PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14642817-1	2003	In this work, the effect of Fenton reaction on two elastin cross-linked amino acids, desmosine (DES) and isodesmosine (IDE), in the absence or presence of different wavelength radiations generated from artificial sources has been evaluated using LC/ESI-MS. Irradiation as well as incubation of DES or IDE solutions in the presence of Fe(2+) and H(2)O(2) resulted in products with m/z 497.1 and 481.1 for [M+H](+).	Iron	28-30	elastin	Homo sapiens	51-58	
28833753-11	2017	Iron-saturated Lf (holo-Lf) increased TE expression and promoted Akt1 phosphorylation, when compared to those parameters in cells treated with iron-free Lf (apo-Lf).	Iron	0-4	elastin	Homo sapiens	38-40	
17634261-3	2007	Recently, it was demonstrated that low concentrations of free iron upregulate elastin gene expression in cultured fibroblasts.	Iron	62-66	elastin	Homo sapiens	78-85	
15537639-0	2005	Fluctuations of intracellular iron modulate elastin production.	Iron	30-34	elastin	Homo sapiens	44-51	
15537639-3	2005	In the present report we demonstrate that treatment of cultured human skin fibroblasts with low concentration of iron 2-20 microm (ferric ammonium citrate) induced a significant increase in the synthesis of tropoelastin and deposition of insoluble elastin.	Iron	113-117	elastin	Homo sapiens	212-219	
15537639-4	2005	Northern blot and real-time reverse transcription-PCR analysis revealed that treatment with 20 microm iron led to an increase of approximately 3-fold in elastin mRNA levels.	Iron	102-106	elastin	Homo sapiens	153-160	
15537639-5	2005	Because treatment with an intracellular iron chelator, desferrioxamine, caused a significant decrease in elastin mRNA level and consequent inhibition of elastin deposition, we conclude that iron facilitates elastin gene expression.	Iron	40-44	elastin	Homo sapiens	105-112	
15537639-5	2005	Because treatment with an intracellular iron chelator, desferrioxamine, caused a significant decrease in elastin mRNA level and consequent inhibition of elastin deposition, we conclude that iron facilitates elastin gene expression.	Iron	40-44	elastin	Homo sapiens	153-160	
15537639-5	2005	Because treatment with an intracellular iron chelator, desferrioxamine, caused a significant decrease in elastin mRNA level and consequent inhibition of elastin deposition, we conclude that iron facilitates elastin gene expression.	Iron	40-44	elastin	Homo sapiens	153-160	
15537639-5	2005	Because treatment with an intracellular iron chelator, desferrioxamine, caused a significant decrease in elastin mRNA level and consequent inhibition of elastin deposition, we conclude that iron facilitates elastin gene expression.	Iron	190-194	elastin	Homo sapiens	105-112	
15537639-5	2005	Because treatment with an intracellular iron chelator, desferrioxamine, caused a significant decrease in elastin mRNA level and consequent inhibition of elastin deposition, we conclude that iron facilitates elastin gene expression.	Iron	190-194	elastin	Homo sapiens	153-160	
15537639-5	2005	Because treatment with an intracellular iron chelator, desferrioxamine, caused a significant decrease in elastin mRNA level and consequent inhibition of elastin deposition, we conclude that iron facilitates elastin gene expression.	Iron	190-194	elastin	Homo sapiens	153-160	
15537639-6	2005	Our experimental evidence also demonstrates the existence of an opposite effect, in which higher, but not cytotoxic concentrations of iron (100-400 microm) induced the production of intracellular reactive oxygen species that coincided with a significant decrease in elastin message stability and the disappearance of iron-dependent stimulatory effect on elastogenesis.	Iron	134-138	elastin	Homo sapiens	266-273	
15537639-8	2005	Thus, presented data, for the first time, demonstrate the existence of two opposite iron-dependent mechanisms that may affect the steady state of elastin message.	Iron	84-88	elastin	Homo sapiens	146-153	
10719247-4	2000	Here, we argue that (i) the heavily glycated proteins known to accumulate in people with diabetes gain an increased affinity for transition metals such as iron and copper, (ii) as a result, proteins such as elastin and collagen within the arterial wall-which are known to be particularly heavily glycosylated in diabetes-may accumulate bound metal, especially copper, (iii) the bound metal causes the catalytic destruction of endothelium derived relaxing factor (nitric oxide or a derivative thereof), thereby engendering a state of chronic vasoconstriction.	Iron	155-159	elastin	Homo sapiens	207-214	
8279451-7	1994	Energy dispersive x-ray analysis and TEM demonstrated iron and calcium on the microfibrillar portion of elastin.	Iron	54-58	elastin	Homo sapiens	104-111	
9753639-2	1998	In support of this we find that, when glycated, three different proteins--albumin, gelatin (a soluble collagen fragment) and elastin--all gain a substantial affinity for the transition metals iron and copper.	Iron	192-196	elastin	Homo sapiens	125-132	
2659611-2	1989	Four points are fundamental: copper is combined with essential enzymatic systems (oxidases, transaminases), copper is necessary for inclusion of iron in the molecule of hemoglobin, copper has a primordial role in the metabolism of molecule of hemoglobin, copper has a primordial role in the metabolism of collagen and elastin and some vascular diseases (aneurysms) are closely related to its lack, finally, there is an increase of plasmatic copper during cancerous diseases, which is significant even at an early time and usually proportional to the evolution.	Iron	145-149	elastin	Homo sapiens	318-325	
6118903-1	1981	Both iron and copper play critical biochemical roles in the post-translational modifications of collagen and elastin.	Iron	5-9	elastin	Homo sapiens	109-116	
90671-4	1979	Substitution of Fe++ for Fe+++ abolished dye binding by elastin.	Iron	16-20	elastin	Homo sapiens	56-63	
90671-4	1979	Substitution of Fe++ for Fe+++ abolished dye binding by elastin.	Iron	25-30	elastin	Homo sapiens	56-63	
31619363-10	2019	Studying aortic rings, we found that iron significantly either prevents or reverts the high-Pi induced collagen deposition and the elastin decrease, preserving elastin structure (0.7 +- 0.1 vs 1.2 +- 0.1; Pi vs Pi + Fe, p < 0.05, elastin mRNA relative expression).	Iron	37-41	elastin	Homo sapiens	131-138	
31619363-10	2019	Studying aortic rings, we found that iron significantly either prevents or reverts the high-Pi induced collagen deposition and the elastin decrease, preserving elastin structure (0.7 +- 0.1 vs 1.2 +- 0.1; Pi vs Pi + Fe, p < 0.05, elastin mRNA relative expression).	Iron	37-41	elastin	Homo sapiens	160-167	
31619363-10	2019	Studying aortic rings, we found that iron significantly either prevents or reverts the high-Pi induced collagen deposition and the elastin decrease, preserving elastin structure (0.7 +- 0.1 vs 1.2 +- 0.1; Pi vs Pi + Fe, p < 0.05, elastin mRNA relative expression).	Iron	37-41	elastin	Homo sapiens	160-167