PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
14699117-0	2004	Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2.	Histidine	12-21	reticulon 2	Homo sapiens	103-107
15010217-9	2004	Phosphate residues generated by the NTPase activity are believed to be transferred from NSP2 to NSP5, leading to the hyperphosphorylation of the latter protein.	Phosphates	0-9	reticulon 2	Homo sapiens	88-92
15010217-10	2004	It is suspected that the transfer of the phosphate group to NSP5 allows NSP2 to return to its noncondensed state and, thus, to accept another NTP molecule.	Phosphates	41-50	reticulon 2	Homo sapiens	72-76
15010217-10	2004	It is suspected that the transfer of the phosphate group to NSP5 allows NSP2 to return to its noncondensed state and, thus, to accept another NTP molecule.	ntp	142-145	reticulon 2	Homo sapiens	72-76
14699117-3	2004	Comparison of x-ray structures has revealed significant structural homology between NSP2 and the histidine triad (HIT) family of nucleotidyl hydrolases, which in turn has suggested the location of the active site for NTP hydrolysis in NSP2.	Histidine	97-106	reticulon 2	Homo sapiens	84-88
14699117-3	2004	Comparison of x-ray structures has revealed significant structural homology between NSP2 and the histidine triad (HIT) family of nucleotidyl hydrolases, which in turn has suggested the location of the active site for NTP hydrolysis in NSP2.	Histidine	97-106	reticulon 2	Homo sapiens	235-239
14699117-3	2004	Comparison of x-ray structures has revealed significant structural homology between NSP2 and the histidine triad (HIT) family of nucleotidyl hydrolases, which in turn has suggested the location of the active site for NTP hydrolysis in NSP2.	ntp	217-220	reticulon 2	Homo sapiens	84-88
14699117-3	2004	Comparison of x-ray structures has revealed significant structural homology between NSP2 and the histidine triad (HIT) family of nucleotidyl hydrolases, which in turn has suggested the location of the active site for NTP hydrolysis in NSP2.	ntp	217-220	reticulon 2	Homo sapiens	235-239
14699117-4	2004	Consistent with the structural predictions, we show here using site-specific mutagenesis and ATP docking simulations that the active site for NTP hydrolysis is localized to residues within a 25-A-deep cleft between the C- and N-terminal domains of the NSP2 monomer.	Adenosine Triphosphate	93-96	reticulon 2	Homo sapiens	252-256
14699117-4	2004	Consistent with the structural predictions, we show here using site-specific mutagenesis and ATP docking simulations that the active site for NTP hydrolysis is localized to residues within a 25-A-deep cleft between the C- and N-terminal domains of the NSP2 monomer.	ntp	142-145	reticulon 2	Homo sapiens	252-256
11162836-2	2001	NS2 shares these features with the nonstructural protein, NSP2, of rotavirus, which like BTV is a member of the family Reoviridae.	CHEMBL3972792	89-92	reticulon 2	Homo sapiens	58-62
12951038-6	2003	Further analysis revealed that NSP2 interfered with the ability of the open core proteins, GTP, and viral mRNA to form the initiation complex for (-) strand synthesis.	Guanosine Triphosphate	91-94	reticulon 2	Homo sapiens	31-35
12072508-6	2002	However, exposure to Mg(2+) and the nonpermissive temperature caused disruption of the tsE octamers and yielded the formation of polydisperse NSP2 aggregates, events not observed with wt octamers.	Magnesium	21-23	reticulon 2	Homo sapiens	142-146
11121414-4	2001	We found that NSP2 exists as an octamer, which is functional in the binding of RNA and ADP.	Adenosine Diphosphate	87-90	reticulon 2	Homo sapiens	14-18
