PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
23197838-4	2012	Single or multiple protein domains up to ~70 kDa are stably enclosed by stabilizing the ATP-hydrolysis transition state of TRiC.	Adenosine Triphosphate	88-91	MARVEL domain containing 2	Homo sapiens	123-127
23041314-0	2012	A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.	Adenosine Triphosphate	14-17	MARVEL domain containing 2	Homo sapiens	89-93
22616716-10	2012	We studied the ATP binding stoichiometry of the multi-subunit chaperonin enzyme TRiC in the ABEL trap by counting the number of hydrolyzed Cy3-ATP using stepwise photobleaching.	Adenosine Triphosphate	15-18	MARVEL domain containing 2	Homo sapiens	80-84
22616716-10	2012	We studied the ATP binding stoichiometry of the multi-subunit chaperonin enzyme TRiC in the ABEL trap by counting the number of hydrolyzed Cy3-ATP using stepwise photobleaching.	3'(2')-O-(N-(2-((2-((1-ethyl-3,3-dimethyl-5-sulfoindol-2-yl)prop-2-enylidene)-3,3-dimethyl-5-sulfoindol-1-yl)amino)ethyl)carbamoyl)-adenosine triphosphate	139-146	MARVEL domain containing 2	Homo sapiens	80-84
23041314-1	2012	The eukaryotic chaperonin TRiC/CCT uses ATP cycling to fold many essential proteins that other chaperones cannot fold.	Adenosine Triphosphate	40-43	MARVEL domain containing 2	Homo sapiens	26-30
23041314-6	2012	The conserved nucleotide-binding hierarchy among TRiC subunits is evolutionarily modulated through differential nucleoside contacts.	Nucleosides	112-122	MARVEL domain containing 2	Homo sapiens	49-53
23041314-8	2012	This unusual mode of ATP utilization likely serves to orchestrate a directional mechanism underlying TRiC/CCT"s unique ability to fold complex eukaryotic proteins.	Adenosine Triphosphate	21-24	MARVEL domain containing 2	Homo sapiens	101-105
22045336-6	2012	We identify and structurally characterize an one-ring closed intermediate induced by ATP hydrolysis wherein the closed TRiC ring exhibits an observable chamber expansion.	Adenosine Triphosphate	85-88	MARVEL domain containing 2	Homo sapiens	119-123
22308438-6	2012	We cross-linked TRiC under native conditions with a cross-linker that is primarily reactive toward exposed lysine side chains that are spatially close in the context of the particle.	Lysine	107-113	MARVEL domain containing 2	Homo sapiens	16-20
22503819-1	2012	TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate folding of approximately 10% of the eukaryotic proteome.	Adenosine Triphosphate	66-69	MARVEL domain containing 2	Homo sapiens	0-4
22503819-5	2012	In vivo disulfide mapping provided additional validation for the crosslinking-derived arrangement as the definitive TRiC topology.	Disulfides	8-17	MARVEL domain containing 2	Homo sapiens	116-120
18775504-4	2009	Using this approach we identified that SK1 interacts with subunit 7 (eta) of cytosolic chaperonin CCT (chaperonin containing t-complex polypeptide, also called TRiC for TCP-1 ring complex), a hexadecameric chaperonin that binds unfolded polypeptides and mediates their folding and release in an ATP-dependent manner.	Adenosine Triphosphate	295-298	MARVEL domain containing 2	Homo sapiens	160-164
21995946-1	2011	The cytosolic chaperonin TRiC was isolated from ovine testes using ultracentrifugation and heparin-Sepharose chromatography.	Heparin	91-98	MARVEL domain containing 2	Homo sapiens	25-29
21995946-1	2011	The cytosolic chaperonin TRiC was isolated from ovine testes using ultracentrifugation and heparin-Sepharose chromatography.	Sepharose	99-108	MARVEL domain containing 2	Homo sapiens	25-29
21995946-6	2011	The chaperonin TRiC was shown to assist an ATP-dependent refolding of recombinant forms of sperm-specific glyceraldehyde-3-phosphate dehydrogenase, an enzyme that is expressed only in precursor cells of the sperms in the seminiferous tubules of the testes.	Adenosine Triphosphate	43-46	MARVEL domain containing 2	Homo sapiens	15-19
21995946-7	2011	In contrast, TRiC did not influence the refolding of muscle isoform of glyceraldehyde-3-phosphate dehydrogenase and assisted the refolding of muscle lactate dehydrogenase by an ATP-independent mechanism.	Adenosine Triphosphate	177-180	MARVEL domain containing 2	Homo sapiens	13-17
