Reijo Lahti

Pre-steady-state kinetics and solvent isotope effects support the "billiard-type" transport mechanism in Na+-translocating pyrophosphatase (2022)

Protein Science

Malinen Anssi M, Anashkin Viktor A, Orlov Victor N, Bogachev Alexander V, Lahti Reijo, Baykov Alexander A

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

The tetrameric structure of nucleotide-regulated pyrophosphatase and its modulation by deletion mutagenesis and ligand binding (2020)

Archives of Biochemistry and Biophysics

Anashkin VA, Salminen A, Orlov VN, Lahti R, Baykov AA

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

Cooperativity in catalysis by canonical family II pyrophosphatases (2019)

Biochemical and Biophysical Research Communications

Viktor A. Anashkin, Vera A. Aksenova, Anu Salminen, Reijo Lahti, Alexander A. Baykov

(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä )

An arginine residue involved in allosteric regulation of cystathionine beta-synthase (CBS) domain-containing pyrophosphatase (2019)

Archives of Biochemistry and Biophysics

Anashkin Viktor A., Orlov Victor N., Lahti Reijo, Baykov Alexander A.

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

Residue Network Involved in the Allosteric Regulation of Cystathionine β-Synthase Domain-Containing Pyrophosphatase by Adenine Nucleotides (2019)

ACS Omega

Viktor A. Anashkin, Anu Salminen, Ekaterina Osipova, Svetlana A. Kurilova, Ilia D. Deltsov, Reijo Lahti, Alexander A. Baykov

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

Role of the potassium/lysine cationic center in catalysis and functional asymmetry in membrane-bound pyrophosphatases (2018)

Biochemical Journal

Artukka E, Luoto HH, Baykov AA, Lahti R, Malinen AM

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

Inorganic pyrophosphatases of Family II—two decades after their discovery (2017)

FEBS Letters

Baykov A., Anashkin V., Salminen A., Lahti R.

(Vertaisarvioitu katsausartikkeli tieteellisessä aikakauslehdessä (A2))

Enzymes regulated via cystathionine beta-synthase domains (2017)

Биохимия / Biochemistry

Anashkin VA, Baykov AA, Lahti R

(Vertaisarvioitu katsausartikkeli tieteellisessä aikakauslehdessä (A2))

An asparagine residue mediates intramolecular communication in nucleotide-regulated pyrophosphatase. (2016)

Biochemical Journal

Anashkin VA, Salminen A, Vorobjeva NN, Lahti R, Baykov AA.

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

Two independent evolutionary routes to Na+/H+ cotransport function in membrane pyrophosphatases. (2016)

Biochemical Journal

Erika Nordbo, Heidi H. Luoto, Alexander A. Baykov, Reijo Lahti, Anssi M. Malinen

(Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1))

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Lahti

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Pre-steady-state kinetics and solvent isotope effects support the "billiard-type" transport mechanism in Na+-translocating pyrophosphatase (2022)

The tetrameric structure of nucleotide-regulated pyrophosphatase and its modulation by deletion mutagenesis and ligand binding (2020)

Cooperativity in catalysis by canonical family II pyrophosphatases (2019)

An arginine residue involved in allosteric regulation of cystathionine beta-synthase (CBS) domain-containing pyrophosphatase (2019)

Residue Network Involved in the Allosteric Regulation of Cystathionine β-Synthase Domain-Containing Pyrophosphatase by Adenine Nucleotides (2019)

Role of the potassium/lysine cationic center in catalysis and functional asymmetry in membrane-bound pyrophosphatases (2018)

Inorganic pyrophosphatases of Family II—two decades after their discovery (2017)

Enzymes regulated via cystathionine beta-synthase domains (2017)

An asparagine residue mediates intramolecular communication in nucleotide-regulated pyrophosphatase. (2016)

Two independent evolutionary routes to Na+/H+ cotransport function in membrane pyrophosphatases. (2016)