Results 231 to 240 of about 945,743 (288)
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Adenylate kinase in human tissue II. Serum adenylate kinase and myocardial infarction

Journal of Molecular and Cellular Cardiology, 1973
Abstract Serum adenylate kinase was measured in 116 patients. An elevated level of serum adenylate kinase correlated well with myocardial infarctions and some other conditions associated with necrotising lesions. By taking advantage of the organ specificity of adenylate kinase, it was determined that a large portion of serum adenylate kinase activity
J M Horenstein   +3 more
openaire   +3 more sources

Identification of a novel adenylate kinase system in the brain: Cloning of the fourth adenylate kinase

Molecular Brain Research, 1998
We identify a novel subtype of adenylate kinase, which is the 4th adenylate kinase (AK4), in the vertebrate. AK4 mRNA is expressed in the mammalian central nervous system in a region-specific manner from the middle stage of embryogenesis to the adulthood in the rodent. The presence of three isozymes of adenylate kinase (AK1, AK2 and AK3) that maintains
Mitsuyo Maeda   +3 more
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Adenylate kinase fromRhodospirillum rubrum

Experientia, 1978
A partial purification and some properties of adenylate kinase from the photosynthetic bacterium Rhodospirillum rubrum are described.
M. C. Archer, H. S. Yang
openaire   +3 more sources

Low resolution structure of adenylate kinase

Journal of Molecular Biology, 1973
Abstract A low resolution model of adenylate kinase has been derived from a 6 A electron density map. The molecular shape can be described approximately as an oblate ellipsoid with dimensions 40 A × 40 A × 30 A. The molecule is composed of two globular units separated by a 10 A deep cleft.
Schulz, G.   +3 more
openaire   +4 more sources

Three-dimensional structure of adenyl kinase

Nature, 1974
A combination of X-ray data at 3 A resolution and sequence results has yielded the atomic structure of adenyl kinase, a ubiquitous enzyme which catalyses the phosphorylation of AMP by ATP. The abundant secondary structures of the protein and the probable binding sites for ATP and AMP are described.
M. Elzinga   +4 more
openaire   +4 more sources

Two conformations of crystalline adenylate kinase

Journal of Molecular Biology, 1977
Abstract Pig muscle adenylate kinase (EC2.7.4.3) can exist in three crystal forms, which are interconvertible. For crystal form A the enzyme structure is known in atomic detail. We report the X-ray diffraction analysis of crystal form B at 4.7 A resolution and a comparison with the A form.
Sachsenheimer, W., Schulz, G.
openaire   +4 more sources

A reactive arginine in adenylate kinase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
Adenylate kinase (ATP:AMP phosphotransferase, EV 2.7.4.3) from pig heart is inactivated by the specific arginyl reagent phenylglyoxal. During inactivation two molecules of phenyglyoxal are incorporated into the protein indicating the modification of one of the 11 arginine residues. The modification of other amino acids is ruled out.
openaire   +3 more sources

Exploring the Dynamic Functional Landscape of Adenylate Kinase Modulated by Substrates.

Journal of Chemical Theory and Computation, 2013
Adenylate kinase (ADK) has been explored widely, through both experimental and theoretical studies. However, still less is known about how the functional dynamics of ADK is modulated explicitly by its natural substrates.
Yong Wang   +3 more
semanticscholar   +1 more source

The many isoforms of human adenylate kinases

The International Journal of Biochemistry & Cell Biology, 2014
Adenine nucleotides are involved in a variety of cellular metabolic processes, including nucleic acid synthesis and repair, formation of coenzymes, energy transfer, cell and ciliary motility, hormone secretion, gene expression regulation and ion-channel control.
Christakis Panayiotou   +2 more
openaire   +3 more sources

Structural topology and activation of an initial adenylate kinase-substrate complex.

Biochemistry, 2013
Enzymatic activity is ultimately defined by the structure, chemistry, and dynamics of the Michaelis complex. A large number of experimentally determined structures between enzymes and substrates, substrate analogues, or inhibitors exist.
Jörgen Ådén   +4 more
semanticscholar   +1 more source

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