20981710-10	2011	The ability of Mm-Cpn to bind and refold a human beta-sheet protein suggests that Mm-Cpn may be useful as a simplified model for the substrate recognition mechanism of TRiC/CCT.	mm-cpn	15-21	MARVEL domain containing 2	Homo sapiens	168-172
20981710-10	2011	The ability of Mm-Cpn to bind and refold a human beta-sheet protein suggests that Mm-Cpn may be useful as a simplified model for the substrate recognition mechanism of TRiC/CCT.	mm-cpn	82-88	MARVEL domain containing 2	Homo sapiens	168-172
20533305-3	2010	TRIC expression and the barrier function were moderated by treatment with the JNK activator anisomycin, and suppressed not only by inhibitors of JNK and PKC but also by siRNAs of TRIC.	Anisomycin	92-102	MARVEL domain containing 2	Homo sapiens	0-4
20533305-4	2010	TRIC expression was induced by treatment with the PKC activator TPA and proinflammatory cytokines IL-1beta, TNFalpha, and IL-1alpha, whereas the changes were inhibited by a JNK inhibitor.	Tetradecanoylphorbol Acetate	64-67	MARVEL domain containing 2	Homo sapiens	0-4
19915590-4	2009	Unexpectedly, TRiC does not physically block the polyQ tract itself, but rather sequesters a short Htt sequence element, N-terminal to the polyQ tract, that promotes the amyloidogenic conformation.	polyglutamine	49-54	MARVEL domain containing 2	Homo sapiens	14-18
19915590-4	2009	Unexpectedly, TRiC does not physically block the polyQ tract itself, but rather sequesters a short Htt sequence element, N-terminal to the polyQ tract, that promotes the amyloidogenic conformation.	polyglutamine	139-144	MARVEL domain containing 2	Homo sapiens	14-18
20822540-8	2010	Moreover, we showed that pCPT-cAMP and 8-Br-cAMP/Na induced expression and membrane translocation of tricellulin.	8-Cpt-camp	25-34	MARVEL domain containing 2	Homo sapiens	101-112
20822540-8	2010	Moreover, we showed that pCPT-cAMP and 8-Br-cAMP/Na induced expression and membrane translocation of tricellulin.	8-Bromo Cyclic Adenosine Monophosphate	39-48	MARVEL domain containing 2	Homo sapiens	101-112
18775504-5	2009	Further analysis of the SK1-CCTeta interaction demonstrated that other CCT/TRiC subunits also associated with SK1 in HEK293T cell lysates in an ATP-sensitive manner, suggesting that the intact, functional, multimeric CCT/TRiC complex associated with SK1.	Adenosine Triphosphate	144-147	MARVEL domain containing 2	Homo sapiens	75-79
18775504-5	2009	Further analysis of the SK1-CCTeta interaction demonstrated that other CCT/TRiC subunits also associated with SK1 in HEK293T cell lysates in an ATP-sensitive manner, suggesting that the intact, functional, multimeric CCT/TRiC complex associated with SK1.	Adenosine Triphosphate	144-147	MARVEL domain containing 2	Homo sapiens	221-225
17018290-1	2006	The ring-shaped hetero-oligomeric chaperonin TRiC/CCT uses ATP to fold a diverse subset of eukaryotic proteins.	Adenosine Triphosphate	59-62	MARVEL domain containing 2	Homo sapiens	45-49
17939680-7	2007	The results suggest that the actin structure is rearranged by a "binding-induced expansion" mechanism in both TRiC and GroEL, but that binding to TRiC, in addition, causes a large and specific separation of two subdomains in the beta-actin molecule, leading to a distinct expansion of its ATP-binding cleft.	Adenosine Triphosphate	289-292	MARVEL domain containing 2	Homo sapiens	146-150
17939680-8	2007	Moreover, the binding of ATP and GroES has less effect on the GroEL-bound beta-actin molecule than the ATP binding to TRiC, where it leads to a major compaction of the beta-actin molecule.	Adenosine Triphosphate	103-106	MARVEL domain containing 2	Homo sapiens	118-122
17417821-4	2007	Using fluorescence resonance energy transfer (FRET) measurements on four distinct doubly fluorescein-labeled variants of actin, we have obtained a fairly detailed map of the structural rearrangements that occur during the TRiC-actin interaction.	Fluorescein	89-100	MARVEL domain containing 2	Homo sapiens	222-226
17417821-6	2007	The target is stretched as a consequence of binding to TRiC and further rearranged in a second step as a consequence of ATP binding; i.e., the mechanism of chaperonins is conserved during evolution.	Adenosine Triphosphate	120-123	MARVEL domain containing 2	Homo sapiens	55-59
