Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Antonio Raggi"'
Autor:
Francesca Ronca, Antonio Raggi
Publikováno v:
Molecular and Cellular Biochemistry.
The N-terminal region of troponin T (TnT) does not bind any protein of the contractile machinery and the role of its hypervariability remains uncertain. In this review we report the evidence of the interaction between TnT and AMP deaminase (AMPD), a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd3cdbbf180a1e432d926da75d209ca7
https://doi.org/10.1007/s11010-023-04763-7
https://doi.org/10.1007/s11010-023-04763-7
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
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39927432539033a988aecdacadea251b
https://pubmed.ncbi.nlm.nih.gov/34710488
https://pubmed.ncbi.nlm.nih.gov/34710488
Autor:
Antonio Raggi, Francesca Ronca
Publikováno v:
Rendiconti Lincei. 28:143-158
In fast muscle, isoforms of troponin T (TnT) contain an N-terminal hypervariable region that does not bind any protein of the thin filament. The N-terminal domain of TnT is removed by calpain during stress conditions and so could modulate the role of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec5597bd74dfed8f885d14efac891f7f
https://doi.org/10.1007/s12210-016-0586-7
https://doi.org/10.1007/s12210-016-0586-7
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae08267efe0dc49d2373060efb56efc0
https://pubmed.ncbi.nlm.nih.gov/30142952
https://pubmed.ncbi.nlm.nih.gov/30142952
Autor:
Chiara Ippolito, L. Rossi, Antonio Raggi, Daniela Martini, Letizia Mattii, Antonietta Raffaella Maria Sabbatini, Greta Alì
Publikováno v:
Histochemistry and cell biology. 148(6)
Histidine-rich glycoprotein (HRG) is a relatively abundant plasma protein that is synthesized by parenchymal liver cells. Using Western blot analysis and immunoperoxidase techniques, we have previously shown the presence of HRG in human skeletal musc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7decacbf11ecd058c319abcc36143fcf
https://pubmed.ncbi.nlm.nih.gov/28702782
https://pubmed.ncbi.nlm.nih.gov/28702782
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e900474a16d57917ec4529eb1cbb59e
https://pubmed.ncbi.nlm.nih.gov/26409900
https://pubmed.ncbi.nlm.nih.gov/26409900
Autor:
Antonietta Raffaella Maria Sabbatini, Antonio Raggi, Maria Ranieri-Raggi, Arthur J. G. Moir, Daniela Martini
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1645:81-88
The histidine-proline-rich glycoprotein (HPRG) component of rabbit skeletal muscle AMP deaminase under denaturing and reducing conditions specifically binds to a Zn(2+)-charged affinity column and is only eluted with an EDTA-containing buffer that st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::483808b2517b88fa91cd2df3b2b58220
https://doi.org/10.1016/s1570-9639(02)00527-7
https://doi.org/10.1016/s1570-9639(02)00527-7
Autor:
Umberto Montali, Antonio Raggi, Maria Ranieri-Raggi, Francesca Ronca, Arthur J. G. Moir, Antonietta Raffaella Maria Sabbatini, Paul E. Brown
Publikováno v:
Scopus-Elsevier
Denaturation of rabbit skeletal-muscle AMP deaminase in acidic medium followed by chromatography on DEAE-cellulose in 8 M urea at pH 8.0 allows separation of two main peptide components of similar apparent molecular mass (75–80 kDa) that we tentati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e30b17ac11a4617381af85af0fb9fc8b
https://doi.org/10.1042/bj3260641
https://doi.org/10.1042/bj3260641