Results 51 to 60 of about 2,040,864 (360)

Allosteric enzymes as biosensors for molecular diagnosis [PDF]

open access: yesFEBS Letters, 2003
Biosensors are hybrid analytical devices that amplify signals generated from the specific interaction between a receptor and the analyte, through a biochemical mechanism. Biosensors use tissues, whole cells, artificial membranes or cell components like proteins or nucleic acids as receptors, coupled to a physicochemical signal transducer.
openaire   +3 more sources

Investigation of Structural Dynamics of Enzymes and Protonation States of Substrates Using Computational Tools. [PDF]

open access: yes, 2016
This review discusses the use of molecular modeling tools, together with existing experimental findings, to provide a complete atomic-level description of enzyme dynamics and function.
Chang, Chia-En A   +3 more
core   +2 more sources

Organism-adapted specificity of the allosteric regulation of pyruvate kinase in lactic acid bacteria. [PDF]

open access: yesPLoS Computational Biology, 2013
Pyruvate kinase (PYK) is a critical allosterically regulated enzyme that links glycolysis, the primary energy metabolism, to cellular metabolism. Lactic acid bacteria rely almost exclusively on glycolysis for their energy production under anaerobic ...
Nadine Veith   +5 more
doaj   +1 more source

Mapping of the Allosteric Site in Cholesterol Hydroxylase CYP46A1 for Efavirenz, a Drug That Stimulates Enzyme Activity*

open access: yesJournal of Biological Chemistry, 2016
Cytochrome P450 46A1 (CYP46A1) is a microsomal enzyme and cholesterol 24-hydroxylase that controls cholesterol elimination from the brain. This P450 is also a potential target for Alzheimer disease because it can be activated pharmacologically by some ...
Kyle W. Anderson   +5 more
semanticscholar   +1 more source

Understanding allosteric and cooperative interactions in enzymes [PDF]

open access: yesThe FEBS Journal, 2013
The paper that introduced biochemists to the idea of allosteric feedback inhibition [Monod J, Changeux J‐P & Jacob F (1963) J Mol Biol 6, 306–329] is now 50 years old, and the two papers on models for enzyme cooperativity that followed it [Monod J, Wyman J & Changeux J‐P (1965) J Mol Biol 12, 88–118; Koshland DE, Némethy G & Filmer D (1966)
openaire   +4 more sources

Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 Å resolution [PDF]

open access: yes, 1999
The three-dimensional structure of the R form of rabbit liver fructose 1,6-bisphosphatase (Fru-1,6-Pase; E.C. 3.1.3.11) has been determined by a combination of heavy-atom and molecular-replacement methods.
Erman, M.   +5 more
core   +2 more sources

Structure and allosteric regulation of human NAD-dependent isocitrate dehydrogenase

open access: yesCell Discovery, 2020
Human NAD-dependent isocitrate dehydrogenase or HsIDH3 catalyzes the decarboxylation of isocitrate into α-ketoglutarate in the TCA cycle. HsIDH3 exists and functions as a heterooctamer composed of the αβ and αγ heterodimers, and is regulated ...
Pengkai Sun   +3 more
doaj   +1 more source

Probing the enzyme kinetics, allosteric modulation and activation of α1- and α2-subunit-containing AMP-activated protein kinase (AMPK) heterotrimeric complexes by pharmacological and physiological activators

open access: yesBiochemical Journal, 2015
We have studied enzyme kinetics, nucleotide binding and allosteric modulation of six recombinant AMP-activated protein kinase (AMPK) isoforms by known allosteric activators.
F. Rajamohan   +11 more
semanticscholar   +1 more source

Virtual screening for NS5B inhibitors of Hepatitis C virus [PDF]

open access: yes, 2012
Hepatitis C Virus (HCV) infection is a serious cause of chronic liver disease worldwide with more than 170 million infected individuals at a risk of developing significant morbidity and mortality.
Achuthsankar S. Nair   +2 more
core   +2 more sources

An Extended C-Terminus, the Possible Culprit for Differential Regulation of 5-Aminolevulinate Synthase Isoforms

open access: yesFrontiers in Molecular Biosciences, 2022
5-Aminolevulinate synthase (ALAS; E.C. 2.3.1.37) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the key regulatory step of porphyrin biosynthesis in metazoa, fungi, and α-proteobacteria.
Gregory A. Hunter   +3 more
doaj   +1 more source

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