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1                                              OAT1 and OAT3 localized to basolateral membranes of nonp
2                                              OAT1 increased the succinate dehydrogenase reaction rate
3                 Organic anion transporter 1 (OAT1) mediates the body disposition of a diverse array o
4                 Organic anion transporter 1 (OAT1), expressed at the basolateral membrane of renal pr
5                 Organic anion transporter 1 (OAT1), originally identified as NKT, has physiological p
6 of ligands with organic anion transporter 1 (OAT1).
7                 Organic anion transporter 1 (OAT1/SLC22A6) is a drug transporter with numerous xenobi
8        Notably, organic anion transporter-1 (OAT1) knockout mice expressed a similar pattern of reduc
9                 Organic anion transporter-1 (OAT1) mediates the body disposition of a diverse array o
10                 Organic anion transporter-1 (OAT1) mediates the body's disposition of a diverse array
11 atory drugs) is organic anion transporter-1 (OAT1), originally identified as NKT.
12 -regulating the organic anion transporter-1 (OAT1).
13 following transporters: GLUT-1; MCT 1 and 2; OAT1; Oatp1; mdr 1a and 1b; MRP 1 and 5; beta-alanine, s
14 e secretory urate transporters-ABCG2, ABCC4, OAT1, and OAT3.
15 ciated growth defects to occur, and ablating OAT1 caused a significant increase in acetate and other
16 sma membrane, and PKC activation accelerated OAT1 internalization without affecting OAT1 recycling.
17 rated OAT1 internalization without affecting OAT1 recycling.
18                                     Although OAT1 function (uptake in oat3(-/-) tissue) was confined
19 d partially reversed by p-aminohippurate (an OAT1 substrate).
20 ffects were fully reversed by probenecid (an OAT1 inhibitor) and partially reversed by p-aminohippura
21  by PKCzeta, subsequently confirmed using an OAT1-specific substrate, adefovir.
22 enous compounds enabling construction of an "OAT1-centered metabolic interaction network." Pathway an
23 d, which are diminished upon adding OCT2 and OAT1/3 transport inhibitors.
24 ll as transcriptomic data from wild-type and OAT1 knock-out animals, resulting in the implication of
25  of organic cation (OCT2) and organic anion (OAT1/3) transporters, which leads to improved drug uptak
26                                The augmented OAT1 expression and transport activity after the treatme
27 sts that OAT1 ubiquitination proceeds before OAT1 internalization.
28 sue assays demonstrated interactions between OAT1 and key intermediates in these metabolic pathways,
29 ive mutant of dynamin-2, a maneuver blocking OAT1 internalization, which suggests that OAT1 ubiquitin
30 preserved kidney structure and function, but OAT1-transported 2OGA was not protective, suggesting tha
31 oduced reactive oxygen species (ROS) control OAT1 activity and are balanced by the glutathione pathwa
32 pecific organic anion transporters of drugs, OAT1 (SLC22A6 or NKT) and OAT3 (SLC22A8), play a role in
33 bolite sensing and signaling as an effective OAT1 regulation mechanism to maintain plasma metabolite
34 port of p-aminohippuric acid and an enhanced OAT1 surface expression.
35 OAT1, which correlated well with an enhanced OAT1-mediated transport of p-aminohippuric acid and an e
36 ute activation of PKC significantly enhances OAT1 ubiquitination both in vitro and ex vivo.
37 e of bortezomib and carfilzomib in enhancing OAT1 expression and transport activity by preventing the
38 ified from cow heart mitochondria an enzyme (OAT1) with OAA tautomerase (OAT) activity that converts
39 s OAT1 activity by altering already existent OAT1 trafficking, and (iii) OAT1 internalization occurs
40  the organic anion transporter (OAT) family: OAT1 (SLC22A6, originally NKT) and OAT3 (SLC22A8).
41  Drugs may alter metabolism by competing for OAT1 binding of metabolites.
42 NA (RT-PCR) and protein (immunoblotting) for OAT1, OAT3, NaDC3, and MRP4 were detected in extracts of
43 of succinate dehydrogenase was necessary for OAT1-associated growth defects to occur, and ablating OA
44 tion at individual sites is not required for OAT1 function, and 3) glycosylation plays an important r
45 hat PKC isoform PKCalpha was responsible for OAT1 ubiquitination.
