UB Paderborn / Katalog / Suche / in CDI

Sortiert nach

Einfacher Volltextzugriff von (fast) überall

Installieren Sie die LibKey Nomad-Browsererweiterung und erhalten Sie von vielen Webseiten einfachen Zugriff auf lizenzierte Volltexte oder Open Access Publikationen. Mehr erfahren...

The critical role of the aldehyde dehydrogenase PauC in spermine, spermidine, and diaminopropane toxicity in Pseudomonas aeruginosa: Its possible use as a drug target

The FEBS journal, 2022-05, Vol.289 (9), p.2685-2705

2022

Volltextzugriff (PDF)

Identification of the allosteric site for neutral amino acids in the maize C 4 isozyme of phosphoenolpyruvate carboxylase: The critical role of Ser-100

The Journal of biological chemistry, 2018-06, Vol.293 (26), p.9945

2018

Volltextzugriff (PDF)

Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant ALDH10 Isoenzyme Involved in the Synthesis of Glycine Betaine

Plant physiology (Bethesda), 2012-04, Vol.158 (4), p.1570-1582

2012

Volltextzugriff (PDF)

Reversible, partial inactivation of plant betaine aldehyde dehydrogenase by betaine aldehyde: mechanism and possible physiological implications

Biochemical journal, 2016-04, Vol.473 (7), p.873-885

2016

Volltextzugriff (PDF)

Exploring the evolutionary route of the acquisition of betaine aldehyde dehydrogenase activity by plant ALDH10 enzymes: implications for the synthesis of the osmoprotectant glycine betaine

BMC plant biology, 2014-05, Vol.14 (1), p.149-149

2014

Volltextzugriff (PDF)

Rapid Purification and Properties of Betaine Aldehyde Dehydrogenase from Pseudomonas aeruginosa

Journal of Bacteriology, 1999-02, Vol.181 (4), p.1292-1300

1999

Volltextzugriff (PDF)

Physiological Implications of the Kinetics of Maize Leaf Phosphoenolpyruvate Carboxylase

Plant physiology (Bethesda), 2000-05, Vol.123 (1), p.149-160

2000

Volltextzugriff (PDF)

Betaine aldehyde dehydrogenase from Pseudomonas aeruginosa: cloning, over-expression in Escherichia coli, and regulation by choline and salt

Archives of microbiology, 2006-03, Vol.185 (1), p.14-22

2006

Volltextzugriff (PDF)

Site-directed mutagenesis and homology modeling indicate an important role of cysteine 439 in the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa

Biochimie, 2005-12, Vol.87 (12), p.1056-1064

2005

Volltextzugriff (PDF)

Monovalent cations requirements for the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, porcine kidney and amaranth leaves

Chemico-biological interactions, 2003-02, Vol.143, p.139-148

2003

Volltextzugriff (PDF)

Structural and biochemical evidence of the glucose 6-phosphate-allosteric site of maize C4-phosphoenolpyruvate carboxylase: its importance in the overall enzyme kinetics

Biochemical journal, 2020-06, Vol.477 (11), p.2095-2114

2020

Volltextzugriff (PDF)

Identification of the allosteric site for neutral amino acids in the maize C4 isozyme of phosphoenolpyruvate carboxylase: The critical role of Ser-100

The Journal of biological chemistry, 2018-06, Vol.293 (26), p.9945-9957

2018

Volltextzugriff (PDF)

Multiple conformations in solution of the maize C4-phosphoenolpyruvate carboxylase isozyme

Heliyon, 2021-11, Vol.7 (11), p.e08464-e08464, Article e08464

2021

Volltextzugriff (PDF)

Potassium and ionic strength effects on the conformational and thermal stability of two aldehyde dehydrogenases reveal structural and functional roles of K⁺-binding sites

PloS one, 2013, Vol.8 (1), p.e54899-e54899

2013

Volltextzugriff (PDF)

Potassium and Ionic Strength Effects on the Conformational and Thermal Stability of Two Aldehyde Dehydrogenases Reveal Structural and Functional Roles of K.sup.+-Binding Sites

PloS one, 2013-01, Vol.8 (1), p.e54899

2013

Volltextzugriff (PDF)

Allosteric Regulation of the Photosynthetic C4 Isoenzyme of Phosphoenolpyruvate Carboxylase: A Comparative Study Between Enzymes from Monocot and Dicot Plants

Journal of the Mexican Chemical Society, 2017-10, Vol.56 (1)

2017

Volltextzugriff (PDF)

Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase—A potential target for antimicrobial agents against Pseudomonas aeruginosa

Biochemical and biophysical research communications, 2006-03, Vol.341 (2), p.408-415

2006

Volltextzugriff (PDF)

Structural and functional roles of potassium ions on aldehyde dehydrogenases

The FASEB journal, 2012-04, Vol.26 (S1)

2012

Volltextzugriff (PDF)