12732144-5	2003	We show that unlike GroEL, TRiC does not close its lid upon nucleotide binding, but instead responds to the trigonal-bipyramidal transition state of ATP hydrolysis.	Adenosine Triphosphate	149-152	MARVEL domain containing 2	Homo sapiens	27-31
16702223-9	2006	We conclude that the chaperonin CCT/TRiC complex binds to and folds Gbeta subunits and that CCT/TRiC mediates Gbetagamma dimer formation by an ATP-dependent reaction.	Adenosine Triphosphate	143-146	MARVEL domain containing 2	Homo sapiens	36-40
16702223-9	2006	We conclude that the chaperonin CCT/TRiC complex binds to and folds Gbeta subunits and that CCT/TRiC mediates Gbetagamma dimer formation by an ATP-dependent reaction.	Adenosine Triphosphate	143-146	MARVEL domain containing 2	Homo sapiens	96-100
34800541-8	2021	The mislocalization of tricellulin at tricellular contact areas was confirmed in MECs treated with IL-1beta or anisomycin.	Anisomycin	111-121	MARVEL domain containing 2	Homo sapiens	23-34
33803263-0	2021	Identification of Decrease in TRiC Proteins as Novel Targets of Alpha-Amanitin-Derived Hepatotoxicity by Comparative Proteomic Analysis In Vitro.	Alpha-Amanitin	64-78	MARVEL domain containing 2	Homo sapiens	30-34
4624816-0	1972	Primary isolation of TRIC organisms in HeLa 229 cells treated with DEAE-dextran.	DEAE-Dextran	67-79	MARVEL domain containing 2	Homo sapiens	21-25
34360593-2	2021	Recently, we showed that downregulated tricellulin, a protein of the tricellular tight junction (tTJ, the site where three epithelial cells meet), increased transepithelial water flux.	Water	173-178	MARVEL domain containing 2	Homo sapiens	39-50
34158536-1	2021	The eukaryotic chaperonin TRiC/CCT is a large ATP-dependent complex essential for cellular protein folding.	Adenosine Triphosphate	46-49	MARVEL domain containing 2	Homo sapiens	26-30
34190393-5	2021	We show that TRiC subunits modulate the unfolded protein response (UPR) and are required to maintain ATP levels in starved planarians.	Adenosine Triphosphate	101-104	MARVEL domain containing 2	Homo sapiens	13-17
322700-0	1977	Treatment of TRIC infection of the eye with rifampicin or chloramphenicol.	Rifampin	44-54	MARVEL domain containing 2	Homo sapiens	13-17
322700-0	1977	Treatment of TRIC infection of the eye with rifampicin or chloramphenicol.	Chloramphenicol	58-73	MARVEL domain containing 2	Homo sapiens	13-17
32866476-1	2021	The eukaryotic chaperonin TRiC/CCT plays a major role in assisting the folding of many proteins through an ATP-driven allosteric cycle.	Adenosine Triphosphate	107-110	MARVEL domain containing 2	Homo sapiens	26-30
5289718-1	1971	For isolating trachoma (TRIC) agent from conjunctival scrapings, both streptomycin and neomycin were effective in preventing bacterial contamination, but at high concentrations neomycin was rather more inhibitory to TRIC agent.	Streptomycin	70-82	MARVEL domain containing 2	Homo sapiens	24-28
5289718-1	1971	For isolating trachoma (TRIC) agent from conjunctival scrapings, both streptomycin and neomycin were effective in preventing bacterial contamination, but at high concentrations neomycin was rather more inhibitory to TRIC agent.	Neomycin	87-95	MARVEL domain containing 2	Homo sapiens	24-28
5289718-1	1971	For isolating trachoma (TRIC) agent from conjunctival scrapings, both streptomycin and neomycin were effective in preventing bacterial contamination, but at high concentrations neomycin was rather more inhibitory to TRIC agent.	Neomycin	177-185	MARVEL domain containing 2	Homo sapiens	24-28
5289718-5	1971	Two freshly isolated TRIC agents differed in their susceptibility to neomycin and streptomycin.	Neomycin	69-77	MARVEL domain containing 2	Homo sapiens	21-25
5289718-5	1971	Two freshly isolated TRIC agents differed in their susceptibility to neomycin and streptomycin.	Streptomycin	82-94	MARVEL domain containing 2	Homo sapiens	21-25
5289718-6	1971	Kanamycin and framycetin appeared to be less suitable than streptomycin for use in isolation of TRIC agent.	Kanamycin	0-9	MARVEL domain containing 2	Homo sapiens	96-100
