PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24648395-0	2014	Arginine decarboxylase and agmatinase: an alternative pathway for de novo biosynthesis of polyamines for development of mammalian conceptuses.	Polyamines	90-100	agmatinase	Homo sapiens	27-37	
24648395-2	2014	However, metabolism of arginine to agmatine via arginine decarboxylase (ADC) and conversion of agmatine to polyamines via agmatinase (AGMAT) is an alternative pathway long recognized in lower organisms, but only recently suggested for neurons and liver cells of mammals.	Polyamines	107-117	agmatinase	Homo sapiens	122-132	
24648395-2	2014	However, metabolism of arginine to agmatine via arginine decarboxylase (ADC) and conversion of agmatine to polyamines via agmatinase (AGMAT) is an alternative pathway long recognized in lower organisms, but only recently suggested for neurons and liver cells of mammals.	Polyamines	107-117	agmatinase	Homo sapiens	134-139	
24648395-3	2014	We now provide evidence for a functional ADC/AGMAT pathway for the synthesis of polyamines in mammalian reproductive tissue for embryonic survival and development.	Polyamines	80-90	agmatinase	Homo sapiens	45-50	
24648395-5	2014	Furthermore, we found that increases in ADC/AGMAT mRNA levels and in the translation of AGMAT mRNA among conceptuses in MAO-ODC1 knockdown compensated for the loss of ODC1, supporting polyamine synthesis from arginine and accounting for the normal and abnormal phenotypes of conceptuses.	Polyamines	184-193	agmatinase	Homo sapiens	88-93	
24648395-6	2014	We conclude that the majority of polyamine synthesis is by the conventional ODC1-dependent pathway (arginine-ornithine-putrescine) and that deficiencies in ODC1 result in increased activity of the rescue ADC/AGMAT-dependent pathway (arginine-agmatine-putrescine) for production of polyamines.	Polyamines	33-42	agmatinase	Homo sapiens	208-213	
24648395-6	2014	We conclude that the majority of polyamine synthesis is by the conventional ODC1-dependent pathway (arginine-ornithine-putrescine) and that deficiencies in ODC1 result in increased activity of the rescue ADC/AGMAT-dependent pathway (arginine-agmatine-putrescine) for production of polyamines.	Polyamines	281-291	agmatinase	Homo sapiens	208-213	
11914032-1	2002	Arginine decarboxylase (ADC) and agmatinase are part of an operon in Escherichia coli, which constitutes the primary pathway of polyamine synthesis from arginine.	Polyamines	128-137	agmatinase	Homo sapiens	33-43	
20563878-7	2011	When comparing the overall agmatinase expression with immunocytochemical data available for agmatine and polyamine biosynthetic enzymes, the observed pattern may argue in favor of an agmatine inactivating function rather than fueling the alternative pathway of polyamine synthesis.	Polyamines	261-270	agmatinase	Homo sapiens	27-37	
11804860-2	2002	Agmatinase, which hydrolyzes agmatine to putrescine and urea, not only represents a potentially important mechanism for regulating the biological effects of agmatine in mammalian cells but also represents an alternative to ornithine decarboxylase for polyamine biosynthesis.	Polyamines	251-260	agmatinase	Homo sapiens	0-10