Substrate Specificity in Promiscuous Enzymes: The Case of the Aminoaldehyde Dehydrogenases from Pseudomonas aeruginosa

Journal of the Mexican Chemical Society, 2023-07, Vol.67 (3), p.240-250

2023

Volltextzugriff (PDF)

Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant ALDH10 Isoenzyme Involved in the Synthesis of Glycine Betaine1[W][OA]

Plant physiology (Bethesda), 2012-04, Vol.158 (4), p.1570-1582

2012

Volltextzugriff (PDF)

Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol

Chemico-biological interactions, 2003-02, Vol.143, p.129-137

2003

Volltextzugriff (PDF)

Complexes of NADH with betaine aldehyde dehydrogenase from leaves of the plant Amaranthus hypochondriacus L

Chemico-biological interactions, 2001-01, Vol.130 (1-3), p.71-80

2001

Volltextzugriff (PDF)

Reaction of the catalytic cysteine of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa with arsenite-BAL and phenylarsine oxide

Chemico-biological interactions, 2009-03, Vol.178 (1), p.64-69

2009

Volltextzugriff (PDF)

Physiological Implications of the Kinetics of Maize Leaf Phosphoenolpyruvate Carboxylase1

Plant physiology (Bethesda), 2000-05, Vol.123 (1), p.149-160

2000

Volltextzugriff (PDF)

Physiological Implications of the Kinetics of Maize Leaf Phospho enol pyruvate Carboxylase

Plant physiology (Bethesda), 2000-05, Vol.123 (1), p.149-160

2000

Volltextzugriff (PDF)

1 – 25 von 32

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(31)
Mit Volltextzugriff
(28)

Publikationsform

Artikel
(32)

Sprache

Erscheinungsjahr

n.n

Menü

Weitere Dienste

Einstellungen

The critical role of the aldehyde dehydrogenase PauC in spermine, spermidine, and diaminopropane toxicity in Pseudomonas aeruginosa: Its possible use as a drug target

Identification of the allosteric site for neutral amino acids in the maize C 4 isozyme of phosphoenolpyruvate carboxylase: The critical role of Ser-100

Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant ALDH10 Isoenzyme Involved in the Synthesis of Glycine Betaine

Reversible, partial inactivation of plant betaine aldehyde dehydrogenase by betaine aldehyde: mechanism and possible physiological implications

Exploring the evolutionary route of the acquisition of betaine aldehyde dehydrogenase activity by plant ALDH10 enzymes: implications for the synthesis of the osmoprotectant glycine betaine

Rapid Purification and Properties of Betaine Aldehyde Dehydrogenase from Pseudomonas aeruginosa

Physiological Implications of the Kinetics of Maize Leaf Phosphoenolpyruvate Carboxylase

Betaine aldehyde dehydrogenase from Pseudomonas aeruginosa: cloning, over-expression in Escherichia coli, and regulation by choline and salt

Site-directed mutagenesis and homology modeling indicate an important role of cysteine 439 in the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa

Monovalent cations requirements for the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, porcine kidney and amaranth leaves

Structural and biochemical evidence of the glucose 6-phosphate-allosteric site of maize C4-phosphoenolpyruvate carboxylase: its importance in the overall enzyme kinetics

Identification of the allosteric site for neutral amino acids in the maize C4 isozyme of phosphoenolpyruvate carboxylase: The critical role of Ser-100

Multiple conformations in solution of the maize C4-phosphoenolpyruvate carboxylase isozyme

Potassium and ionic strength effects on the conformational and thermal stability of two aldehyde dehydrogenases reveal structural and functional roles of K⁺-binding sites

Potassium and Ionic Strength Effects on the Conformational and Thermal Stability of Two Aldehyde Dehydrogenases Reveal Structural and Functional Roles of K.sup.+-Binding Sites

Allosteric Regulation of the Photosynthetic C4 Isoenzyme of Phosphoenolpyruvate Carboxylase: A Comparative Study Between Enzymes from Monocot and Dicot Plants

Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase—A potential target for antimicrobial agents against Pseudomonas aeruginosa

Structural and functional roles of potassium ions on aldehyde dehydrogenases

Substrate Specificity in Promiscuous Enzymes: The Case of the Aminoaldehyde Dehydrogenases from Pseudomonas aeruginosa

Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant ALDH10 Isoenzyme Involved in the Synthesis of Glycine Betaine1[W][OA]

Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol

Complexes of NADH with betaine aldehyde dehydrogenase from leaves of the plant Amaranthus hypochondriacus L

Reaction of the catalytic cysteine of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa with arsenite-BAL and phenylarsine oxide

Physiological Implications of the Kinetics of Maize Leaf Phosphoenolpyruvate Carboxylase1

Physiological Implications of the Kinetics of Maize Leaf Phospho enol pyruvate Carboxylase

Suchergebnisse filtern