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Details on Person Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications

Class:IdLiteratureReference:6807571
_displayNameHistatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications
_timestamp2015-11-03 14:50:43
author[Person:6807569] Melino, Sonia
[Person:6807579] Santone, Celeste
[Person:6807588] Di Nardo, Paolo
[Person:6807574] Sarkar, Bibudhendra
created[InstanceEdit:6807563] Shamovsky, Veronica, 2015-11-03
journalFEBS J.
pages657-72
pubMedIdentifier24219363
titleHistatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications
volume281
year2014
(literatureReference)[Summation:8861674] Histatins (HTNs) is a family of small, histidine-rich (18-28...
[Reaction:6807144] HTN1,HTN3 or HTN5 binds the bacterial anionic surface [Homo sapiens]
[Reaction:6807581] HTN5, (HTN1, HTN3) binds fungal SSA1/SSA2 [Homo sapiens]
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No pathways have been reviewed or authored by Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications (6807571)