Zobrazeno 1 - 10
of 34
pro vyhledávání: '"histidine–proline-rich glycoprotein"'
Publikováno v:
Biomolecules, Vol 4, Iss 2, Pp 474-497 (2014)
Metallochaperones function as intracellular shuttles for metal ions. At present, no evidence for the existence of any eukaryotic zinc-chaperone has been provided although metallochaperones could be critical for the physiological functions of Zn2+ met
Externí odkaz:
https://doaj.org/article/2efe46a4af4a4e7db8b4bca114abafc6
Autor:
Francesca Ronca, Antonio Raggi
Publikováno v:
Biomolecules, Vol 8, Iss 3, p 79 (2018)
Multiple muscle-specific isoforms of the Zn2+ metalloenzyme AMP deaminase (AMPD) have been identified based on their biochemical and genetic differences. Our previous observations suggested that the metal binding protein histidine-proline-rich glycop
Externí odkaz:
https://doaj.org/article/b8e86b9d978a4f3794c48f61ddadd69d
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 9343, p 9343 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 24
International journal of molecular sciences
21 (2020). doi:10.3390/ijms21249343
info:cnr-pdr/source/autori:Santoro, Anna Maria; Zimbone, Stefania; Magri, Antonio; La Mendola, Diego; Grasso, Giulia/titolo:The Role of Copper (II) on Kininogen Binding to Tropomyosin in the Presence of a Histidine-Proline-Rich Peptide/doi:10.3390%2Fijms21249343/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:21
International Journal of Molecular Sciences
Volume 21
Issue 24
International journal of molecular sciences
21 (2020). doi:10.3390/ijms21249343
info:cnr-pdr/source/autori:Santoro, Anna Maria; Zimbone, Stefania; Magri, Antonio; La Mendola, Diego; Grasso, Giulia/titolo:The Role of Copper (II) on Kininogen Binding to Tropomyosin in the Presence of a Histidine-Proline-Rich Peptide/doi:10.3390%2Fijms21249343/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:21
The antiangiogenic activity of the H/P domain of histidine&ndash
proline-rich glycoprotein is mediated by its binding with tropomyosin, a protein exposed on endothelial cell-surface during the angiogenic switch, in presence of zinc ions. Althoug
proline-rich glycoprotein is mediated by its binding with tropomyosin, a protein exposed on endothelial cell-surface during the angiogenic switch, in presence of zinc ions. Althoug
Autor:
Antonio Raggi, Francesca Ronca
Publikováno v:
Biochimica et biophysica acta. General subjects. 1866(2)
Background Skeletal muscle AMP deaminase (AMPD1) regulates the concentration of adenine nucleotides during muscle contraction. We previously provided evidence that rabbit AMPD1 is composed by two HPRG 73 kDa subunits and two 85 kDa catalytic subunits
Akademický článek
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Autor:
Antonio Raggi, Francesca Ronca
Publikováno v:
Biomolecules
Biomolecules, Vol 8, Iss 3, p 79 (2018)
Biomolecules, Vol 8, Iss 3, p 79 (2018)
Multiple muscle-specific isoforms of the Zn2+ metalloenzyme AMP deaminase (AMPD) have been identified based on their biochemical and genetic differences. Our previous observations suggested that the metal binding protein histidine-proline-rich glycop
Akademický článek
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Autor:
Antonio Raggi, Francesca Ronca
Publikováno v:
Biochimie. 118
Histidine-proline-rich glycoprotein (HPRG), or histidine-rich glycoprotein (HRG), is a serum protein that is synthesized in the liver and is actively internalised by different cells, including skeletal muscle. The multidomain arrangement of HPRG comp
Publikováno v:
Biochemistry. 35(6)
The complete primary structure of rabbit plasma histidine-proline-rich glycoprotein (HPRG), also known as histidine-rich glycoprotein, was determined by a combination of cDNA and peptide sequencing. Limited proteolysis with plasmin yielded three disu
Akademický článek
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