The glycine-rich loop of adenylate kinase forms a giant anion hole (Q28287798)

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Language	Label	Description	Also known as
English	The glycine-rich loop of adenylate kinase forms a giant anion hole	scientific article

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The glycine-rich loop of adenylate kinase forms a giant anion hole (English)

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author name string

D Dreusicke

1

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G E Schulz

2

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language of work or name

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publication date

24 November 1986

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208

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2

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301-4

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Two conformations of crystalline adenylate kinase

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Substrate positions and induced-fit in crystalline adenylate kinase

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Complete amino acid sequence of beta-tubulin from porcine brain

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Mechanism of activation of a human oncogene

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A point mutation is responsible for the acquisition of transforming properties by the T24 human bladder carcinoma oncogene

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Phosphate-binding sequences in nucleotide-binding proteins

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Amino acid sequence of the alpha subunit of transducin deduced from the cDNA sequence

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ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins

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The alpha-helix dipole and the properties of proteins

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Protein structural domains in the Caenorhabditis elegans unc-54 myosin heavy chain gene are not separated by introns

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Homologies between signal transducing G proteins and ras gene products

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Biological properties of human c-Ha-ras1 genes mutated at codon 12.

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Three-dimensional structure of adenyl kinase

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Homology between human bladder carcinoma oncogene product and mitochondrial ATP-synthase

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Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant

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Homologies and anomalies in primary structural patterns of nucleotide binding proteins

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Purification, characterization and crystallization of pork myokinase

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Low resolution structure of adenylate kinase

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Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase

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10.1016/0014-5793(86)81037-7

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