11121414-8	2001	The secondary structure of NSP2 showed a high fraction of beta-sheet, with small changes induced by magnesium that were reversed in the presence of RNA.	Magnesium	100-109	reticulon 2	Homo sapiens	27-31
11162836-10	2001	Although the nature of the enzymatic activities differs significantly, the fact that both NS2 and NSP2 hydrolyze NTPs, undergo phosphorylation, bind RNA, and assemble into multimers consisting of 6 +/- 2 subunits suggests that they are functional homologs.	ntps	113-117	reticulon 2	Homo sapiens	98-102
10559306-2	1999	To better understand the structure and function of the protein, C-terminally His-tagged NSP2 was expressed in bacteria and purified to homogeneity.	Histidine	77-80	reticulon 2	Homo sapiens	88-92
10881675-4	2000	Compared to Nsp2 of the North American strains and the European strain, the predicted Nsp2 of strain SP contains 36 and 155 amino acid insertions, respectively, near the C-terminus, in addition to several highly variable regions.	TFF2 protein, human	101-103	reticulon 2	Homo sapiens	12-16
10881675-4	2000	Compared to Nsp2 of the North American strains and the European strain, the predicted Nsp2 of strain SP contains 36 and 155 amino acid insertions, respectively, near the C-terminus, in addition to several highly variable regions.	TFF2 protein, human	101-103	reticulon 2	Homo sapiens	86-90
10748213-5	2000	Using a novel RNA triphosphatase assay, we show here that nonstructural protein Nsp2 (799 amino acids) of Semliki Forest virus specifically cleaves the gamma,beta-triphosphate bond at the 5" end of RNA.	beta-triphosphate	158-175	reticulon 2	Homo sapiens	80-84
10217401-3	1999	Here we expressed polyhistidine-tagged nsP2 in Escherichia coli, purified it by metal-affinity chromatography, and used it in RNA helicase assays.	polyhistidine	18-31	reticulon 2	Homo sapiens	39-43
10217401-3	1999	Here we expressed polyhistidine-tagged nsP2 in Escherichia coli, purified it by metal-affinity chromatography, and used it in RNA helicase assays.	Metals	80-85	reticulon 2	Homo sapiens	39-43
10217401-5	1999	Unwinding of alpha-32P-labelled partially double-stranded RNA required nsP2, Mg2+ and NTPs.	alpha-32p	13-22	reticulon 2	Homo sapiens	71-75
9693037-11	1998	The amino-terminal regions of the RTN2-A and RTN2-B proteins are rich in negatively charged residues and in proline and serine residues and contain multiple potential phosphorylation sites.	Serine	120-126	reticulon 2	Homo sapiens	45-49
10073689-6	1999	Nsp2, thought to have a species-specific function, showed the greatest divergence, sharing only 32% amino acid identity with LV and containing 120 additional amino acids in the central region.	Leucovorin	125-127	reticulon 2	Homo sapiens	0-4
9693037-11	1998	The amino-terminal regions of the RTN2-A and RTN2-B proteins are rich in negatively charged residues and in proline and serine residues and contain multiple potential phosphorylation sites.	Proline	108-115	reticulon 2	Homo sapiens	34-38
9693037-11	1998	The amino-terminal regions of the RTN2-A and RTN2-B proteins are rich in negatively charged residues and in proline and serine residues and contain multiple potential phosphorylation sites.	Proline	108-115	reticulon 2	Homo sapiens	45-49
9693037-11	1998	The amino-terminal regions of the RTN2-A and RTN2-B proteins are rich in negatively charged residues and in proline and serine residues and contain multiple potential phosphorylation sites.	Serine	120-126	reticulon 2	Homo sapiens	34-38
1448929-5	1992	These results suggest that nsP2 is a papain-like proteinase whose catalytic dyad is composed of Cys-481 and His-558.	Cysteine	96-99	reticulon 2	Homo sapiens	27-31
