PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
364475-0	1978	Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	94-114
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	129-149
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	210-215
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	210-215
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	210-215
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	151-156
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	42-53	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	129-149
21924318-0	2012	The eubacterial protein synthesis inhibitor pulvomycin interacts with archaeal elongation factor 1alpha from Sulfolobus solfataricus.	pulvomycin	44-54	Hsp20/alpha crystallin family protein	Saccharolobus solfataricus	79-103
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	42-53	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	151-156
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	42-53	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	210-215
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	42-53	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	210-215
364475-1	1978	Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated.	pulvomycin	42-53	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	210-215
364475-2	1978	Hydrolysis of GTP by EF-Tu, induced by aminoacyl-tRNA, ribosomes, and mRNA or by kirromycin, is inhibited by pulvomycin.	pulvomycin	109-119	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	21-26
364475-3	1978	As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP.	pulvomycin	99-109	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	158-163
364475-3	1978	As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP.	pulvomycin	99-109	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	212-217
33920736-4	2021	In this study, a docetaxel-resistant TNBC cell line (MDA-MB-231-DTR) was established, and mechanisms for the antitumor activity of pulvomycin, a novel STAT3 inhibitor isolated from marine-derived actinomycete, were investigated.	pulvomycin	131-141	signal transducer and activator of transcription 3	Mus musculus	151-156
33920736-7	2021	In addition, pulvomycin suppressed the activation of STAT3 and subsequently induced G0/G1 cell cycle arrest and apoptosis.	pulvomycin	13-23	signal transducer and activator of transcription 3	Mus musculus	53-58
33920736-9	2021	In an MDA-MB-231-DTR-bearing xenograft mouse model, the combination of pulvomycin and docetaxel effectively inhibited tumor growth through STAT3 regulation.	pulvomycin	71-81	signal transducer and activator of transcription 3	Mus musculus	139-144
33920736-0	2021	Antitumor Activity of Pulvomycin via Targeting Activated-STAT3 Signaling in Docetaxel-Resistant Triple-Negative Breast Cancer Cells.	pulvomycin	22-32	signal transducer and activator of transcription 3	Mus musculus	57-62
21924318-1	2012	The effect of pulvomycin on the biochemical and fluorescence spectroscopic properties of the archaeal elongation factor 1alpha from Sulfolobus solfataricus (SsEF-1alpha), the functional analog of eubacterial EF-Tu, was investigated.	pulvomycin	14-24	Hsp20/alpha crystallin family protein	Saccharolobus solfataricus	102-126
21924318-1	2012	The effect of pulvomycin on the biochemical and fluorescence spectroscopic properties of the archaeal elongation factor 1alpha from Sulfolobus solfataricus (SsEF-1alpha), the functional analog of eubacterial EF-Tu, was investigated.	pulvomycin	14-24	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	157-168
21924318-3	2012	The effect of the antibiotic on the partial reactions catalysed by SsEF-1alpha indicated that pulvomycin was able to decrease the affinity of the elongation factor toward aa-tRNA only in the presence of GTP, to an extent similar to that measured in the presence of GDP.	pulvomycin	94-104	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	67-78
21924318-7	2012	This finding was confirmed by the protection against chemical denaturation of SsEF-1alpha, observed in the presence of pulvomycin.	pulvomycin	119-129	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	78-89
16876786-2	2006	Kirromycin and enacyloxin block EF-Tu.GDP on the ribosome; pulvomycin and GE2270 A inhibit the interaction of EF-Tu.GTP with aa-tRNA.	pulvomycin	59-69	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	110-115
9405422-8	1997	Kirromycin and pulvomycin, antibiotics that specifically bind to EF-Tu and inhibit its activity in peptide elongation, also strongly inhibit EF-Tu-mediated renaturation of denatured rhodanese to levels near those observed for spontaneous, unassisted refolding.	pulvomycin	15-25	Tu translation elongation factor, mitochondrial	Homo sapiens	65-70
15581367-0	2004	Effects of the antibiotic pulvomycin on the elongation factor Tu-dependent reactions.	pulvomycin	26-36	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	44-64
15581367-2	2004	The antibiotic pulvomycin is an inhibitor of protein synthesis that prevents the formation of the ternary complex between elongation factor (EF-) Tu.GTP and aminoacyl-tRNA.	pulvomycin	15-25	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	122-148
15581367-4	2004	Pulvomycin markedly affects the equilibrium and kinetics of the EF-Tu-nucleotide interaction, particularly of the EF-Tu.GTP complex.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	64-69
15581367-4	2004	Pulvomycin markedly affects the equilibrium and kinetics of the EF-Tu-nucleotide interaction, particularly of the EF-Tu.GTP complex.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	114-119
15581367-7	2004	The effects of pulvomycin and EF-Ts can coexist and are simply additive, supporting the conclusion that these two ligands interact with different sites of EF-Tu.	pulvomycin	15-25	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	155-160
15581367-9	2004	Pulvomycin enhances the intrinsic EF-Tu GTPase activity, like kirromycin, though to a much more modest extent.	pulvomycin	0-10	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	34-39
15581367-12	2004	The property of pulvomycin to modify selectively the conformation(s) of EF-Tu is also supported by its effect on heat- and urea-dependent denaturation, and tryptic digestion of the protein.	pulvomycin	16-26	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	72-77
15581367-13	2004	Specific differences and similarities between the action of pulvomycin and the other EF-Tu-specific antibiotics are described and discussed.	pulvomycin	60-70	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	85-90
9405422-8	1997	Kirromycin and pulvomycin, antibiotics that specifically bind to EF-Tu and inhibit its activity in peptide elongation, also strongly inhibit EF-Tu-mediated renaturation of denatured rhodanese to levels near those observed for spontaneous, unassisted refolding.	pulvomycin	15-25	Tu translation elongation factor, mitochondrial	Homo sapiens	141-146