5289718-6	1971	Kanamycin and framycetin appeared to be less suitable than streptomycin for use in isolation of TRIC agent.	Framycetin	14-24	MARVEL domain containing 2	Homo sapiens	96-100
5289718-6	1971	Kanamycin and framycetin appeared to be less suitable than streptomycin for use in isolation of TRIC agent.	Streptomycin	59-71	MARVEL domain containing 2	Homo sapiens	96-100
5289718-7	1971	In isolation studies, the possibility of inhibiting TRIC agent by high concentrations of antibotics, including streptomycin, should be borne in mind.	Streptomycin	111-123	MARVEL domain containing 2	Homo sapiens	52-56
33660567-7	2021	In 2.5D culture, treatment with PF-43 inhibited the decreases of angulin-1/LSR, TRIC, pJNK, pAMPK and pMAPK induced by HMGB1 and the inflammatory cytokines.	pf-43	32-37	MARVEL domain containing 2	Homo sapiens	80-84
33660567-8	2021	Treatment with PF-43 inhibited in part the induced phosphorylation of the serine of angulin-1/LSR and TRIC.	pf-43	15-20	MARVEL domain containing 2	Homo sapiens	102-106
5016295-0	1972	Differentiation of TRIC and LGV organisms based on enhancement of infectivity by DEAE-dextran in cell culture.	DEAE-Dextran	81-93	MARVEL domain containing 2	Homo sapiens	19-23
4960882-0	1967	Sensitivity and resistance of TRIC agents to penicillin, tetracycline and sulfa drugs.	Penicillins	45-55	MARVEL domain containing 2	Homo sapiens	30-34
4960882-0	1967	Sensitivity and resistance of TRIC agents to penicillin, tetracycline and sulfa drugs.	Tetracycline	57-69	MARVEL domain containing 2	Homo sapiens	30-34
4960882-0	1967	Sensitivity and resistance of TRIC agents to penicillin, tetracycline and sulfa drugs.	dimethyl trisulfide	74-79	MARVEL domain containing 2	Homo sapiens	30-34
5843954-0	1965	Growth of TRIC agents in various tissue growing on polythene.	Polyethylene	51-60	MARVEL domain containing 2	Homo sapiens	10-14
31581480-9	2019	Aspartate residues 487 and 441 were identified as caspase cleavage-sites in the C-terminal coiled-coil domain of human tricellulin.	Aspartic Acid	0-9	MARVEL domain containing 2	Homo sapiens	119-130
33441725-4	2021	Furthermore, we show that upon artemisinin exposure, genome-wide binding sites for PfGCN5 are increased and it is directly associated with the genes implicated in artemisinin resistance generation like BiP and TRiC chaperone.	artemisinin	31-42	MARVEL domain containing 2	Homo sapiens	210-214
33441725-4	2021	Furthermore, we show that upon artemisinin exposure, genome-wide binding sites for PfGCN5 are increased and it is directly associated with the genes implicated in artemisinin resistance generation like BiP and TRiC chaperone.	artemisinin	163-174	MARVEL domain containing 2	Homo sapiens	210-214
33100129-7	2020	While 3-oxo-C12 increased paracellular permeability and decreased occludin and tricellulin signal at bicellular and tricellular TJ, respectively, 3-oxo-C12:2 modified neither permeability nor TJ integrity.	3-oxo-c12	6-15	MARVEL domain containing 2	Homo sapiens	79-90
33100129-8	2020	Whereas 3-oxo-C12 potentiated the hyperpermeability induced by cytokines, 3-oxo-C12:2 attenuated their deleterious effects on occludin and tricellulin, and maintained their interaction with their partner ZO-1.	3-oxo-c12	74-83	MARVEL domain containing 2	Homo sapiens	139-150
33100129-9	2020	In addition, 3-oxo-C12:2 limited the cytokine-induced ubiquitination of occludin and tricellulin, suggesting that this AHL prevented their endocytosis.	3-oxo-c12	13-22	MARVEL domain containing 2	Homo sapiens	85-96
32268122-3	2020	We find that the NSPC chaperone network robustly maintains misfolded protein solubility and stress resilience through high levels of the ATP-dependent chaperonin TRiC/CCT.	Adenosine Triphosphate	137-140	MARVEL domain containing 2	Homo sapiens	162-166
32127489-0	2020	Plasmodium chaperonin TRiC/CCT identified as a target of the antihistamine clemastine using parallel chemoproteomic strategy.	Clemastine	75-85	MARVEL domain containing 2	Homo sapiens	22-26
