R. Berni

ORCID: 0000-0002-1839-0479
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Research Areas
  • Retinoids in leukemia and cellular processes
  • Biotin and Related Studies
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Enzyme Structure and Function
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Cellular transport and secretion
  • Retinal Development and Disorders
  • Metabolism and Genetic Disorders
  • Protein Kinase Regulation and GTPase Signaling
  • Monoclonal and Polyclonal Antibodies Research
  • Biochemical effects in animals
  • Sulfur Compounds in Biology
  • Porphyrin Metabolism and Disorders
  • Amino Acid Enzymes and Metabolism
  • Protein Interaction Studies and Fluorescence Analysis
  • Cell Adhesion Molecules Research
  • Neonatal Health and Biochemistry
  • Antioxidant Activity and Oxidative Stress
  • Ubiquitin and proteasome pathways
  • Mitochondrial Function and Pathology
  • Chemical and Physical Properties in Aqueous Solutions
  • Synthesis and Characterization of Heterocyclic Compounds
  • Folate and B Vitamins Research
  • Chemical Synthesis and Analysis
  • Peptidase Inhibition and Analysis

University of Parma
2011-2023

Nara Institute of Science and Technology
2005

University of Pavia
1993-2001

University of Padua
1993-1994

Indiana University School of Medicine
1994

Italian Association for Cancer Research
1994

Indiana University – Purdue University Indianapolis
1994

National Research Council
1994

Industriale Chimica (Italy)
1994

Sapienza University of Rome
1991

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRetinol-binding protein is in the molten globule state at low pHV. E. Bychkova, Rodolfo Berni, Gian Luigi Rossi, V. P. Kutyshenko, and O. B. PtitsynCite this: Biochemistry 1992, 31, 33, 7566–7571Publication Date (Print):August 25, 1992Publication History Published online1 May 2002Published inissue 25 August 1992https://pubs.acs.org/doi/10.1021/bi00148a018https://doi.org/10.1021/bi00148a018research-articleACS PublicationsRequest reuse...

10.1021/bi00148a018 article EN Biochemistry 1992-08-25

The synthetic retinoid fenretinide (4‐HPR; N ‐[4‐hydroxyphenyl] all‐ trans ‐retinamide) interacts with plasma apo‐retinol‐binding protein (RBP)to form a tight complex (λ H J = 0.2 μM) which does not exhibit binding affinity to transthyretin (TTR). Therefore, substantial modification of the retinol hydroxyl group appear affect interaction RBP but drastically interfere protein—protein recognition. remarkable early reduction in level induced by administration may be associated high this and its...

10.1016/0014-5793(92)81046-o article EN FEBS Letters 1992-08-10

Two cellular retinol-binding proteins (CRBP I and II) with distinct tissue distributions retinoid-binding properties have been recognized thus far in mammals. Here, we report the identification of a human protein resembling type (55.6% identity) II (49.6% CRBPs, but unique H residue site distinctively different distribution. Additionally, this binding III) exhibits remarkable sequence identity (62.2%) recently identified ι-crystallin/CRBP diurnal gecko Lygodactylus picturatus [Werten, P. J....

10.1073/pnas.061455898 article EN Proceedings of the National Academy of Sciences 2001-03-27

The three-dimensional structures of bovine plasma retinol-binding protein (bRBP) complexed with retinol (space group P212121, a = 46.08,b 49.12,c 76.10

10.1016/s0021-9258(18)82046-4 article EN cc-by Journal of Biological Chemistry 1993-05-01

Transthyretin (TTR) is an amyloidogenic protein, the potential of which enhanced by a number specific point mutations. The ability to inhibit TTR fibrillogenesis known for several classes compounds, including natural polyphenols, protect native state specifically interacting with its thyroxine binding sites. Comparative analyses interaction and both stilbenoids flavonoids, some their main metabolites have been carried out. A finding this investigation was highly preferential resveratrol...

10.1074/jbc.m115.690172 article EN cc-by Journal of Biological Chemistry 2015-10-15

Three cellular retinol-binding protein (CRBP) types (CRBP I, II, and III) with distinct tissue distributions retinoid binding properties have been structurally characterized thus far. A human protein, whose mRNA is expressed primarily in kidney, heart, transverse colon, shown here to be a CRBP family member (human IV), according amino acid sequence, phylogenetic analysis, gene structure organization, x-ray structural analysis. Retinol IV leads an absorption spectrum from typical holo-CRBP by...

10.1074/jbc.m207124200 article EN cc-by Journal of Biological Chemistry 2002-10-25

10.1016/0167-4838(95)00264-2 article EN Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1996-05-01

The hydrolytic cleavage of the hydantoin ring allantoin, catalyzed by allantoinase, is required for utilization nitrogen present in purine-derived compounds. allantoinase gene (DAL1), however, missing many completely sequenced organisms able to use allantoin as a source. Here we show that an alternative (puuE) can be precisely identified analyzing its logic relationship with three other genes pathway. novel annotated structure and sequence data bases polysaccharide deacetylase homology...

