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Items: 11

1.

Erratum: Nepravishta, R., et al. CoCUN, a Novel Ubiquitin Binding Domain Identified in N4BP1. Biomolecules 2019, 9, 284.

Nepravishta R, Ferrentino F, Mandaliti W, Mattioni A, Weber J, Polo S, Castagnoli L, Cesareni G, Paci M, Santonico E.

Biomolecules. 2019 Nov 28;9(12). pii: E803. doi: 10.3390/biom9120803.

2.

CoCUN, a Novel Ubiquitin Binding Domain Identified in N4BP1.

Nepravishta R, Ferrentino F, Mandaliti W, Mattioni A, Weber J, Polo S, Castagnoli L, Cesareni G, Paci M, Santonico E.

Biomolecules. 2019 Jul 17;9(7). pii: E284. doi: 10.3390/biom9070284. Erratum in: Biomolecules. 2019 Nov 28;9(12):.

3.

CUBAN, a Case Study of Selective Binding: Structural Details of the Discrimination between Ubiquitin and NEDD8.

Santonico E, Nepravishta R, Mandaliti W, Castagnoli L, Cesareni G, Paci M.

Int J Mol Sci. 2019 Mar 8;20(5). pii: E1185. doi: 10.3390/ijms20051185.

4.

Selectivity of the CUBAN domain in the recognition of ubiquitin and NEDD8.

Castagnoli L, Mandaliti W, Nepravishta R, Valentini E, Mattioni A, Procopio R, Iannuccelli M, Polo S, Paci M, Cesareni G, Santonico E.

FEBS J. 2019 Feb;286(4):653-677. doi: 10.1111/febs.14752. Epub 2019 Feb 5.

5.

Potential mechanism of thymosin-α1-membrane interactions leading to pleiotropy: experimental evidence and hypotheses.

Mandaliti W, Nepravishta R, Pica F, Vallebona PS, Garaci E, Paci M.

Expert Opin Biol Ther. 2018 Jul;18(sup1):33-42. doi: 10.1080/14712598.2018.1456527. Review.

PMID:
30063856
6.

The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein.

Giachin G, Nepravishta R, Mandaliti W, Melino S, Margon A, Scaini D, Mazzei P, Piccolo A, Legname G, Paci M, Leita L.

PLoS One. 2017 Nov 21;12(11):e0188308. doi: 10.1371/journal.pone.0188308. eCollection 2017.

7.

Thymosin α1 Interacts with Hyaluronic Acid Electrostatically by Its Terminal Sequence LKEKK.

Mandaliti W, Nepravishta R, Pica F, Vallebona PS, Garaci E, Paci M.

Molecules. 2017 Oct 27;22(11). pii: E1843. doi: 10.3390/molecules22111843.

8.

Thymosin α1 Interacts with Exposed Phosphatidylserine in Membrane Models and in Cells and Uses Serum Albumin as a Carrier.

Mandaliti W, Nepravishta R, Sinibaldi Vallebona P, Pica F, Garaci E, Paci M.

Biochemistry. 2016 Mar 15;55(10):1462-72. doi: 10.1021/acs.biochem.5b01345. Epub 2016 Mar 3.

PMID:
26909491
9.

New studies about the insertion mechanism of Thymosin α1 in negative regions of model membranes as starting point of the bioactivity.

Mandaliti W, Nepravishta R, Sinibaldi Vallebona P, Pica F, Garaci E, Paci M.

Amino Acids. 2016 May;48(5):1231-9. doi: 10.1007/s00726-016-2169-4. Epub 2016 Jan 22.

PMID:
26801937
10.

Thymosin α1 inserts N terminus into model membranes assuming a helical conformation.

Nepravishta R, Mandaliti W, Eliseo T, Sinibaldi Vallebona P, Pica F, Garaci E, Paci M.

Expert Opin Biol Ther. 2015;15 Suppl 1:S71-81. doi: 10.1517/14712598.2015.1009034. Epub 2015 Feb 2.

PMID:
25642593
11.

Structure of the cyclic peptide [W8S]contryphan Vn: effect of the tryptophan/serine substitution on trans-cis proline isomerization.

Nepravishta R, Mandaliti W, Melino S, Eliseo T, Paci M.

Amino Acids. 2014 Dec;46(12):2841-53. doi: 10.1007/s00726-014-1841-9. Epub 2014 Sep 27.

PMID:
25261131

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