PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32820343-2 2020 It is commonly assumed that the upregulation of the facilitated glucose transporter GLUT1 meets the tumor"s demand for sugar. Sugars 119-124 solute carrier family 2 member 1 Homo sapiens 84-89 32933091-3 2020 The way to improve the selectivity of a drug to the cancer cells seems to be its conjugation with a sugar molecule, which should facilitate its selective transport through GLUT transporters (glucose transporters), whose overexpression is seen in some types of cancer. Sugars 100-105 solute carrier family 2 member 1 Homo sapiens 172-176 32789453-3 2021 Recently, we discovered that WZB117, a specific Glut1 inhibitor, restricts glycolysis by inhibiting the passive sugar transport of human red blood cells and cancer cells. Sugars 112-117 solute carrier family 2 member 1 Homo sapiens 48-53 33536238-1 2021 The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. Sugars 113-118 solute carrier family 2 member 1 Homo sapiens 31-36 31367876-0 2019 Sugar Modification Enhances Cytotoxic Activity of PAMAM-Doxorubicin Conjugate in Glucose-Deprived MCF-7 Cells - Possible Role of GLUT1 Transporter. Sugars 0-5 solute carrier family 2 member 1 Homo sapiens 129-134 32339462-7 2020 Depletion of caveolin-1 - the main structural protein of caveolae structures - in bladder cancer cells resistant to PDT increased the amount of sugar-binding proteins, i.e. GLUT1, at the cell membrane resulting in an improved PcGal16 uptake and PDT efficacy. Sugars 144-149 solute carrier family 2 member 1 Homo sapiens 173-178 30361436-0 2018 Red wine and green tea flavonoids are cis-allosteric activators and competitive inhibitors of glucose transporter 1 (GLUT1)-mediated sugar uptake. Sugars 133-138 solute carrier family 2 member 1 Homo sapiens 94-115 31324056-2 2019 GLUT1 is an important target in cancer treatment because cancer cells upregulate GLUT1, a membrane protein that facilitates the basal uptake of glucose in most cell types, to ensure the flux of sugar into metabolic pathways. Sugars 194-199 solute carrier family 2 member 1 Homo sapiens 0-5 31324056-2 2019 GLUT1 is an important target in cancer treatment because cancer cells upregulate GLUT1, a membrane protein that facilitates the basal uptake of glucose in most cell types, to ensure the flux of sugar into metabolic pathways. Sugars 194-199 solute carrier family 2 member 1 Homo sapiens 81-86 30361436-6 2018 Docking studies suggest that only one flavonoid can bind to GLUT1 at any instant, but sugar transport and ligand-binding studies indicate that human erythrocyte GLUT1 can bind at least two flavonoid molecules simultaneously. Sugars 86-91 solute carrier family 2 member 1 Homo sapiens 161-166 30361436-0 2018 Red wine and green tea flavonoids are cis-allosteric activators and competitive inhibitors of glucose transporter 1 (GLUT1)-mediated sugar uptake. Sugars 133-138 solute carrier family 2 member 1 Homo sapiens 117-122 29797802-2 2018 Glucose transporter-1 (GLUT-1) is a member of facilitative sugar transporters that are integral membrane glycoproteins moving sugar across cell membrane. Sugars 59-64 solute carrier family 2 member 1 Homo sapiens 0-21 30144735-9 2018 In summary, our results indicate that whereas GLUT1 could be considered as a basal, constant sugar intake system for the whole of pregnancy in queens, GLUT3 is specially required for optimizing glucose uptake during the first half of pregnancy in this species through a progesterone-related mechanism. Sugars 93-98 solute carrier family 2 member 1 Homo sapiens 46-51 29953861-4 2018 In previous study, WZB117 (2-fluoro-6-(m-hydroxybenzoyloxy) phenyl m-hydroxybenzoate) inhibits GLUT1 by binding the exofacial sugar-binding site and inhibits the insulin-sensitive GLUT4 with greater potency than its inhibition of either GLUT1 or GLUT3. Sugars 126-131 solute carrier family 2 member 1 Homo sapiens 95-100 29953861-4 2018 In previous study, WZB117 (2-fluoro-6-(m-hydroxybenzoyloxy) phenyl m-hydroxybenzoate) inhibits GLUT1 by binding the exofacial sugar-binding site and inhibits the insulin-sensitive GLUT4 with greater potency than its inhibition of either GLUT1 or GLUT3. Sugars 126-131 solute carrier family 2 member 1 Homo sapiens 237-242 29797802-2 2018 Glucose transporter-1 (GLUT-1) is a