. Korn, M. Rędowicz, 2000 .

Two-state thermal unfolding of a long dimeric coiled-coil: the Acanthamoeba myosin II rod.

M. Zółkiewski, A. Ginsburg, J. Hammer, 1997, Biochemistry.

Amino acid sequence of Acanthamoeba actin.

J. Vandekerckhove, A. Lal, E. Korn, 1984, Journal of molecular biology.

Metabolism of unsaturated fatty acids in protozoa.

E. Korn, A. M. Lees, 1966, Biochemistry.

Synthesis of ca-Linolenic Acid by Leishmania enriettii

C. Greenblatt, E. Korn, 1963, Science.

THE BIOSYNTHESIS OF FATTY ACIDS IN THE CELLULAR SLIME MOLD, DICTYOSTELIUM DISCOIDEUM.

F. Davidoff, E. Korn, 1963, The Journal of biological chemistry.

Effect of muscle tropomyosin on the kinetics of polymerization of muscle actin.

A. Lal, E. Korn, 1986, Biochemistry.

Effects of phosphorylation and nucleotides on the conformation of myosin II from Acanthamoeba castellanii.

B. Martin, M. Zółkiewski, A. Ginsburg, 1994, The Journal of biological chemistry.

Complete nucleotide sequence of the lipase gene from Staphylococcus hyicus cloned in Staphylococcus carnosus.

K. Schleifer, F. Götz, E. Korn, 1985, Nucleic acids research.

Uptake of free fatty acids and chylomicron glycerides by guinea pig mammary gland in pregnancy and lactation.

O. Mcbride, E. Korn, O. McBride, 1964, Journal of lipid research.

Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin.

M. Zółkiewski, A. Ginsburg, E. Korn, 1996, Biophysical chemistry.

An Experimentally Based Computer Search Identifies Unstructured Membrane-binding Sites in Proteins

E. Korn, H. Brzeska, Jake Guag, 2009, The Journal of Biological Chemistry.

Molecular Basis of Dynamic Relocalization of Dictyostelium Myosin IB*

M. Titus, E. Korn, G. Preston, 2012, The Journal of Biological Chemistry.

Molecular Basis of Dynamic Relocalization of Dictyostelium

M. Titus, E. Korn, G. Preston, 2012 .

Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii

E. Korn, I. Baines, A. Corigliano-Murphy, 1995, The Journal of cell biology.

Localization of actobindin, profilin I, profilin II, and phosphatidylinositol-4,5-bisphosphate (PIP2) in Acanthamoeba castellanii.

M. Bubb, E. Korn, I. Baines, 1998, Cell motility and the cytoskeleton.

The interfaces of actin and Acanthamoeba actobindin. Identification of a new actin-binding motif.

J Vandekerckhove, J. Vandekerckhove, K. Vancompernolle, 1991, The Journal of biological chemistry.

Purification and characterization of actobindin, a new actin monomer-binding protein from Acanthamoeba castellanii.

E. Korn, P. Lambooy, 1986, The Journal of biological chemistry.

The kinetics of actin nucleation and polymerization.

E. Korn, L. Tobacman, L S Tobacman, 1983, The Journal of biological chemistry.

Purification of actobindin from Acanthamoeba castellanii.

M. Bubb, E. Korn, 1991, Methods in enzymology.

Actobindin binds with high affinity to a covalently cross-linked actin dimer.

M. Bubb, E. Korn, M. Lewis, 1994, The Journal of biological chemistry.

Actin polymerization and ATP hydrolysis.

E. Korn, D. Pantaloni, M. Carlier, 1987, Science.

Lack of NH2-terminal processing of actin from Acanthamoeba castellanii.

E. Korn, P. Rubenstein, K. Redman, 1985, The Journal of biological chemistry.

Chapter 2 Acanthamoeba Myosin I: Past, Present, and Future

E. Korn, 1991 .

The Catalytic Domain of Acanthamoeba Myosin I

J. Szczepanowska, E. Korn, H. Brzeska, 1996 .

Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments

R. Levine, E. Korn, S. Shu, 2006, Proceedings of the National Academy of Sciences.

Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals

Shixin Yang, S. Bernstein, M. Ikebe, 2018, Proceedings of the National Academy of Sciences.

The uptake of doubly labeled chylomicrons by guinea pig mammary gland and liver.

O. Mcbride, E. Korn, 1964, Journal of lipid research.

Activation of myosin in HeLa cells causes redistribution of focal adhesions and F-actin from cell center to cell periphery.