46        We demonstrate a key in vivo role for OAT1 and/or OAT3 in the handling of over 35 uremic toxin
47 ent analysis indicated an important role for OAT1 in metabolism involving: the TCA cycle, tryptophan
48 ork is also consistent with a major role for OAT1 in modulating metabolic and signaling pathways invo
49   These results indicate a critical role for OAT1 in the functioning of the classical pathway.
50 gencies have recommended drugs be tested for OAT1 and OAT3 binding or transport, it follows that thes
51 timulated urate transport mediated by GLUT9, OAT1, OAT3, ABCG2, and ABCC4 and inhibited insulin's sti
52 ee-dimensional model was generated for human OAT1 (hOAT1) based on fold recognition to the crystal st
53 ngs demonstrated for the first time that (i) OAT1 constitutively traffics between plasma membrane and
54 already existent OAT1 trafficking, and (iii) OAT1 internalization occurs partly through a dynamin- an
55                         The model implicated OAT1 in the regulation of many classes of lipids, includ
56 unteers and rats in vivo, leading to induced OAT1 expression and increased removal of indoxyl sulfate
57 models, we show that indoxyl sulfate induces OAT1 via AhR and EGFR signaling, controlled by miR-223.
58 sts, and beta-lactam antibiotics) to inhibit OAT1 expressed in Chinese hamster ovary cells.
59 ctivation of protein kinase C (PKC) inhibits OAT1 activity by promoting ubiquitination of the transpo
60 ctivation of protein kinase C (PKC) inhibits OAT1 activity by reducing OAT1 cell-surface expression t
61 c drug and organic anion transporters (OATs) OAT1 (SLC22a6) and OAT3 (SLC22a8).
62  the present study implicate the activity of OAT1 in the uptake and toxicity of Hg (when in the form
63            We have now generated a colony of OAT1 knock-out mice, permitting elucidation of the role
64           To investigate the contribution of OAT1 and OAT3 in various nephron segments, the OAT-selec
65 ies; therefore, the relative contribution of OAT1 has remained unclear.
66 the ubiquitination-induced downregulation of OAT1 expression and transport activity.
67 opathy demonstrated lower gene expression of OAT1 and OAT3.
68 ion and characterization of glycosylation of OAT1 and may provide important insights into the structu
69 al differences in the relative importance of OAT1 and OAT3 in antiviral handling in developing and ma
70 l compounds were evaluated for inhibition of OAT1 and OAT3.
71 nock-out mice, suggesting the involvement of OAT1 in their renal secretion.
72          To assess the impact of the loss of OAT1 or OAT3 function on the kidney, an organ where thes
73 t of extracellular alphaKG on the potency of OAT1 inhibition should be considered when assessing drug
74  carfilzomib resulted from a reduced rate of OAT1 degradation.
75 ucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not requir
76 zomib and carfilzomib in their regulation of OAT1 expression and transport activity.
77   Therefore, understanding the regulation of OAT1 has profound clinical significance.
78  novel mechanistic insights into the role of OAT1 and other drug transporters implicated in metabolic
79 rprisingly little is known about the role of OAT1 in lipid metabolism.
80 Signaling Theory, the data support a role of OAT1 in systemic lipid metabolism.
81  mice, permitting elucidation of the role of OAT1 in the context of these other potentially functiona
82              To directly address the role of OAT1 ubiquitination, we then generated two OAT1 mutants,
83 This gives a picture of the in vivo roles of OAT1 and OAT3 in the regulation of the uremic solutes an
84 We therefore examined the potential roles of OAT1 in metabolic pathways using Recon 1, a functionally
85 mentally validated, confidence ranked set of OAT1-interacting endogenous compounds enabling construct
86  might represent physiological substrates of OAT1.
87 cy are potential transportable substrates of OAT1.
88  plays an important role in the targeting of OAT1 onto the plasma membrane.
89          We further showed that treatment of OAT1-expressing cells with concanavalin A, depletion of
90 troscopy has revealed that ubiquitination of OAT1 consists of polyubiquitin chains, primarily through
91 -8, 12) showed potent inhibitory activity on OAT1, while seven flavones (2, 3, 6-9, 12) showed marked
92 e C (PKC) inhibits OAT1 activity by reducing OAT1 cell-surface expression through accelerating its in
93 antly blocked constitutive and PKC-regulated OAT1 internalization.
94 biquitination is essential for PKC-regulated OAT1 trafficking.