32127489-2	2020	Here, we applied parallel chemoproteomic platforms to discover the mechanism of action of clemastine and identify that clemastine binds to the Plasmodium falciparum TCP-1 ring complex or chaperonin containing TCP-1 (TRiC/CCT), an essential heterooligomeric complex required for de novo cytoskeletal protein folding.	Clemastine	119-129	MARVEL domain containing 2	Homo sapiens	216-220
32127489-3	2020	Clemastine destabilized all eight P. falciparum TRiC subunits based on thermal proteome profiling (TPP).	Clemastine	0-10	MARVEL domain containing 2	Homo sapiens	48-52
32127489-3	2020	Clemastine destabilized all eight P. falciparum TRiC subunits based on thermal proteome profiling (TPP).	tpp	99-102	MARVEL domain containing 2	Homo sapiens	48-52
32127489-4	2020	Further analysis using stability of proteins from rates of oxidation (SPROX) revealed a clemastine-induced thermodynamic stabilization of the Plasmodium TRiC delta subunit, suggesting an interaction with this protein subunit.	sprox	70-75	MARVEL domain containing 2	Homo sapiens	153-157
32127489-4	2020	Further analysis using stability of proteins from rates of oxidation (SPROX) revealed a clemastine-induced thermodynamic stabilization of the Plasmodium TRiC delta subunit, suggesting an interaction with this protein subunit.	Clemastine	88-98	MARVEL domain containing 2	Homo sapiens	153-157
32127489-5	2020	We demonstrate that clemastine reduces levels of the major TRiC substrate tubulin in P. falciparum parasites.	Clemastine	20-30	MARVEL domain containing 2	Homo sapiens	59-63
32127489-7	2020	This clemastine-induced disruption of TRiC function is not observed in human host cells, demonstrating a species selectivity required for targeting an intracellular human pathogen.	Clemastine	5-15	MARVEL domain containing 2	Homo sapiens	38-42
31662022-4	2020	During cytokinesis induced by treatment with taxol, the epithelial barrier was maintained and the tricellular tight junction molecules LSR and tricellulin were concentrated at the flank of the acetylated tubulin-positive midbody and in gamma-tubulin-positive centrosomes with the dynein adaptor Hook2, whereas the other molecules were localized there as well.	Paclitaxel	45-50	MARVEL domain containing 2	Homo sapiens	143-154
31581480-9	2019	Aspartate residues 487 and 441 were identified as caspase cleavage-sites in the C-terminal coiled-coil domain of human tricellulin.	Carbon	80-81	MARVEL domain containing 2	Homo sapiens	119-130
31581480-11	2019	Deletion of the tricellulin C-terminal amino acids prevented binding to lipolysis-stimulated lipoprotein receptor (LSR)/angulin-1 and thus should impair specific localization of tricellulin to tTJs.	Carbon	28-29	MARVEL domain containing 2	Homo sapiens	16-27
31581480-11	2019	Deletion of the tricellulin C-terminal amino acids prevented binding to lipolysis-stimulated lipoprotein receptor (LSR)/angulin-1 and thus should impair specific localization of tricellulin to tTJs.	Carbon	28-29	MARVEL domain containing 2	Homo sapiens	178-189
28633193-8	2017	Circular dichroism spectroscopy and molecular modeling suggest that trictide adopts a beta-sheet structure, resulting in a peculiar interaction surface for its binding to tricellulin.	trictide	68-76	MARVEL domain containing 2	Homo sapiens	171-182
30550880-3	2019	In this work, we investigate this dependence for peptaibol trichogin GA IV (Tric) in the 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) model membrane in the range of peptide concentrations between 0.5 and 3.3 mol%.	1-palmitoyl-2-oleoylphosphatidylcholine	89-137	MARVEL domain containing 2	Homo sapiens	76-80
30550880-3	2019	In this work, we investigate this dependence for peptaibol trichogin GA IV (Tric) in the 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) model membrane in the range of peptide concentrations between 0.5 and 3.3 mol%.	1-palmitoyl-2-oleoylphosphatidylcholine	139-143	MARVEL domain containing 2	Homo sapiens	76-80
30550880-7	2019	As the 5-DSA molecules represent a model for the behavior of fatty acids participating in bacterial membrane homeostasis, such capturing action by Tric may represent an additional mechanism of its antibiotic activity.	Fatty Acids	61-72	MARVEL domain containing 2	Homo sapiens	147-151