10.1074/jbc.m801195200 article EN cc-by Journal of Biological Chemistry 2008-06-13

Human transthyretin (TTR) is an amyloidogenic protein whose mild amyloidogenicity enhanced by many point mutations affecting considerably the amyloid disease phenotype. To ascertain whether high potential of TTR variants may be explained on basis conformational change hypothesis, aim this work was to determine structural alterations for five crystallized under native and/or destabilizing (moderately acidic pH) conditions. While at pH changes more significant because a higher local...

10.1074/jbc.m109.017657 article EN cc-by Journal of Biological Chemistry 2009-07-16

Studies have been conducted to investigate the structure-function relationships of retinoids in their vitro interaction with plasma retinol-binding protein (RBP) and influence on retinol concentration. Two classes retinoids, one bearing modifications area hydroxyl end group (fenretinide, N-(ethyl) retinamide, all-trans, 13-cis retinoic acid) other also cyclohexene ring (etretinate, acitretin, arotinoid Ro 13-7410), were investigated. Whereas substantial do not prevent binding RBP, an intact...

10.1096/fasebj.7.12.8375617 article EN The FASEB Journal 1993-09-01

Abstract The objective of the study was to investigate relationship between first trimester maternal serum levels TTR-RBP4-ROH complex components and later insurgence an altered glucose metabolism during pregnancy. Retrospective case control including 96 patients 12th 14th week gestation, 32 that developed gestational diabetes mellitus (GDM), respectively, 21 non-insulin-treated (dGDM) 11 insulin-treated (iGDM), 20 large for age fetuses (LGA) without GDM 44 with normal outcome as control....

10.1515/cclm-2014-0929 article EN Clinical Chemistry and Laboratory Medicine (CCLM) 2015-01-01

In the course of reaction catalyzed by rhodanese, enzyme cycles between two catalytic intermediates, sulfur-free and sulfur-substituted (persulfide-containing) forms. The crystal structure which was prepared in solution then crystallized, is highly similar to that enzyme. inactivation rhodanese with a small molar excess hydrogen peroxide relies essentially on modification limited active site, consisting oxidation essential sulfhydryl sulfenyl group (-S-OH). Upon monoiodoacetate crystal,...

10.1074/jbc.271.35.21054 article EN cc-by Journal of Biological Chemistry 1996-08-01

In plasma the thyroid hormone-binding protein transthyretin (TTR) forms a tight complex with specific retinol carrier retinol-binding (RBP).The Ile-84 + Ser mutation and several other point mutations in TTR are associated familial amyloidotic polyneuropathy, which is characterized by extracellular depositions of amyloid fibrils mainly consisting mutated "RS.The interactions human RBP recombinant normal Ser-84 TTRs were investigated monitoring fluorescence anisotropy RBP-bound retinol.A...

10.1016/s0021-9258(17)31527-2 article EN cc-by Journal of Biological Chemistry 1994-09-01

1. Retinol‐binding protein (RBP) has been isolated from the pooled plasma or rainbow trouts ( Oncorhinchus mykiss ) by gel filtration, hydrophobic interaction chromatography and ion‐exchange chromatography. By this procedure two forms of protein, both with a molecular mass (approximately 20 kDa) similar to that mammalian RBP, were purified homogeneity. Five amino acid substitutions have found in partial (about 60%) sequences trout which are presumably acetylated at their N terminus. The...

10.1111/j.1432-1033.1992.tb16610.x article EN European Journal of Biochemistry 1992-02-01

The complete degradation of uric acid to (S)-allantoin, as recently elucidated, involves three enzymatic reactions. Inactivation by pseudogenization the genes pathway occurred during hominoid evolution, resulting in a high concentration urate blood and susceptibility gout. Here, we describe 1.8Å resolution crystal structure homodimeric 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase, which catalyzes last step pathway, for both ligand-free enzyme complex with substrate analogs...

10.1074/jbc.m701297200 article EN cc-by Journal of Biological Chemistry 2007-04-12

Transthyretin is a tetrameric binding protein involved in the transport of thyroid hormones and cotransport retinol by forming complex plasma with retinol‐binding protein. In present study, we report crystal structure macromolecular complex, which human transthyretin, holo‐retinol‐binding murine anti‐retinol‐binding Fab are assembled according to 1 : 2 stoichiometry. The main interactions, both polar apolar, between transthyretin involve hydroxyl group limited number solvent exposed...

10.1111/j.1742-4658.2008.06705.x article EN FEBS Journal 2008-11-11
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