9018056-2	1997	nsP2, used for immunization, was expressed as a histidine fusion protein in Escherichia coli and purified by metal affinity chromatography.	Metals	109-114	reticulon 2	Homo sapiens	0-4
8610462-5	1996	Substitution of the second arginine in its nuclear localization signal (P648RRRV) with aspartic acid rendered nsP2 totally cytoplasmic.	Arginine	27-35	reticulon 2	Homo sapiens	110-114
8610462-5	1996	Substitution of the second arginine in its nuclear localization signal (P648RRRV) with aspartic acid rendered nsP2 totally cytoplasmic.	Aspartic Acid	87-100	reticulon 2	Homo sapiens	110-114
8057461-8	1994	Radiolabeled ribonucleoside triphosphates could be cross-linked to both the full-length and the carboxy-terminally truncated nsP2 protein, and both polypeptides had RNA-binding capacity.	ribonucleoside triphosphates	13-41	reticulon 2	Homo sapiens	125-129
8057461-9	1994	We also expressed and purified an nsP2 variant which had a single amino acid substitution in the nucleotide-binding motif (Lys-192-->Asn).	Lysine	123-126	reticulon 2	Homo sapiens	34-38
8057461-9	1994	We also expressed and purified an nsP2 variant which had a single amino acid substitution in the nucleotide-binding motif (Lys-192-->Asn).	Asparagine	136-139	reticulon 2	Homo sapiens	34-38
8032268-2	1994	The pentapeptide sequence P 648R RRV is an essential part of the nuclear localization signal (NLS) of nsP2, the middle arginine being the most critical residue for nuclear targeting.	Arginine	119-127	reticulon 2	Homo sapiens	102-106
1448929-5	1992	These results suggest that nsP2 is a papain-like proteinase whose catalytic dyad is composed of Cys-481 and His-558.	Histidine	108-111	reticulon 2	Homo sapiens	27-31
1448929-6	1992	Since an asparagine residue has been implicated in the active site of papain, we changed the four conserved asparagine residues in the C-terminal half of nsP2 and found that all could be substituted without total loss of activity.	Asparagine	9-19	reticulon 2	Homo sapiens	154-158
1448929-6	1992	Since an asparagine residue has been implicated in the active site of papain, we changed the four conserved asparagine residues in the C-terminal half of nsP2 and found that all could be substituted without total loss of activity.	Asparagine	108-118	reticulon 2	Homo sapiens	154-158
2141206-2	1990	The penultimate Gly in nsP1 or nsP2 or both was substituted by Ala, Val, or Glu, and processing was studied in vitro.	Glycine	16-19	reticulon 2	Homo sapiens	31-35
1386484-6	1992	When the three arginines were substituted with aspartic acids, the mutant nsP2 was localized in the cytoplasm.	Arginine	15-24	reticulon 2	Homo sapiens	74-78
1386484-6	1992	When the three arginines were substituted with aspartic acids, the mutant nsP2 was localized in the cytoplasm.	Aspartic Acid	47-61	reticulon 2	Homo sapiens	74-78
2525839-4	1989	The nsP1-2 and nsP2-3 cleavage sites are alanyl-alanine and both were susceptible to proteolysis in vitro only after all of nsp1 and nsP2 and 157 amino acids of nsP3 were translated.	alanylalanine	41-55	reticulon 2	Homo sapiens	15-19
2139138-3	1990	Subfractionation of [35S]methionine-labeled Semliki Forest virus-infected cells showed that 80 to 90% of the nuclear nsP2 was associated with the nuclear matrix.	Sulfur-35	21-24	reticulon 2	Homo sapiens	117-121
2139138-3	1990	Subfractionation of [35S]methionine-labeled Semliki Forest virus-infected cells showed that 80 to 90% of the nuclear nsP2 was associated with the nuclear matrix.	Methionine	25-35	reticulon 2	Homo sapiens	117-121
2521674-11	1989	The second change, a substitution of Gln by Arg in ts118 at residue 93 in nsP4, had little apparent phenotype on its own, but in combination with the change in nsP2 led to a ts phenotype.	Arginine	44-47	reticulon 2	Homo sapiens	160-164
