A. Raggi

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Isolation by zinc-affinity chromatography of the histidine-proline-rich-glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzy

A. Moir, D. Martini, M. Ranieri-Raggi, 2003, Biochimica et biophysica acta.

Immunohistochemical localization of histidine-rich glycoprotein in human skeletal muscle: preferential distribution of the protein at the sarcomeric I-band

D. Martini, L. Mattii, C. Ippolito, 2017, Histochemistry and Cell Biology.

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

F. Ronca, A. Raggi, 2018, Biomolecules.

Immunohistochemical analysis of human skeletal muscle AMP deaminase deficiency. Evidence of a correlation between the muscle HPRG content and the level of the residual AMP deaminase activity

A. Moir, A. Toscano, D. Martini, 2006, Journal of Muscle Research & Cell Motility.

Interaction of rat muscle AMP aminohydrolase with chelating agents and metal ions

M. Ranieri, G. Ronca, A. Raggi, 1970, FEBS letters.

Presence in Human Skeletal Muscle of an AMP Deaminase-associated Protein That Reacts with an Antibody to Human Plasma Histidine-Proline-rich Glycoprotein

A. Moir, P. Viacava, J. R. Ashby, 1999, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

Association of purified skeletal-muscle AMP deaminase with a histidine-proline-rich-glycoprotein-like molecule.

A. Moir, F. Ronca, U. Montali, 1997, The Biochemical journal.

Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. A new model for substrate interactions at a dinuclear cocatalytic Zn site.

A. Moir, S. Mangani, D. Martini, 2007, Biochimica et biophysica acta.

Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site.

A. Moir, S. Mangani, D. Martini, 2007, Biochimica et biophysica acta.

Characterization of the Zinc-binding Site of the Histidine-Proline-rich Glycoprotein Associated with Rabbit Skeletal Muscle AMP Deaminase*

A. Moir, S. Mangani, D. Martini, 2003, The Journal of Biological Chemistry.

Effect of pH on the kinetic properties of rat skeletal muscle AMP deaminase.

M. Ranieri-Raggi, A. Raggi, C. Bergamini, 1980, The Italian journal of biochemistry.

Specific modification of the GTP binding sites of rat 5'-adenylic acid aminohydrolase by periodate-oxidized GTP.

M. Ranieri-Raggi, A. Raggi, 1976, Biochimica et Biophysica Acta.

Regulation of skeletal muscle AMP deaminase: lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the rabbit enzyme.

D. Martini, M. Ranieri-Raggi, A. Sabbatini, 2001, Biochimica et biophysica acta.

Interaction with troponin T from white skeletal muscle restores in white skeletal muscle AMP deaminase those allosteric properties removed by limited proteolysis.

A. Moir, M. Ranieri-Raggi, A. Raggi, 1985, Biochimica et biophysica acta.

Regulation of skeletal muscle AMP deaminase effects of limited proteolysis on the activity of the rabbit enzyme

M. Ranieri-Raggi, A. Raggi, 1979, FEBS letters.

Negative homotropic cooperativity in rat muscle AMP deaminase. A kinetic study on the inhibition of the enzyme by ATP.

M. Ranieri-Raggi, A. Raggi, 1979, Biochimica et biophysica acta.

Isozymes of AMP deaminase in red and white skeletal muscles

G. Ronca, A. Raggi, C. Bergamini, 1975, FEBS letters.

The nature of inactivation of rat muscle 5'-adenylate aminohydrolase by fluorodinitrobenzene.

G. Ronca, A. Raggi, C. Bergamini, 1975, The Biochemical journal.

Muscle AMP aminohydrolase. X. Effect of anions on the kinetic and regulatory properties of the rat muscle enzyme.

G. Ronca, A. Raggi, S. Ronca-Testoni, 1972, The Italian journal of biochemistry.

Muscle AMP aminohydrolase. IV. Purification of rat muscle enzyme.

M. Ranieri, G. Ronca, A. Raggi, 1970, The Italian journal of biochemistry.

Muscle AMP aminohydrolase. 3. A comparative study on the regulatory properties of skeletal muscle enzyme from various species.

G. Ronca, A. Raggi, S. Ronca-Testoni, 1970, Biochimica et biophysica acta.

Muscle AMP aminohydrolase. I. Some regulatory properties of rat skeletal muscle enzyme.

G. Ronca, A. Raggi, S. Ronca-Testoni, 1968, Biochimica et biophysica acta.

Structure-function relationships in mammalian histidine-proline-rich glycoprotein.

F. Ronca, A. Raggi, 2015, Biochimie.

Muscle AMP aminohydrolase. II. Distribution of AMP aminohydrolase, myokinase and creatine kinase activities in skeletal muscle.

G. Ronca, A. Raggi, S. Ronco-Testoni, 1969, Biochimica et biophysica acta.

Muscle AMP aminohydrolase. 8. The reactivity of the sulfhydryl groups of rat muscle AMP deaminase.

M. Ranieri, C. Rossi, G. Ronca, 1972, Biochimica et biophysica acta.

Role of troponin T and AMP deaminase in the modulation of skeletal muscle contraction

F. Ronca, Francesca Ronca, Antonio Raggi, 2017, Rendiconti Lincei.

Structure-function relationships in cardiac troponin T.

A. Moir, S. Perry, R. Grand, 1989, Biochimica et biophysica acta.

Evidence of a species-differentiated regulatory domain within the N-terminal region of skeletal muscle AMP deaminase.

A. Moir, F. Ronca, M. Ranieri-Raggi, 1994, Biochimica et biophysica acta.

Effects of storage on activity and subunit structure of rabbit skeletal-muscle AMP deaminase.

M. Ranieri-Raggi, A. Raggi, 1980, The Biochemical journal.

A calpain-like proteolytic activity produces the limited cleavage at the N-terminal regulatory domain of rabbit skeletal muscle AMP deaminase: evidence of a protective molecular mechanism.

A. Moir, D. Martini, U. Montali, 2004, Biochimica et biophysica acta.

Regulation of skeletal-muscle AMP deaminase. Evidence for a highly pH-dependent inhibition by ATP of the homogeneous derivative of the rabbit enzyme yielded by limited proteolysis.

M. Ranieri-Raggi, A. Raggi, 1990, The Biochemical journal.

Regulation of skeletal muscle AMP deaminase. Carbethoxylation of His-51 belonging to the zinc coordination sphere of the rabbit enzyme promotes its desensitization towards the inhibition by ATP.

F. Ronca, A. Raggi, 2021, Biochimica et biophysica acta. General subjects.

The Role of Histidine-Proline-Rich Glycoprotein as Zinc Chaperone for Skeletal Muscle AMP Deaminase

A. Moir, M. Ranieri-Raggi, A. Raggi, 2014, Biomolecules.

Regulatory properties of AMP deaminase isoenzymes from rabbit red muscle.

M. Ranieri-Raggi, A. Raggi, 1987, The Biochemical journal.

Adenylate metabolism in the heart. Regulatory properties of rabbit cardiac adenylate deaminase.

R. Barsacchi, M. Ranieri-Raggi, A. Raggi, 1979, Biochemical Journal.

Role of the interaction between troponin T and AMP deaminase by zinc bridge in modulating muscle contraction and ammonia production

F. Ronca, A. Raggi, 2023, Molecular and cellular biochemistry.

Evidence that muscle cells do not express the histidine-rich glycoprotein associated with AMP deaminase but can internalise the plasma protein

A. Moir, D. Martini, L. Mattii, 2011, European journal of histochemistry : EJH.