Characterization of the monocarboxylate transporter 1 expressed in Xenopus laevis oocytes by changes in cytosolic pH.
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The Contribution of Blood Lactate to Brain Energy Metabolism in Humans Measured by Dynamic 13C Nuclear Magnetic Resonance SpectroscopyThe cataract and glucosuria associated monocarboxylate transporter MCT12 is a new creatine transporterThe proton-linked monocarboxylate transporter (MCT) family: structure, function and regulationThe orphan transporter v7-3 (slc6a15) is a Na+-dependent neutral amino acid transporter (B0AT2)CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expressionThe in vivo neuron-to-astrocyte lactate shuttle in human brain: evidence from modeling of measured lactate levels during visual stimulationCharacterisation of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscleSupply and demand in cerebral energy metabolism: the role of nutrient transportersLactate metabolism: a new paradigm for the third millenniumRegulation of monocarboxylic acid transporter-1 by cAMP dependent vesicular trafficking in brain microvascular endothelial cellsIs L-lactate a novel signaling molecule in the brain?Voltage dependence of H+ buffering mediated by sodium bicarbonate cotransport expressed in Xenopus oocytesNeuroprotective role of monocarboxylate transport during glucose deprivation in slice cultures of rat hippocampusTransport of lactate and pyruvate in the intraerythrocytic malaria parasite, Plasmodium falciparumCrucial residue involved in L-lactate recognition by human monocarboxylate transporter 4 (hMCT4)The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is modulated by the associated ancillary proteinStudies on the DIDS-binding site of monocarboxylate transporter 1 suggest a homology model of the open conformation and a plausible translocation cycleAR-C155858 is a potent inhibitor of monocarboxylate transporters MCT1 and MCT2 that binds to an intracellular site involving transmembrane helices 7-10Neutral amino acid transporter ASCT2 displays substrate-induced Na+ exchange and a substrate-gated anion conductanceTissue-specific expression of monocarboxylate transporters during fasting in mice.H+-coupled nutrient, micronutrient and drug transporters in the mammalian small intestineTumor metabolism of lactate: the influence and therapeutic potential for MCT and CD147 regulation.Lactate transport in skeletal muscle - role and regulation of the monocarboxylate transporter.Role of monocarboxylate transporters in drug delivery to the brain.Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters.Role of plasma membrane transporters in muscle metabolism.CD147 required for corneal endothelial lactate transport.Transport activity of the sodium bicarbonate cotransporter NBCe1 is enhanced by different isoforms of carbonic anhydraseFacilitated lactate transport by MCT1 when coexpressed with the sodium bicarbonate cotransporter (NBC) in Xenopus oocytesThe monocarboxylate transporter family--Structure and functional characterization.Kinetic analysis and design of experiments to identify the catalytic mechanism of the monocarboxylate transporter isoforms 4 and 1.Intramolecular proton shuttle supports not only catalytic but also noncatalytic function of carbonic anhydrase II.Regulation of the glutamine transporter SN1 by extracellular pH and intracellular