2521674-13	1989	In addition, the result with ts118 suggests that nsP2 and nsP4 may interact with each other in a complex.	ts118	29-34	reticulon 2	Homo sapiens	49-53
31802759-3	2019	The single-crystal X-ray structure analysis revealed an angle of 13.36 (8)  between the planes of the rings, as well as molecules linked by Nsp2-H...N hydrogen bonds forming dimers along the crystal.	Hydrogen	151-159	reticulon 2	Homo sapiens	140-144
31802759-5	2019	The existence of Nsp2-H...N hydrogen bonds in the crystal was confirmed spectroscopically by the IR peaks from the N-H stretching vibration shifting to lower wavenumbers in the solid state relative to those in the gas phase.	Hydrogen	28-36	reticulon 2	Homo sapiens	17-21
31802759-5	2019	The existence of Nsp2-H...N hydrogen bonds in the crystal was confirmed spectroscopically by the IR peaks from the N-H stretching vibration shifting to lower wavenumbers in the solid state relative to those in the gas phase.	Hydrogen	115-118	reticulon 2	Homo sapiens	17-21
31443266-8	2019	Our extensive docking and molecular dynamics simulations studies leads to two best interacting compounds, Ribostamycin sulfate and E-64, with utmost stable complexes at active site of nsp2 protease.	Ribostamycin sulfate	106-126	reticulon 2	Homo sapiens	184-188
31561412-1	2019	The papain-like cysteine protease 2 (PLP2) within the N-terminus of the porcine reproductive and respiratory syndrome virus (PRRSV) nsp2 replicase protein specifies a deubiquitinating enzyme (DUB), but its biochemical properties and the role in infection have remained poorly defined.	Cysteine	16-24	reticulon 2	Homo sapiens	132-136
31561412-1	2019	The papain-like cysteine protease 2 (PLP2) within the N-terminus of the porcine reproductive and respiratory syndrome virus (PRRSV) nsp2 replicase protein specifies a deubiquitinating enzyme (DUB), but its biochemical properties and the role in infection have remained poorly defined.	Nitrogen	54-55	reticulon 2	Homo sapiens	132-136
31531426-1	2019	A photo- and dioxygen-enabled intermolecular radical Csp3-Nsp2 cross-coupling between guanidines and perfluoroalkyl iodides has been developed.	Oxygen	13-21	reticulon 2	Homo sapiens	58-62
31531426-1	2019	A photo- and dioxygen-enabled intermolecular radical Csp3-Nsp2 cross-coupling between guanidines and perfluoroalkyl iodides has been developed.	Guanidines	86-96	reticulon 2	Homo sapiens	58-62
31531426-1	2019	A photo- and dioxygen-enabled intermolecular radical Csp3-Nsp2 cross-coupling between guanidines and perfluoroalkyl iodides has been developed.	perfluoroalkyl iodides	101-123	reticulon 2	Homo sapiens	58-62
31531426-2	2019	N2-Perfluoroalkacylguanidines, which are of biological importance, were obtained under mild conditions via Nsp2-perfluoroalkylation and subsequent hydrolysis.	n2-perfluoroalkacylguanidines	0-29	reticulon 2	Homo sapiens	107-111
31443266-8	2019	Our extensive docking and molecular dynamics simulations studies leads to two best interacting compounds, Ribostamycin sulfate and E-64, with utmost stable complexes at active site of nsp2 protease.	E 64	131-135	reticulon 2	Homo sapiens	184-188
29291232-7	2017	In addition, we show that MAb BR/PNsp2-2A20 recognizes a 20 amino acid peptide (707) GRFEFLPKMILETPPPHPCG (727) of Nsp2.	amino acid peptide	60-78	reticulon 2	Homo sapiens	34-38
31030842-3	2019	The complete genomes of the two isolates were then determined, and sequence alignment revealed that GZgy17 had the same discontinuous 30-amino acid (aa) deletion in NSP2 as JXA1, while SCya18 contained the discontinuous 131-aa deletion in NSP2 identical to that of NADC30, when compared to the strain VR-2332.	gzgy17	100-106	reticulon 2	Homo sapiens	165-169
