Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Anna Morleo"'
Publikováno v:
Journal of Molecular Biology. 413:940-951
Ferredoxins are ubiquitous proteins with electron transfer activity involved in a variety of biological processes. In this work, we investigated the characteristics and function of Fdx1 from Sorangium cellulosum So ce56 by using a combination of bioi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c99a5f651ddab4d99d9e98a8f97838c6
https://doi.org/10.1016/j.jmb.2011.09.010
https://doi.org/10.1016/j.jmb.2011.09.010
Publikováno v:
Biochemistry. 47:12795-12801
The HscA/HscB chaperone/cochaperone system accelerates transfer of iron-sulfur clusters from the FeS-scaffold protein IscU (IscU(2)[2Fe2S], holo-IscU) to acceptor proteins in an ATP-dependent manner. We have employed visible region circular dichroism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4db396533d290296b6e34bb2e74c497a
https://doi.org/10.1021/bi801565j
https://doi.org/10.1021/bi801565j
Autor:
Francesco Bonomi, Stefania Iametti, Donald M. Kurtz, Anna Morleo, Pasquale Ferranti, Enzio Ragg
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 13:981-991
The relationship between iron uptake by aporubredoxins (apoRds) and formation of native holorubredoxins (holoRd), including their Fe(SCys)(4) sites, was studied. In the absence of denaturants, apoRds exhibited spectroscopic features consistent with s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51576b1d1cf7eda85b94be99cca0bd98
https://doi.org/10.1007/s00775-008-0385-4
https://doi.org/10.1007/s00775-008-0385-4
Autor:
Stefania Iametti, Pasquale Ferranti, Fabio Sessa, Valentina Trinetta, Francesco Bonomi, Anna Morleo
Publikováno v:
FEMS microbiology letters. 334(2)
Sakacin A was purified to homogeneity through simple chromatographic procedures from cultures of Lactobacillus sakei DSMZ 6333 grown on a low-cost medium. The highly purified protein dissipated both transmembrane potential (ΔΨ) and transmembrane pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e670a25ebeb2c090c8b9309d4001f1de
https://pubmed.ncbi.nlm.nih.gov/22765043
https://pubmed.ncbi.nlm.nih.gov/22765043
Publikováno v:
Biochemistry. 50(44)
The scaffold protein IscU and molecular chaperones HscA and HscB play central roles in biological assembly of iron-sulfur clusters and maturation of iron-sulfur proteins. However, the structure of IscU-FeS complexes and the molecular mechanism whereb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f43b8a4826b761ce633fa18233650957
https://pubmed.ncbi.nlm.nih.gov/21977977
https://pubmed.ncbi.nlm.nih.gov/21977977
Publikováno v:
Biochemistry. 49(31)
Addition of iron salts to chaotrope-denatured aporubredoxin (apoRd) leads to nearly quantitative recovery of its single Fe(SCys)(4) site and native protein structure without significant dilution of the chaotrope. This "high-chaotrope" approach was us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3575f8715beb855fac71a412a9076297
https://pubmed.ncbi.nlm.nih.gov/20614892
https://pubmed.ncbi.nlm.nih.gov/20614892
Autor:
Francesco Bonomi, Stefania Mazzini, Marly K. Eidsness, Donald M. Kurtz, Anna Morleo, Stefania Iametti
The thermostabilities of Fe(2+) ligation in rubredoxins (Rds) from the hyperthermophile Pyrococcus furiosus (Pf) and the mesophiles Clostridium pasteurianum (Cp) and Desulfovibrio vulgaris (Dv) were compared. Residue 44 forms an NH.S(Cys) hydrogen bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eea2b536d9573d70d57d69e68e30e79d
http://hdl.handle.net/2434/6311
http://hdl.handle.net/2434/6311
Autor:
Marcella Cesana, Brunella Franco, Byung-Hoon Lee, Filomena Massa, Manuela Morleo, Miguel A. Prado, Roberta Tammaro, Daniel Finley
Publikováno v:
Human molecular genetics. 28(5)
Primary cilia are hair-like organelles that play crucial roles in vertebrate development, organogenesis and when dysfunctional result in pleiotropic human genetic disorders called ciliopathies, characterized by overlapping phenotypes, such as renal a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bede7565daeb76fdc95e215349843753
https://pubmed.ncbi.nlm.nih.gov/30388222
https://pubmed.ncbi.nlm.nih.gov/30388222