31939165-4	2019	TRiC-mediated substrate folding is regulated through its ATP-driven conformational changes.	Adenosine Triphosphate	57-60	MARVEL domain containing 2	Homo sapiens	0-4
28633193-0	2017	Trictide, a tricellulin-derived peptide to overcome cellular barriers.	trictide	0-8	MARVEL domain containing 2	Homo sapiens	12-23
28633193-4	2017	The peptidomimetic trictide, a synthetic peptide derived from tricellulin ECL2, increases the passage of ions, as well as of small and larger molecules up to 10 kDa, between 16 and 30 h after application to human epithelial colorectal adenocarcinoma cell line 2.	trictide	19-27	MARVEL domain containing 2	Homo sapiens	62-73
31226440-8	2019	Here, we report transcriptomics analysis demonstrating that the expression profile of TRIC-isolated trophoblast cells was distinct from that of maternal cervical cells and included genes associated with the EVT phenotype and invasion.	EVT	207-210	MARVEL domain containing 2	Homo sapiens	86-90
30978594-0	2019	The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story.	Adenosine Triphosphate	4-7	MARVEL domain containing 2	Homo sapiens	30-34
30978594-4	2019	These new insights are revealing how the different TRiC/CCT subunits create asymmetry in its ATP-driven conformational cycle and its interaction with non-native polypeptides, which ultimately underlie its unique ability to fold proteins that cannot be folded by other chaperones.	Adenosine Triphosphate	93-96	MARVEL domain containing 2	Homo sapiens	51-55
30100183-7	2018	ATP binding to TRiC effects an asymmetric conformational change in the chaperonin ring.	Adenosine Triphosphate	0-3	MARVEL domain containing 2	Homo sapiens	15-19
25342745-0	2014	The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation.	Tryptophan	46-49	MARVEL domain containing 2	Homo sapiens	24-28
25919114-0	2015	Redox Regulation of Cell Contacts by Tricellulin and Occludin: Redox-Sensitive Cysteine Sites in Tricellulin Regulate Both Tri- and Bicellular Junctions in Tissue Barriers as Shown in Hypoxia and Ischemia.	Cysteine	79-87	MARVEL domain containing 2	Homo sapiens	37-48
25919114-0	2015	Redox Regulation of Cell Contacts by Tricellulin and Occludin: Redox-Sensitive Cysteine Sites in Tricellulin Regulate Both Tri- and Bicellular Junctions in Tissue Barriers as Shown in Hypoxia and Ischemia.	Cysteine	79-87	MARVEL domain containing 2	Homo sapiens	97-108
25755282-7	2015	USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates.	polyglutamine	127-140	MARVEL domain containing 2	Homo sapiens	40-44
28461478-0	2017	Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis.	Adenosine Triphosphate	35-38	MARVEL domain containing 2	Homo sapiens	61-65
28461478-2	2017	The CCT/TRiC chaperonin nanomachine undergoes ATP-driven conformational changes that are crucial for its folding function.	Adenosine Triphosphate	46-49	MARVEL domain containing 2	Homo sapiens	8-12
27686496-0	2016	Transient Kinetic Analysis of ATP Hydrolysis by the CCT/TRiC Chaperonin.	Adenosine Triphosphate	30-33	MARVEL domain containing 2	Homo sapiens	56-60
27686496-1	2016	The chaperonin-containing t-complex polypeptide 1 (CCT, also known as TRiC) assists protein folding in an ATP-dependent manner.	Adenosine Triphosphate	106-109	MARVEL domain containing 2	Homo sapiens	70-74
27686496-2	2016	CCT/TRiC was mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis was measured as a function of time using the coumarin-labeled phosphate-binding protein method.	Phosphates	83-92	MARVEL domain containing 2	Homo sapiens	4-8
27686496-5	2016	The values of the observed rate constants corresponding to the burst phases are found to decrease with increasing ATP and K+ concentrations, thereby indicating that the apo state of CCT/TRiC is in equilibrium between several conformations and that "conformational selection" by ATP takes place before hydrolysis.	Adenosine Triphosphate	114-117	MARVEL domain containing 2	Homo sapiens	186-190
27686496-5	2016	The values of the observed rate constants corresponding to the burst phases are found to decrease with increasing ATP and K+ concentrations, thereby indicating that the apo state of CCT/TRiC is in equilibrium between several conformations and that "conformational selection" by ATP takes place before hydrolysis.	Adenosine Triphosphate	278-281	MARVEL domain containing 2	Homo sapiens	186-190