29348627-7	2018	In silico analysis showed close (<=1.7 A) polar interaction (hydrogen bond) between Glu4, Arg7, 96, 225 of nsP2 with Lys256, 206, Val367 and Phe312 of nsP1 respectively.	Hydrogen	64-72	reticulon 2	Homo sapiens	110-114
27923923-5	2016	Our approach involved ectopic expression of arterivirus nonstructural proteins nsp2 and nsp3, which induce DMV formation in the absence of other viral triggers of the interferon response, such as replicating viral RNA.	(2R,3R)-2,3-dihydroxy-3-methylpentanoic acid	107-110	reticulon 2	Homo sapiens	79-83
28713014-6	2017	Meanwhile, we identified two recombination breakpoints located in the nt1737 and nt3506 of nsp2-coding region, which had higher nucleotide homology with NADC30 and NADC30-like CHsx1401.	nadc30	153-159	reticulon 2	Homo sapiens	91-95
28713014-6	2017	Meanwhile, we identified two recombination breakpoints located in the nt1737 and nt3506 of nsp2-coding region, which had higher nucleotide homology with NADC30 and NADC30-like CHsx1401.	nadc30	164-170	reticulon 2	Homo sapiens	91-95
24959709-5	2014	Immunoprecipitation analysis showed that nsP2 interacts with Hsp90 during infection; however this interaction is reduced in the presence of GA.	geldanamycin	140-142	reticulon 2	Homo sapiens	41-45
27845418-0	2016	Chikungunya virus infectivity, RNA replication and non-structural polyprotein processing depend on the nsP2 protease"s active site cysteine residue.	Cysteine	131-139	reticulon 2	Homo sapiens	103-107
27845418-6	2016	Third, substitution of Ser482 residue, recently reported to contribute to the protease activity of nsP2, with Ala has almost no negative effect on the protease activity of CHIKV nsP2.	Alanine	110-113	reticulon 2	Homo sapiens	99-103
25552719-6	2015	Introducing PG into recombinant nsP2 inhibited proteolytic cleavage of nsP1/nsP2 and nsP3/nsP4 sites, reduced GTPase and RNA helicase activities, and abolished RNA stimulation of GTPase activity.	pg	12-14	reticulon 2	Homo sapiens	76-80
26597768-0	2015	Chikungunya nsP2 protease is not a papain-like cysteine protease and the catalytic dyad cysteine is interchangeable with a proximal serine.	Serine	132-138	reticulon 2	Homo sapiens	12-16
26597768-4	2015	Classically the alphavirus nsP2 protease is thought to be papain-like with the enzyme reaction proceeding through a cysteine/histidine catalytic dyad.	Cysteine	116-124	reticulon 2	Homo sapiens	27-31
26597768-4	2015	Classically the alphavirus nsP2 protease is thought to be papain-like with the enzyme reaction proceeding through a cysteine/histidine catalytic dyad.	Histidine	125-134	reticulon 2	Homo sapiens	27-31
25552719-6	2015	Introducing PG into recombinant nsP2 inhibited proteolytic cleavage of nsP1/nsP2 and nsP3/nsP4 sites, reduced GTPase and RNA helicase activities, and abolished RNA stimulation of GTPase activity.	pg	12-14	reticulon 2	Homo sapiens	32-36
23193175-5	2013	When coexpressed with NSP2, an NSP5 mutant devoid of the iron-sulfur cluster still forms viroplasm-like structures.	Iron	57-61	reticulon 2	Homo sapiens	22-26
23926336-7	2013	As revealed by protein/protein interaction analysis, confocal immunofluorescence microscopy, and viroplasm-like structure formation analysis, thiazolides act by hindering the interaction between the nonstructural proteins NSP5 and NSP2.	thiazolides	142-153	reticulon 2	Homo sapiens	231-235
23193175-5	2013	When coexpressed with NSP2, an NSP5 mutant devoid of the iron-sulfur cluster still forms viroplasm-like structures.	Sulfur	62-68	reticulon 2	Homo sapiens	22-26
23115286-5	2013	We show that SUMO can be covalently conjugated to the viroplasm proteins VP1, VP2, NSP2, VP6, and NSP5.	sumo	13-17	reticulon 2	Homo sapiens	83-87