J. Szczepanowska, E. Korn, H. Brzeska, 2006, Cell motility and the cytoskeleton.

Selective localization of myosin‐I proteins in macropinosomes and actin waves

M. Titus, E. Korn, H. Brzeska, 2016, Cytoskeleton.

Phosphorylation and activation of smooth muscle myosin by Acanthamoeba myosin I heavy chain kinase.

J. Sellers, J. Hammer, E. Korn, 1984, The Journal of biological chemistry.

Polymerization of ADP-actin and ATP-actin under sonication and characteristics of the ATP-actin equilibrium polymer.

E. Korn, D. Pantaloni, M. Carlier, 1985, The Journal of biological chemistry.

The hydrolysis of ATP that accompanies actin polymerization is essentially irreversible

M. Webb, M. Carlier, E. Korn, 1988, FEBS letters.

[72] Lipoprotein lipase (clearing factor)

E. Korn, 1962 .

Biochemical and biological properties of cortexillin III, a component of Dictyostelium DGAP1–cortexillin complexes

M. Gucek, G. Piszczek, Guanghui Wang, 2014, Molecular biology of the cell.

Actin cross-linking proteins cortexillin I and II are required for cAMP signaling during Dictyostelium chemotaxis and development

P. Kriebel, E. Korn, M. Daniels, 2012, Molecular biology of the cell.

Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state.

E. Korn, D. Pantaloni, M. Carlier, 1984, The Journal of biological chemistry.

Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells.

F. Matsumura, J. Szczepanowska, E. Korn, 2004, Cell motility and the cytoskeleton.

The Association of Myosin IB with Actin Waves in Dictyostelium Requires Both the Plasma Membrane-Binding Site and Actin-Binding Region in the Myosin Tail

M. Titus, E. Korn, H. Brzeska, 2014, PloS one.

Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin.

E. Korn, D. Pantaloni, M. Carlier, 1986, The Journal of biological chemistry.

Stimulation of actin ATPase activity by cytochalasins provides evidence for a new species of monomeric actin.

S. Brenner, E. Korn, 1981, The Journal of biological chemistry.

LIPIDS OF ACANTHAMOEBA CASTELLANII Composition and Effects of Phagocytosis on Incorporation of Radioactive Precursors

F. R. Smith, E. Korn, A. Ulsamer, 2003 .

Current concepts of membrane structure and function.

E. Korn, 1969, Federation proceedings.

Kinetics of polymerization and ATP hydrolysis by covalently crosslinked actin dimer.

E. Korn, S. Mockrin, 1983, Journal of Biological Chemistry.

Interdependence of factors affecting the actin-activated ATPase activity of myosin II from Acanthamoeba castellanii.

J. Kuźnicki, E. Korn, 1984, The Journal of biological chemistry.

Rate constants for actin polymerization in ATP determined using cross-linked actin trimers as nuclei.

S. Brenner, A. Lal, E. Korn, 1984, The Journal of biological chemistry.

Regulation of the actin-activated ATPase activity of Acanthamoeba myosin II by copolymerization with phosphorylated and dephosphorylated peptides derived from the carboxyl-terminal end of the heavy chain.

V. Sathyamoorthy, B. Bowers, E. Korn, 1990, The Journal of biological chemistry.

Cooperative dependence of the actin-activated Mg2+-ATPase activity of Acanthamoeba myosin II on the extent of filament phosphorylation.

E. Korn, M. Atkinson, P. Lambooy, 1989, The Journal of biological chemistry.

Experimental evidence for the contractile activities of Acanthamoeba myosins IA and IB.

J. Albanesi, E. Korn, H. Fujisaki, 1985, The Journal of biological chemistry.

Rabbit skeletal muscle actin behaves differently than Acanthamoeba actin when added to soluble extracts of Acanthamoeba castellanii.

M. Bubb, E. Korn, L. Holliday, 1993, Biochemical and biophysical research communications.

The degradation of heparin by bacterial enzymes. II. Acetone powder extracts.

E. Korn, A. N. Payza, 1956, Journal of Biological Chemistry.

The interfaces of actin and Acanthamoeba actobindin

J. Vandekerckhove, K. Vancompernolle, M. Bubb, 1991 .

Thermally induced unfolding of Acanthamoeba myosin II and skeletal muscle myosin: nucleotide effects.

M. Zółkiewski, A. Ginsburg, E. Korn, 1995, Archives of biochemistry and biophysics.

Functional Analysis of Tail Domains of AcanthamoebaMyosin IC by Characterization of Truncation and Deletion Mutants*

E. Korn, H. Brzeska, Xiong Liu, 2000, The Journal of Biological Chemistry.

Extensive purification from Acanthamoeba castellanii of a microtubule-dependent translocator with microtubule-activated Mg2+-ATPase activity.

