Y. Milgrom

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The permeability transition in heart mitochondria is regulated synergistically by ADP and cyclosporin A.

S. Novgorodov, T. Gudz, Y. Milgrom, 1992, The Journal of biological chemistry.

Probes of inhibition of Escherichia coli F1-ATPase by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole in the presence of MgADP and MgATP support a bi-site mechanism of ATP hydrolysis by the enzyme

V. V. Bulygin, Y. Milgrom, 2010, Biochemistry (Moscow).

Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase.

P. Boyer, Y. Milgrom, M. Murataliev, 1998, The Biochemical journal.

F-ATPase of Escherichia coli membranes: The ubiquitous MgADP-inhibited state and the inhibited state induced by the ε-subunit's C-terminal domain are mutually exclusive.

T. M. Duncan, Y. Milgrom, T. Duncan, 2020, Biochimica et biophysica acta. Bioenergetics.

The interaction of mitochondrial ATPase with an alkylating ATP‐analog

V. A. Kurbatov, V. Budker, Y. Milgrom, 1977, FEBS letters.

MgATP-concentration dependence of protection of yeast vacuolar V-ATPase from inactivation by 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole supports a bi-site catalytic mechanism of ATP hydrolysis.

Y. Milgrom, E. Milgrom, 2012, Biochemical and biophysical research communications.

An ATP dependence of mitochondrial F1‐ATPase inactivation by the natural inhibitor protein agrees with the alternating‐site binding‐change mechanism

Y. Milgrom, 1989 .

The nucleotide binding site of F1‐ATPase which carries out uni‐site catalysis is one of the alternating active sites of the enzyme

Y. Milgrom, M. Murataliev, I. Kozlov, 1985, FEBS letters.

The membrane in submitochondrial particles protects F1‐ATPase from trinitrobenzolsulphonate and dinitrofluorobenzole

Y. Milgrom, I. Kozlov, N.R. Drozdovskaya, 1982, FEBS letters.

An active-site-directed adenosine triphosphate analogue binds to the beta-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety.

Y. Milgrom, V. Drutsa, Z. Shabarova, 1979, The Biochemical journal.

The non-catalytic nucleotide-binding site of mitochondrial ATPase is localised on the alpha-subunit(s) of factor F1.

Y. Milgrom, I. Kozlov, 1980, European journal of biochemistry.

The F1-type ATPase in anaerobic Lactobacillus casei.

V. Skulachev, Y. Milgrom, I. V. Mesyanzhinova, 1990, Biochimica et biophysica acta.

The interaction of mitochondrial transhydrogenase with derivatives of coenzyme A.

Y. Milgrom, I. Kozlov, L. Saburova, 1984, European journal of biochemistry.

The effect of inorganic pyrophosphate on the activity and Pi-binding properties of mitochondrial F1-ATPase.

Y. Milgrom, M. Murataliev, Kalashnikova TYw, 1988, European journal of biochemistry.

A bi-site mechanism for Escherichia coli F1-ATPase accounts for the observed positive catalytic cooperativity.

V. V. Bulygin, Y. Milgrom, Vladimir V Bulygin, 2009, Biochimica et biophysica acta.

Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites.

R. L. Cross, Y. Milgrom, Yakov M Milgrom, 2005, Proceedings of the National Academy of Sciences of the United States of America.

The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site.

P. Boyer, Y. Milgrom, 1990, Biochimica et biophysica acta.

Interaction of nucleotide-depleted F1-ATPase with ADP: Characterization of a high-affinity binding site responsible for ADP-induced inhibition

Y. Milgrom, M. Murataliev, 1989 .

Characterization of the nucleotide tight‐binding sites of the isolated mitochondrial F1‐ATPase

Y. Milgrom, M. Murataliev, 1987, FEBS letters.

Characteristics of the combination of inhibitory Mg2+ and azide with the F1 ATPase from chloroplasts.

P. Boyer, Y. Milgrom, M. Murataliev, 1991, Biochemistry.

When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites.

Y. Milgrom, 1991, European journal of biochemistry.

The complex of mitochondrial F1‐ATPase with the natural inhibitor protein is unable to catalyze single‐site ATP hydrolysis

Y. Milgrom, T. Kalashnikova, N. V. Postanogova, 1988, FEBS letters.

Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP.

R. L. Cross, Y. Milgrom, D. Hyndman, 1994, The Journal of biological chemistry.

Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.

R. L. Cross, Y. Milgrom, 1993, The Journal of biological chemistry.

Characteristics of protection by MgADP and MgATP of α3β3Γ subcomplex of thermophilic Bacillus PS3 βY341W-mutant F1-ATPase from inhibition by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole support a Bi-site mechanism of catalysis

Y. Milgrom, 2011, Biochemistry (Moscow).

ATP binding and hydrolysis steps of the uni-site catalysis by the mitochondrial F(1)-ATPase are affected by inorganic phosphate.

Y. Milgrom, 2010, Biochimica et biophysica acta.

Studies of nucleotide binding to the catalytic sites of Escherichia coli βY331W-F1-ATPase using fluorescence quenching

V. V. Bulygin, Y. Milgrom, 2007, Proceedings of the National Academy of Sciences.

Nucleotide-depleted Beef Heart F1-ATPase Exhibits Strong Positive Catalytic Cooperativity*

R. L. Cross, Y. Milgrom, 1997, The Journal of Biological Chemistry.

Steady‐state rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic site

Y. Milgrom, M. Murataliev, 1987, FEBS letters.

Complex effects of macrolide venturicidins on bacterial F-ATPases likely contribute to their action as antibiotic adjuvants

Y. Milgrom, Thomas M. Duncan, 2021, Scientific Reports.

Using 2'(3')-O-trinitrophenyl derivatives of adenine nucleotides to study the structure and mechanism of functioning of soluble mitochondrial ATPase.

Y. Milgrom, I. Kozlov, Novikova IYu, 1982, European journal of biochemistry.