22811529-3	2012	In addition to sequence-independent single-stranded RNA-binding and helix-destabilizing activities, NSP2 exhibits monomer-associated nucleoside and 5" RNA triphosphatase (NTPase/RTPase) activities that are mediated by a conserved H225 residue within a narrow enzymatic cleft.	1-PHENYLPIPERAZINE	230-234	reticulon 2	Homo sapiens	100-104
22811529-6	2012	As the only rotavirus protein with 5" RTPase activity, NSP2 is implicated in the removal of the gamma-phosphate from the rotavirus (-)RNA.	gamma-phosphate	96-111	reticulon 2	Homo sapiens	55-59
22811529-7	2012	To understand how NSP2, despite its sequence-independent RNA-binding property, recognizes (-)RNA to hydrolyze the gamma-phosphate within the catalytic cleft, we determined a crystal structure of NSP2 in complex with the 5" consensus sequence of minus-strand rotavirus RNA.	gamma-phosphate	114-129	reticulon 2	Homo sapiens	18-22
22811529-7	2012	To understand how NSP2, despite its sequence-independent RNA-binding property, recognizes (-)RNA to hydrolyze the gamma-phosphate within the catalytic cleft, we determined a crystal structure of NSP2 in complex with the 5" consensus sequence of minus-strand rotavirus RNA.	gamma-phosphate	114-129	reticulon 2	Homo sapiens	195-199
22811529-8	2012	Our studies show that the 5" GG of the bound oligoribonucleotide interacts extensively with highly conserved residues in the NSP2 enzymatic cleft.	Oligoribonucleotides	45-64	reticulon 2	Homo sapiens	125-129
22514352-7	2012	This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation.	Sulfur	67-68	reticulon 2	Homo sapiens	17-21
22514352-7	2012	This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation.	S-Adenosylmethionine	69-87	reticulon 2	Homo sapiens	17-21
22514352-7	2012	This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation.	S-Adenosylmethionine	89-92	reticulon 2	Homo sapiens	17-21
21445710-9	2012	Using these pharmacophore features, we screened a large public library of compounds (Asinex, Maybridge, TOSLab, Binding Database) to find a potential ligand that could inhibit the nsP2 protein.	asinex	85-91	reticulon 2	Homo sapiens	180-184
22616823-5	2012	Levels of viral proteins VP2, VP6, and NSP2 in GRA treated cells were measured by immunoblot to determine if there was an effect of GRA treatment on the accumulation of viral protein.	18alpha-glycyrrhetinic acid	47-50	reticulon 2	Homo sapiens	39-43
21445710-9	2012	Using these pharmacophore features, we screened a large public library of compounds (Asinex, Maybridge, TOSLab, Binding Database) to find a potential ligand that could inhibit the nsP2 protein.	toslab	104-110	reticulon 2	Homo sapiens	180-184
21543324-7	2011	Nevertheless, the catalytic cysteine and histidine residues constitute an active site that is highly similar to these in papain-like and nsP2 proteases.	Cysteine	28-36	reticulon 2	Homo sapiens	137-141
21543324-7	2011	Nevertheless, the catalytic cysteine and histidine residues constitute an active site that is highly similar to these in papain-like and nsP2 proteases.	Histidine	41-50	reticulon 2	Homo sapiens	137-141
20668084-1	2010	The nsp2 replicase protein of porcine reproductive and respiratory syndrome virus (PRRSV) was recently demonstrated to be processed from its precursor by the PL2 protease at or near the G(1196) G(1197) dipeptide in transfected CHO cells.	Dipeptides	202-211	reticulon 2	Homo sapiens	4-8
20007278-7	2010	Biochemical analyses indicated that the nsp2 protein is associated with the cytoplasmic side of the DMVs.	dmvs	100-104	reticulon 2	Homo sapiens	40-44