26919977-9	2016	This case study demonstrates the utility of TRIC to accurately identify fetal gender as a means of reducing the need for prophylactic administration of exogenous steroids in pregnancies at risk of CAH.	Steroids	162-170	MARVEL domain containing 2	Homo sapiens	44-48
25975750-5	2015	The purpose of this study is to investigate the expression and localization of TRIC in choroidal epithelial cells in vitro and whether altered TRIC expression mediates Pb-induced loss of barrier function.	Lead	168-170	MARVEL domain containing 2	Homo sapiens	143-147
25975750-7	2015	Downregulation of TRIC by siRNA increased the BCB permeability corroborated by altered transendothelial electrical resistance (TEER) and FITC-dextran flux.	Bromocholine bromide	46-49	MARVEL domain containing 2	Homo sapiens	18-22
25975750-7	2015	Downregulation of TRIC by siRNA increased the BCB permeability corroborated by altered transendothelial electrical resistance (TEER) and FITC-dextran flux.	fluorescein isothiocyanate dextran	137-149	MARVEL domain containing 2	Homo sapiens	18-22
25975750-8	2015	Treatment with 10muM Pb reduced TRIC protein expression, but overexpression of TRIC alleviated the Pb-induced increase in BCB permeability.	10mum pb	15-23	MARVEL domain containing 2	Homo sapiens	32-36
25975750-8	2015	Treatment with 10muM Pb reduced TRIC protein expression, but overexpression of TRIC alleviated the Pb-induced increase in BCB permeability.	Lead	21-23	MARVEL domain containing 2	Homo sapiens	32-36
25975750-8	2015	Treatment with 10muM Pb reduced TRIC protein expression, but overexpression of TRIC alleviated the Pb-induced increase in BCB permeability.	Bromocholine bromide	122-125	MARVEL domain containing 2	Homo sapiens	79-83
25179274-2	2015	It is often found in surface waters in both the acidic (HTric) and basic (Tric(-)) forms (pKa ~8), and it can undergo direct photodegradation to produce several intermediates including a dioxin congener (2,8-dichlorodibenzodioxin, hereafter 28DCDD).	Water	29-35	MARVEL domain containing 2	Homo sapiens	57-61
25179274-2	2015	It is often found in surface waters in both the acidic (HTric) and basic (Tric(-)) forms (pKa ~8), and it can undergo direct photodegradation to produce several intermediates including a dioxin congener (2,8-dichlorodibenzodioxin, hereafter 28DCDD).	Dioxins	187-193	MARVEL domain containing 2	Homo sapiens	57-61
25179274-2	2015	It is often found in surface waters in both the acidic (HTric) and basic (Tric(-)) forms (pKa ~8), and it can undergo direct photodegradation to produce several intermediates including a dioxin congener (2,8-dichlorodibenzodioxin, hereafter 28DCDD).	2,8-Dichlorodibenzo-4-dioxin	204-229	MARVEL domain containing 2	Homo sapiens	57-61
25179274-7	2015	In the case of Tric(-) the direct photolysis is much more important than for HTric, but triplet-sensitised transformation could produce 28DCDD + 27DCDD with higher yield compared to the direct photolysis, and it could play some role as dioxin source in deep waters with elevated DOC.	28dcdd + 27dcdd	136-151	MARVEL domain containing 2	Homo sapiens	15-19
25179274-7	2015	In the case of Tric(-) the direct photolysis is much more important than for HTric, but triplet-sensitised transformation could produce 28DCDD + 27DCDD with higher yield compared to the direct photolysis, and it could play some role as dioxin source in deep waters with elevated DOC.	Dioxins	236-242	MARVEL domain containing 2	Homo sapiens	15-19
25668204-1	2015	The immunoglobulin (Ig)-like domain containing receptor 1 (ILDR1) gene encodes angulin-2/ILDR1, a recently discovered tight junction protein, which forms tricellular tight junction (tTJ) structures with tricellulin and lipolysis-stimulated lipoprotein receptor (LSR) at tricellular contacts (TCs) in the inner ear.	9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide	292-295	MARVEL domain containing 2	Homo sapiens	203-214