B. Kachar, J. Albanesi, E. Korn, 1987, The Journal of biological chemistry.

Acceptors of fatty acid for glyceride synthesis in guinea pig mammary gland.

O. Mcbride, E. Korn, 1964, Journal of Lipid Research.

Isolation and characterization of covalently cross-linked actin dimer.

E. Korn, S. Mockrin, 1981, Journal of Biological Chemistry.

The effects of Mg2+ at the high-affinity and low-affinity sites on the polymerization of actin and associated ATP hydrolysis.

E. Korn, D. Pantaloni, M. Carlier, 1986, The Journal of biological chemistry.

The mechanisms of ATP hydrolysis accompanying the polymerization of Mg-actin and Ca-actin.

E. Korn, D. Pantaloni, M. Carlier, 1987, The Journal of biological chemistry.

Genetic evidence that Acanthamoeba myosin I is a true myosin.

J. Hammer, E. Korn, G. Jung, 1986, Proceedings of the National Academy of Sciences of the United States of America.

ENZYMATIC SYNTHESIS OF 4-AMINO-5-IMIDAZ-OLECARBOXAMIDE RIBOSIDE FROM 4-AMINO-5-IMIDAZOLECARBOXAMIDE AND RIBOSIDE-1-PHOSPHATE1

E. Korn, J. M. Buchanan, F. Charalampous, 1953 .

THE FINE STRUCTURE OF ACANTHAMOEBA CASTELLANII

B. Bowers, E. Korn, Blair Bowers, 1968, The Journal of cell biology.

Steady state length distribution of F-actin under controlled fragmentation and mechanism of length redistribution following fragmentation.

E. Korn, D. Pantaloni, M. Carlier, 1984, The Journal of biological chemistry.

Preparation of a phospholipid-insensitive, autophosphorylation-activated catalytic fragment of Acanthamoeba myosin I heavy chain kinase.

B. Martin, E. Korn, I. Baines, 1992, The Journal of biological chemistry.

Localization of the actin-binding sites of Acanthamoeba myosin IB and effect of limited proteolysis on its actin-activated Mg2+-ATPase activity.

E. Korn, T. Lynch, H. Brzeska, 1988, The Journal of biological chemistry.

Interaction of cytochalasin D with actin filaments in the presence of ADP and ATP.

M. Carlier, E. Korn, D. Pantaloni, 1986, The Journal of biological chemistry.

An Experimentally Based Computer Search Identifies Unstructured Membrane-binding Sites in Proteins

E. Korn, H. Brzeska, Jake Guag, 2009, The Journal of Biological Chemistry.

Inhibition of Acanthamoeba myosin I heavy chain kinase by Ca(2+)-calmodulin.

E. Korn, H. Brzeska, D. Kulesza-Lipka, 1992, The Journal of biological chemistry.

Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail

E. Appella, E. Korn, M. Atkinson, 1988, FEBS letters.

Inhibition of Mg ++ ATPase activity of actin-activated Acanthamoeba myosin by muscle troponin-tropomyosin: implications for the mechanism of control of amoeba motility and muscle contraction.

T. Pollard, E. Eisenberg, E. Korn, 1973, Biochemical and biophysical research communications.

The interaction of F-actin with phosphorylated and unphosphorylated myosins IA and IB from Acanthamoeba castellanii.

J. Hammer, J. Albanesi, E. Korn, 1983, The Journal of biological chemistry.

Interaction of phospholipid vesicles with cells. Endocytosis and fusion as alternate mechanisms for the uptake of lipid-soluble and water-soluble molecules

E. Korn, S. Batzri, 1975, The Journal of cell biology.

The Inhibited, Interacting-Heads Motif Characterizes Myosin II from the Earliest Animals with Muscles

M. Ikebe, E. Korn, J. Mun, 2015 .

Myosins of nonmuscle cells.

J. Hammer, E. Korn, 1988, Annual review of biophysics and biophysical chemistry.

DISCUSSION PAPER: AMOEBA PLASMA MEMBRANE

T. Olivecrona, E. Korn, 1972, Annals of the New York Academy of Sciences.

FATTY ACIDS OF ACANTHAMOEBA SP.

E. Korn, 1963, The Journal of biological chemistry.

The syntbesis of heparin by slices of mouse mast cell tumor.

E. Korn, 1959, The Journal of biological chemistry.

The Polymerization of Actin

E. Korn, 1981 .

Tail chimeras of Dictyostelium myosin II support cytokinesis and other myosin II activities but not full development

C. Parent, T. Uyeda, E. Korn, 2002, Journal of Cell Science.