20483643-3	2010	The catalytic mechanism of the nsP2 protease appears similar to the papain-like cysteine proteases, with the conserved catalytic dyad forming a thiolate-imidazolium ion pair in the nsP2-activated state.	thiolate	144-152	reticulon 2	Homo sapiens	31-35
20483643-3	2010	The catalytic mechanism of the nsP2 protease appears similar to the papain-like cysteine proteases, with the conserved catalytic dyad forming a thiolate-imidazolium ion pair in the nsP2-activated state.	thiolate	144-152	reticulon 2	Homo sapiens	181-185
20483643-3	2010	The catalytic mechanism of the nsP2 protease appears similar to the papain-like cysteine proteases, with the conserved catalytic dyad forming a thiolate-imidazolium ion pair in the nsP2-activated state.	imidazolium	153-164	reticulon 2	Homo sapiens	31-35
20483643-3	2010	The catalytic mechanism of the nsP2 protease appears similar to the papain-like cysteine proteases, with the conserved catalytic dyad forming a thiolate-imidazolium ion pair in the nsP2-activated state.	imidazolium	153-164	reticulon 2	Homo sapiens	181-185
20483643-5	2010	Analysis of bimolecular complexes of Venezuelan equine encephalitis virus (VEEV) nsP2 protease with each of the nsP1234 cleavage sites identified protease residues His(510), Ser(511), His(546) and Lys(706) as critical for cleavage site recognition.	Histidine	164-167	reticulon 2	Homo sapiens	81-85
20483643-5	2010	Analysis of bimolecular complexes of Venezuelan equine encephalitis virus (VEEV) nsP2 protease with each of the nsP1234 cleavage sites identified protease residues His(510), Ser(511), His(546) and Lys(706) as critical for cleavage site recognition.	Serine	174-177	reticulon 2	Homo sapiens	81-85
20483643-5	2010	Analysis of bimolecular complexes of Venezuelan equine encephalitis virus (VEEV) nsP2 protease with each of the nsP1234 cleavage sites identified protease residues His(510), Ser(511), His(546) and Lys(706) as critical for cleavage site recognition.	Histidine	184-187	reticulon 2	Homo sapiens	81-85
20483643-5	2010	Analysis of bimolecular complexes of Venezuelan equine encephalitis virus (VEEV) nsP2 protease with each of the nsP1234 cleavage sites identified protease residues His(510), Ser(511), His(546) and Lys(706) as critical for cleavage site recognition.	Lysine	197-200	reticulon 2	Homo sapiens	81-85
18442838-3	2008	Interestingly, mutant P718T in replicase nsp2 subunit was able to replicate in only a small percentage of BHK cells, producing beta-gal-expressing colonies without selection.	beta-D-galactose	127-135	reticulon 2	Homo sapiens	41-45
19587037-6	2009	Introduction of targeted amino acid mutations in the protease domain confirmed the importance of the putative Cys(55)- His(124) catalytic motif for nsp2/3 proteolysis in vitro, as were three additional conserved cysteine residues (Cys(111), Cys(142), and Cys(147)).	Cysteine	110-113	reticulon 2	Homo sapiens	148-152
19587037-6	2009	Introduction of targeted amino acid mutations in the protease domain confirmed the importance of the putative Cys(55)- His(124) catalytic motif for nsp2/3 proteolysis in vitro, as were three additional conserved cysteine residues (Cys(111), Cys(142), and Cys(147)).	Histidine	119-122	reticulon 2	Homo sapiens	148-152
20112680-3	2009	The recombinant protein (Nsp2-N and Nsp2-C) were over expressed in E. coli BL21 and purified by Ni-NTA agarose affinity chromatogram and gel filtration.	ni-nta	96-102	reticulon 2	Homo sapiens	25-29
20112680-3	2009	The recombinant protein (Nsp2-N and Nsp2-C) were over expressed in E. coli BL21 and purified by Ni-NTA agarose affinity chromatogram and gel filtration.	Sepharose	103-110	reticulon 2	Homo sapiens	25-29
