PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31393126-6	2019	A total of 50 N-glycopeptides and 30 N-glycans have been site-specific glycosylation profiled in major royal jelly protein 1 (MRJP1) and MRJP2 of RJ for the first time.	n-glycopeptides	14-29	major royal jelly protein 1	Apis mellifera	126-131
32683019-4	2020	Cypermethrin caused minor induction of mrjp1, mrjp2, mmp1 and ilp1.	cypermethrin	0-12	major royal jelly protein 1	Apis mellifera	39-44
32683019-5	2020	The sima transcript showed down-regulation at 48 h and up-regulation at 72 h. Exposure to thiacloprid caused down-regulation of vitellogenin, mrjp1 and sima at 24 h, and hbg3 at 72 h, as well as induction of ilp1 at 48 h. The buffy transcript was down-regulated at 24 h and up-regulated at 48 h. Despite compound-specific expression patterns, each insecticide altered the expression of some of the suggested endocrine system related genes.	thiacloprid	90-101	major royal jelly protein 1	Apis mellifera	142-147
31393126-6	2019	A total of 50 N-glycopeptides and 30 N-glycans have been site-specific glycosylation profiled in major royal jelly protein 1 (MRJP1) and MRJP2 of RJ for the first time.	n-glycans	37-46	major royal jelly protein 1	Apis mellifera	126-131
31393126-8	2019	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.	Nitrogen	4-5	major royal jelly protein 1	Apis mellifera	112-117
31393126-9	2019	There were 18, 17, and 2 N-glycans attached to MRJP1, MRJP2, and MRJP3, respectively.	n-glycans	25-34	major royal jelly protein 1	Apis mellifera	47-52
31393126-10	2019	The diversity of N-glycans attached to each single glycosylation site of these glycoproteins confirmed that MRJP1 and MRJP2 heterogeneity was mostly associated with their glycoform populations.	n-glycans	17-26	major royal jelly protein 1	Apis mellifera	108-113
30235865-8	2018	We found that the expression of the mrjps (mrjp1-3) that were finally secreted in large amounts into the food jelly, in particular, were down regulated by 20-hydroxyecdysone treatment, with mrjp3 showing the highest repression value.	Ecdysterone	155-173	major royal jelly protein 1	Apis mellifera	43-48
14659076-4	2003	The open-reading frame of the MRJP1 homologue (AcMRJP1) was 1299 nucleotides that encoded 433 deduced amino acids with three predicted N-linked glycosylation sites.	Nitrogen	135-136	major royal jelly protein 1	Apis mellifera	30-35
30135511-4	2018	Herein, we identify and report a 16-molecule architecture of native MRJP1 oligomer containing four MRJP1, four apisimin, and eight unanticipated 24-methylenecholesterol molecules at 2.65 A resolution.	24-methylenecholesterol	145-168	major royal jelly protein 1	Apis mellifera	68-73
30135511-5	2018	MRJP1 has a unique six-bladed beta-propeller fold with three disulfide bonds, and it interacts with apisimin mainly by hydrophobic interaction.	Disulfides	61-70	major royal jelly protein 1	Apis mellifera	0-5
30135511-6	2018	Every four 24-methylenecholesterol molecules are packaged by two MRJP1 and two apisimin molecules.	methylenecholesterol	14-34	major royal jelly protein 1	Apis mellifera	65-70
28252287-8	2017	Hydrogen/deuterium exchange MS reveals that MRJP1 within these complexes is extensively disordered in the range of residues 20-265.	Hydrogen	0-8	major royal jelly protein 1	Apis mellifera	44-49
28252287-8	2017	Hydrogen/deuterium exchange MS reveals that MRJP1 within these complexes is extensively disordered in the range of residues 20-265.	Deuterium	9-18	major royal jelly protein 1	Apis mellifera	44-49
22366273-7	2012	We further showed that (i) the treatment of purified defensin1 in solution containing high amount of MGO caused a time-dependent loss of its antibacterial activity and (ii) increasing MGO concentrations in a non-manuka honey were connected with a gradual increase in the molecular weight of MRJP1.	Pyruvaldehyde	101-104	major royal jelly protein 1	Apis mellifera	291-296
22366273-7	2012	We further showed that (i) the treatment of purified defensin1 in solution containing high amount of MGO caused a time-dependent loss of its antibacterial activity and (ii) increasing MGO concentrations in a non-manuka honey were connected with a gradual increase in the molecular weight of MRJP1.	Pyruvaldehyde	184-187	major royal jelly protein 1	Apis mellifera	291-296
22366273-8	2012	Obtained results demonstrate that MGO abrogates the antibacterial activity of defensin1 and modifies MRJP1 in manuka honey.	Pyruvaldehyde	34-37	major royal jelly protein 1	Apis mellifera	101-106