95 315 play a synergistic role in PKC-regulated OAT1 ubiquitination, trafficking, and transport activity
96 ndosomes, (ii) PKC activation down-regulates OAT1 activity by altering already existent OAT1 traffick
97 nstrate that PKCzeta activation up-regulates OAT1 and OAT3 function, and that protein-protein interac
98 inding provides a new strategy in regulating OAT1 function that can be used to accelerate the clearan
99                      Transport of the shared OAT1/OAT3 substrate, rho-aminohippurate, behaved similar
100                                        Since OAT1 and OAT3 are inhibited by many drugs, the data impl
101 lyubiquitin chains, abolishes PKC-stimulated OAT1 ubiquitination and internalization.
102 her show that ubiquitination of cell-surface OAT1 increases in cells transfected with dominant negati
103               We previously demonstrate that OAT1 activity was down-regulated by activation of protei
104               We previously established that OAT1 constitutively internalizes from and recycles back
105           We had previously established that OAT1 undergoes constitutive internalization from and rec
106                                The fact that OAT1 can affect many systemic biological pathways sugges
107 This observation raises the possibility that OAT1 helps regulate broader metabolic activities.
108                       We finally showed that OAT1 colocalized with transferrin, a marker for clathrin
109         In the current study, we showed that OAT1 constitutively internalized from and recycled back
110 ed metabolomics in knockouts have shown that OAT1 mediates the secretion or reabsorption of many impo
111                     Our results suggest that OAT1 is a universal metabolite repair enzyme that is req
112                          This suggested that OAT1 activity was also modified by PKCzeta, subsequently
113 ng OAT1 internalization, which suggests that OAT1 ubiquitination proceeds before OAT1 internalization
114 s and pathway analysis support the view that OAT1 plays a greater role in kidney proximal tubule meta
115 o have strong OAT activity, and ablating the OAT1 homolog caused significant growth defects.
116 oxicity of this conjugate was reduced by the OAT1-exchangeable dicarboxylates alpha-ketoglutarate, gl
117 evaluate these flavones as inhibitors of the OAT1 and OAT3, and as antifungal agents.
118 s with OAT1 highlights the complexity of the OAT1 ligand-binding surface.
119 thranilate, and N-formylanthranilate through OAT1, the kidney responds by activating its own tryptoph
120 y demonstrated that ubiquitin conjugation to OAT1 leads to OAT1 internalization from the cell surface
121  that ubiquitin conjugation to OAT1 leads to OAT1 internalization from the cell surface and subsequen
122 predictions for metabolic pathways linked to OAT1-related transport.
123  (OCT2 and OCT3), organic anion transporter (OAT1), and monoamine transporters were also inhibited by
124               The organic anion transporters OAT1 (SLC22A6) and OAT3 (SLC22A8) have similar substrate
125 e established the organic anion transporters OAT1 (SLC22A6, NKT) and OAT3 (SLC22A8) among the main mu
126               The organic anion transporters OAT1 (SLC22A6, originally identified by us as NKT) and O
127 rocalyx with the organic anion transporters (OAT1 and OAT3) and microorganisms led to the elucidation
128 ed by leucine to organic anion transporters (OAT1 and OAT3) and the monocarboxylate transporter type
129 he multispecific organic anion transporters, OAT1 (SLC22A6) and OAT3 (SLC22A8), the main kidney elimi
130 f OAT1 ubiquitination, we then generated two OAT1 mutants, each having multiple lysines (K) simultane
131  preventing the degradation of ubiquitinated OAT1 in proteasomes.
132 d pepstatin A, suggesting that ubiquitinated OAT1 degrades through proteasomes.
133  current study showed that the ubiquitinated OAT1 accumulated in the presence of the proteasomal inhi
134 lzomib extremely increased the ubiquitinated OAT1, which correlated well with an enhanced OAT1-mediat
135 dentified the pathway in which ubiquitinated OAT1 degrades and unveiled a novel role of anticancer dr
136 fier was able to successfully predict unique OAT1 versus OAT3 drugs; this suggests the feasibility of
137 ggest the potential molecular basis by which OAT1 and OAT3 modulate distinct metabolic and signaling
138                                Compared with OAT1, OAT3 tends to interact with more complex substrate
139 o determine if drug candidates interact with OAT1 and/or OAT3.
140 s that some of these compounds interact with OAT1 in vitro.
141  results suggest that drugs interacting with OAT1 and OAT3 can have far reaching consequences on meta
142 cellular alphaKG on ligand interactions with OAT1 highlights the complexity of the OAT1 ligand-bindin

 
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