25668204-5	2015	Interestingly, partial mislocalization of the p.P69H variant protein and tricellulin at TCs was observed, in contrast to a severe mislocalization and complete failure of tricellulin recruitment of the other reported ILDR1 mutations.	9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide	88-91	MARVEL domain containing 2	Homo sapiens	73-84
25342745-0	2014	The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation.	Aspartic Acid	50-53	MARVEL domain containing 2	Homo sapiens	24-28
23239027-10	2013	These findings show the heterogeneity of the molecular organization of tTJs in terms of the content of LSR, ILDR1 or ILDR2, and suggest that ILDR1-mediated recruitment of tricellulin to TCs is required for hearing.	9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide	186-189	MARVEL domain containing 2	Homo sapiens	171-182
25437552-3	2014	Here, we demonstrate that HSF1 is directly regulated by TRiC/CCT, a central ATP-dependent chaperonin complex that folds cytosolic proteins.	Adenosine Triphosphate	76-79	MARVEL domain containing 2	Homo sapiens	56-60
23250572-2	2013	We scrutinized the brain for tricellulin expression in endothelial and neural cells by using real-time polymerase chain reaction, Western blot and immunohistochemical and immunocytochemical analysis of cultured brain cells and paraffin sections of brain.	Paraffin	227-235	MARVEL domain containing 2	Homo sapiens	29-40
24298020-0	2014	Vaccinia-related kinase 2 mediates accumulation of polyglutamine aggregates via negative regulation of the chaperonin TRiC.	polyglutamine	51-64	MARVEL domain containing 2	Homo sapiens	118-122
24298020-2	2014	Recently, the eukaryotic chaperonin TRiC hetero-oligomeric complex has been shown to play an important role in protecting cells against the accumulation of misfolded polyQ protein aggregates.	polyglutamine	166-171	MARVEL domain containing 2	Homo sapiens	36-40
24298020-6	2014	Interestingly, VRK2-mediated downregulation of TRiC increased aggregate formation of a polyQ-expanded huntingtin fragment.	polyglutamine	87-92	MARVEL domain containing 2	Homo sapiens	47-51
24298020-11	2014	Taken together, these results demonstrate that VRK2 is crucial to regulate the ubiquitination-proteosomal degradation of TRiC, which controls folding of polyglutamine proteins involved in Huntington"s disease.	polyglutamine	153-166	MARVEL domain containing 2	Homo sapiens	121-125
23073616-0	2013	Behavior of tricellulin during destruction and formation of tight junctions under various extracellular calcium conditions.	Calcium	104-111	MARVEL domain containing 2	Homo sapiens	12-23
23073616-3	2013	By using the well-differentiated pancreatic cancer cell line HPAC, which highly expresses tricellulin at tricellular contacts, we have investigated changes in the localization, expression and phosphorylation of tricellulin and in its TJ functions as a barrier and fence during the destruction and formation of TJs induced by changes in the extracellular calcium concentration.	Calcium	354-361	MARVEL domain containing 2	Homo sapiens	211-222
23073616-4	2013	During both extracellular Ca(2+) depletion caused by EGTA treatment and Ca(2+) repletion after Ca(2+) starvation, the expression of tricellulin increased in whole lysates and in Triton-X-100-insoluble fractions without any change in its mRNA.	Egtazic Acid	53-57	MARVEL domain containing 2	Homo sapiens	132-143
23073616-4	2013	During both extracellular Ca(2+) depletion caused by EGTA treatment and Ca(2+) repletion after Ca(2+) starvation, the expression of tricellulin increased in whole lysates and in Triton-X-100-insoluble fractions without any change in its mRNA.	Octoxynol	178-190	MARVEL domain containing 2	Homo sapiens	132-143
23073616-6	2013	Immunoprecipitation assays showed that tricellulin was phosphorylated on threonine residues when it increased after Ca(2+) depletion and repletion.	Threonine	73-82	MARVEL domain containing 2	Homo sapiens	39-50
23073616-10	2013	Thus, the dynamic behavior of tricellulin during the destruction and formation of TJs under various extracellular calcium conditions seems to be closely associated with the barrier and fence functions of TJs.	Calcium	114-121	MARVEL domain containing 2	Homo sapiens	30-41