sodium ions.Enzymatic suppression of the membrane conductance associated with the glutamine transporter SNAT3 expressed in Xenopus oocytes by carbonic anhydrase II.Nonenzymatic proton handling by carbonic anhydrase II during H+-lactate cotransport via monocarboxylate transporter 1.MCT2 expression and lactate influx in anorexigenic and orexigenic neurons of the arcuate nucleus.Inward flux of lactate⁻ through monocarboxylate transporters contributes to regulatory volume increase in mouse muscle fibresAnalysis of the binding moiety mediating the interaction between monocarboxylate transporters and carbonic anhydrase IITransport activity of the high-affinity monocarboxylate transporter MCT2 is enhanced by extracellular carbonic anhydrase IV but not by intracellular carbonic anhydrase IIMolecular basis for the interaction of the mammalian amino acid transporters B0AT1 and B0AT3 with their ancillary protein collectrin
P2860
Q22336991-D0416C67-8E05-4DDB-8F74-BF71C525C70DQ24338344-BE1CC30E-A254-4B52-A120-B68E7864503DQ24531840-019EF953-3658-4DE3-9312-B7C16FAED674Q24541425-ACF01408-3533-434F-8995-2CB9C576EEBDQ24630430-8426D0EF-F7D3-4B7D-AAF4-49B619F38A45Q24648293-3D227186-CEBE-4BC5-8D46-CDB7579A182CQ24650995-C1EAFB41-88F1-4F4F-A779-5A3AC3AE06CAQ24671074-38ABE1CE-2DDA-41E5-A924-90B7D6CB296BQ24677962-E295E7DF-7502-408D-BBB9-6C83EE235FC1Q27332278-E58F2FF3-32BE-470E-9CCA-A23186B2AFBDQ28083173-0B73EDF1-C237-4800-ADAA-553797421996Q28259915-FF92065D-9D0B-45D9-A518-D648E95AEA9DQ28356199-A6316027-A14D-414E-89A2-60B68FD9F9FCQ28363250-4960EB8B-6FA8-4519-B7FD-62431641AC50Q28535008-3B8A1111-A1FC-4BE8-823A-EA8BABDE4F34Q28576555-5EC765C5-ED38-4D40-AA6E-6D82B25900A6Q28580055-D1FDEDCC-1396-46D1-B512-BA48B4306477Q28580635-ED283925-0F13-4713-AAC4-8A094623F2FFQ28609231-A29AAD86-784F-4772-8E5D-736C78466D5CQ30316982-029DF3D8-CABE-4FE9-8577-DC542A0D39F2Q33578118-4F7C3A97-A529-459E-A33C-AFAC2E7358BBQ33641532-254CBFBA-8662-4D7C-AEE7-4B22C26A46E3Q33652197-8D883EC7-82CD-4962-8A25-120A5F6B6B76Q33854710-69716F1C-95F8-4582-ACA4-E59223A79DD4Q33940393-95155082-9045-449A-8885-FB6FA1149C20Q33973728-8297A4F8-7D7A-479F-8FB9-873DED13828EQ33975123-926A0117-2073-4BD3-B1A6-28BFE6150C1DQ34072636-5D4A9E12-CDE2-4CD6-836C-072F30985284Q34184269-346776D4-6A81-41C5-83FE-B7773EB8BED6Q34237222-36D85125-D1D8-490F-925E-7F80674C5203Q34494499-502941BD-E992-4075-AEF0-588C395A96D8Q34582558-04E83D4B-DBD9-4930-B2D2-089BFD1BD600Q34647464-100A255C-B7F7-4AA9-8CC7-F222D28BBD8AQ34654580-50FD6175-A1EB-4D5A-A424-76FF3E3A2A80Q34656483-74F6C2F9-A790-430F-B15A-D824D0937777Q34701707-DA0408C5-43B4-42D7-B2C9-854F2B33075CQ35078397-20F51ECD-97CF-4AF2-BACC-6FD271F91CAFQ35080397-FFC39AEA-E52D-4653-AD27-ED15E7E6D430Q35145047-0D521FCC-79F8-481C-A8FA-382AA05BFC69Q35736694-CA0A6C2F-67CF-46AB-9EA2-13DABCB14012
P2860
Characterization of the monocarboxylate transporter 1 expressed in Xenopus laevis oocytes by changes in cytosolic pH.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Characterization of the monoca ...... es by changes in cytosolic pH.
@en
type
label
Characterization of the monoca ...... es by changes in cytosolic pH.
@en
prefLabel
Characterization of the monoca ...... es by changes in cytosolic pH.
@en
P2093
P2860
P356
P1433
P1476
Characterization of the monoca ...... es by changes in cytosolic pH.
@en
P2093
P2860
P304
P356
10.1042/BJ3330167
P407
P478
333 ( Pt 1)
P577
1998-07-01T00:00:00Z