PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17176059-1	2006	The salivary antimicrobial peptide histatin 5 is characterized by its cationic nature, structural flexibility, and the presence of two metal-binding sites (the ATCUN motif and a Zn-binding motif).	Zinc	178-180	histatin 3	Homo sapiens	35-45	
31052346-4	2019	Here we apply a multi-disciplinary approach using small angle X-ray scattering, nuclear magnetic resonance spectroscopy, calorimetry and computations to show that that saliva protein Histatin 5 forms highly dynamic oligomers in the presence of Zn2+.	Zinc	244-248	histatin 3	Homo sapiens	183-193	
31052346-7	2019	Finally, as Histatin 5 is an important saliva component, we suggest that Zn2+ induced oligomerisation may be crucial for maintaining saliva homeostasis.	Zinc	73-77	histatin 3	Homo sapiens	12-22	
22786744-8	2012	However, with cyclic histatin 5, the presence of Zn(2+) ions is also necessary to fuse the peptide to the micelle.	Zinc	49-51	histatin 3	Homo sapiens	21-31	
32751915-2	2020	Hst 5 binds to multiple cations including dimerization-inducing zinc (Zn2+), although the function of this capability is incompletely understood.	Zinc	70-74	histatin 3	Homo sapiens	0-5	
32751915-3	2020	Hst 5 is taken up by C. albicans and acts on intracellular targets under metal-free conditions; however, Zn2+ is abundant in saliva and may functionally affect Hst 5.	Zinc	105-109	histatin 3	Homo sapiens	0-5	
32751915-3	2020	Hst 5 is taken up by C. albicans and acts on intracellular targets under metal-free conditions; however, Zn2+ is abundant in saliva and may functionally affect Hst 5.	Zinc	105-109	histatin 3	Homo sapiens	160-165	
32751915-5	2020	Through the use of Hst 5 and two derivatives, P113 (AA 4-15 of Hst 5) and Hst 5DeltaMB (AA 1-3 and 15-19 mutated to Glu), we determined that Zn2+ significantly increases killing activity of Hst 5 and P113 for both C. albicans and Candida glabrata.	Zinc	141-145	histatin 3	Homo sapiens	19-24	
32751915-5	2020	Through the use of Hst 5 and two derivatives, P113 (AA 4-15 of Hst 5) and Hst 5DeltaMB (AA 1-3 and 15-19 mutated to Glu), we determined that Zn2+ significantly increases killing activity of Hst 5 and P113 for both C. albicans and Candida glabrata.	Zinc	141-145	histatin 3	Homo sapiens	63-68	
32751915-5	2020	Through the use of Hst 5 and two derivatives, P113 (AA 4-15 of Hst 5) and Hst 5DeltaMB (AA 1-3 and 15-19 mutated to Glu), we determined that Zn2+ significantly increases killing activity of Hst 5 and P113 for both C. albicans and Candida glabrata.	Zinc	141-145	histatin 3	Homo sapiens	63-68	
32751915-8	2020	High-performance liquid chromatography (HPLC) showed that the higher relative Zn2+ affinity of Hst 5 likely promotes dimerization.	Zinc	78-82	histatin 3	Homo sapiens	95-100	
32751915-9	2020	Together, these results suggest peptide assembly into fungicidal pore structures in the presence of Zn2+, representing a novel mechanism of action that has exciting potential to expand the list of Hst 5-susceptible pathogens.	Zinc	100-104	histatin 3	Homo sapiens	197-202	
20815365-0	2010	Structural characterization and antimicrobial activity of the Zn(II) complex with P113 (demegen), a derivative of histatin 5.	Zinc	62-68	histatin 3	Homo sapiens	114-124	
16704414-6	2006	Similar Zn2+-dependent antibacterial activities were shown for histatin 5 as well as histidine-containing peptides derived from the Zn2+- and heparin-binding domain 5 of human kininogen.	Zinc	8-12	histatin 3	Homo sapiens	63-73	
11006580-3	2000	H3 and H5 formed high affinity complexes with Cu(2+) and Ni(2+) and, to a lesser extent, with Zn(2+).	Zinc	94-96	histatin 3	Homo sapiens	0-2	
11006580-3	2000	H3 and H5 formed high affinity complexes with Cu(2+) and Ni(2+) and, to a lesser extent, with Zn(2+).	Zinc	94-96	histatin 3	Homo sapiens	7-9	
10423240-0	1999	Zn(2+) ions selectively induce antimicrobial salivary peptide histatin-5 to fuse negatively charged vesicles.	Zinc	0-2	histatin 3	Homo sapiens	62-72