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Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase

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Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase (English)

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Mark J Pallen

1

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language of work or name

English

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publication date

August 2003

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published in

Protein Science

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volume

12

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issue

8

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page(s)

1804-7

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cites work

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The calmodulin-binding domain of the catalytic gamma subunit of phosphorylase kinase interacts with its inhibitory alpha subunit: evidence for a Ca2+ sensitive network of quaternary interactions

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Glucoamylase: structure/function relationships, and protein engineering

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Autosomal glycogenosis of liver and muscle due to phosphorylase kinase deficiency is caused by mutations in the phosphorylase kinase beta subunit (PHKB).

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Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.

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Studies on interaction of phosphorylase kinase from rabbit skeletal muscle with glycogen in the presence of ATP and ADP.

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The regulatory alpha subunit of phosphorylase kinase may directly participate in the binding of glycogen phosphorylase

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28 November 2018

Activators of phosphorylase kinase alter the cross-linking of its catalytic subunit to the C-terminal one-sixth of its regulatory alpha subunit

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12 December 2020

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inferred from PubMed ID database lookup

Kinetics of the interaction of rabbit skeletal muscle phosphorylase kinase with glycogen

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12 December 2020

based on heuristic

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PubMed publication ID

12876330

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ResearchGate publication ID

10649332

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(Q24644676)

Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase

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