19428754-1	2009	The point mutations at residue 726 Pro in the nonstructural gene 2 (nsP2-726P) could make Sindbis virus (SINV) replicons lacking the structural protein-coding region less cytopathic and capable of persisting in some vertebrate cell lines.	Proline	35-38	reticulon 2	Homo sapiens	68-72
16873255-3	2006	NSP2 of the rotavirus group causing endemic infantile diarrhea (group A) was shown to self-assemble into large doughnut-shaped octamers with circumferential grooves and deep clefts containing nucleotide-binding histidine triad (HIT)-like motifs.	Histidine	211-220	reticulon 2	Homo sapiens	0-4
18411274-9	2008	Replicase subunits directly involved in viral RNA synthesis (nsp9 and nsp10) or DMV formation (nsp2 and nsp3) exclusively cosedimented with the active RTC.	(2R,3R)-2,3-dihydroxy-3-methylpentanoic acid	80-83	reticulon 2	Homo sapiens	95-99
17825341-6	2007	Through its NDP kinase activity, the NSP2 octamer may support NSP5 phosphorylation by creating a constant source of ATP molecules for the autokinase activity of NSP5 and for cellular kinases associated with NSP5.	Adenosine Triphosphate	116-119	reticulon 2	Homo sapiens	37-41
17652399-8	2007	Leptomycin B treatment resulted in nuclear accumulation of nsP2, demonstrating that nuclear export of nsP2 is mediated via the CRM1 nuclear export pathway.	leptomycin B	0-12	reticulon 2	Homo sapiens	59-63
17652399-8	2007	Leptomycin B treatment resulted in nuclear accumulation of nsP2, demonstrating that nuclear export of nsP2 is mediated via the CRM1 nuclear export pathway.	leptomycin B	0-12	reticulon 2	Homo sapiens	102-106
16934294-0	2006	Histidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activities.	Histidine	0-9	reticulon 2	Homo sapiens	44-48
16934294-7	2006	Our results show that NSP2 hydrolyzes the gammaP from RNAs and NTPs through Mg(2+)-dependent activities that proceed with similar reaction velocities, that require the catalytic His225 residue, and that produce a phosphorylated intermediate.	magnesium ion	76-82	reticulon 2	Homo sapiens	22-26
17804496-5	2007	These studies showed that nucleotides bind inside a cleft between the two domains of NSP2 in a region that exhibits structural similarity to ubiquitous cellular HIT (histidine triad) proteins.	Histidine	166-175	reticulon 2	Homo sapiens	85-89
17804496-9	2007	Bioluminometric assay showed that NSP2 exhibits an NDP kinase-like activity that transfers the bound phosphate to NDPs.	Phosphates	101-110	reticulon 2	Homo sapiens	34-38
17804496-9	2007	Bioluminometric assay showed that NSP2 exhibits an NDP kinase-like activity that transfers the bound phosphate to NDPs.	N,N-di-n-propylserotonin	114-118	reticulon 2	Homo sapiens	34-38
15899130-6	2005	Then the recombinant eukaryotic expression vector pCI-neo/nsp2 was transfected into COS-7 cells using lipofectin reagent to express the nsp2 protein.	1,2-dielaidoylphosphatidylethanolamine	102-112	reticulon 2	Homo sapiens	136-140
15899130-7	2005	The expressive protein of SARS-CoV nsp2 was analyzed by 7% sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE).	Sodium Dodecyl Sulfate	59-80	reticulon 2	Homo sapiens	35-39
15899130-7	2005	The expressive protein of SARS-CoV nsp2 was analyzed by 7% sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE).	polyacrylamide	81-95	reticulon 2	Homo sapiens	35-39
15899130-7	2005	The expressive protein of SARS-CoV nsp2 was analyzed by 7% sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE).	Sodium Dodecyl Sulfate	117-120	reticulon 2	Homo sapiens	35-39
15899130-12	2005	The eukaryotic expression vector (pCI-neo/nsp2) was constructed and expressed the protein in COS-7 cells successfully.	carbonyl sulfide	93-96	reticulon 2	Homo sapiens	42-46