member of facilitative sugar transporters that are integral membrane glycoproteins moving sugar across cell membrane. Sugars 59-64 solute carrier family 2 member 1 Homo sapiens 23-29 29209831-0 2018 Kinetic Basis of Cis- and Trans-Allostery in GLUT1-Mediated Sugar Transport. Sugars 60-65 solute carrier family 2 member 1 Homo sapiens 45-50 29209831-1 2018 A growing body of evidence demonstrates that GLUT1-mediated erythrocyte sugar transport is more complex than widely assumed and that contemporary interpretations of emergent GLUT1 structural data are incompatible with the available transport and biochemical data. Sugars 72-77 solute carrier family 2 member 1 Homo sapiens 45-50 28636761-4 2017 In this review, the current state of knowledge of the molecular interactions behind Glut-mediated sugar uptake, Glut-targeting probes, therapeutics, and inhibitors are discussed. Sugars 98-103 solute carrier family 2 member 1 Homo sapiens 84-88 29066623-1 2017 Recent structural studies suggest that GLUT1 (glucose transporter 1)-mediated sugar transport is mediated by an alternating access transporter that successively presents exofacial (e2) and endofacial (e1) substrate-binding sites. Sugars 78-83 solute carrier family 2 member 1 Homo sapiens 39-44 29066623-1 2017 Recent structural studies suggest that GLUT1 (glucose transporter 1)-mediated sugar transport is mediated by an alternating access transporter that successively presents exofacial (e2) and endofacial (e1) substrate-binding sites. Sugars 78-83 solute carrier family 2 member 1 Homo sapiens 46-67 29066623-4 2017 Here, homology modeling supported the alternating access transporter model for sugar transport by confirming at least four GLUT1 conformations, the so-called outward, outward-occluded, inward-occluded, and inward GLUT1 conformations. Sugars 79-84 solute carrier family 2 member 1 Homo sapiens 123-128 29066623-4 2017 Here, homology modeling supported the alternating access transporter model for sugar transport by confirming at least four GLUT1 conformations, the so-called outward, outward-occluded, inward-occluded, and inward GLUT1 conformations. Sugars 79-84 solute carrier family 2 member 1 Homo sapiens 213-218 29066623-6 2017 Gln-282 contributed to sugar binding in all GLUT1 conformations via hydrogen bonding. Sugars 23-28 solute carrier family 2 member 1 Homo sapiens 44-49 25031038-11 2014 However, qualitative patterns of GLUT expression in the muscle (step 2) raise more questions than they answer regarding sugar transport in hummingbirds and suggest major differences in the regulation of sugar flux compared to nectar bats. Sugars 203-208 solute carrier family 2 member 1 Homo sapiens 33-37 28467806-6 2017 GLUT inhibitor mediated cell viability analysis, GLUT1 knockdown cell line-based cytotoxicity evaluation, and platinum accumulation study demonstrated that the cellular uptake of the sugar-conjugates was regulated by GLUT1. Sugars 183-188 solute carrier family 2 member 1 Homo sapiens 0-4 28467806-6 2017 GLUT inhibitor mediated cell viability analysis, GLUT1 knockdown cell line-based cytotoxicity evaluation, and platinum accumulation study demonstrated that the cellular uptake of the sugar-conjugates was regulated by GLUT1. Sugars 183-188 solute carrier family 2 member 1 Homo sapiens 49-54 28467806-6 2017 GLUT inhibitor mediated cell viability analysis, GLUT1 knockdown cell line-based cytotoxicity evaluation, and platinum accumulation study demonstrated that the cellular uptake of the sugar-conjugates was regulated by GLUT1. Sugars 183-188 solute carrier family 2 member 1 Homo sapiens 217-222 27688191-6 2017 Each sugar motif was found to be useful to enable the platinum(II) complexes as substrate for GLUT mediated cell uptake. Sugars 5-10 solute carrier family 2 member 1 Homo sapiens 94-98 26706102-5 2016 The results showed that the sugar-conjugated platinum(II) complexes can be recognized by the glucose recognition binding site of GLUT1 and their cell killing effect depends highly on the GLUT1 inhibitor, quercetin. Sugars 28-33 solute carrier family 2 member 1 Homo sapiens 129-134 26706102-5 2016 The results showed that the sugar-conjugated platinum(II) complexes can be recognized by the glucose recognition binding site of GLUT1 and their cell killing effect depends highly on the GLUT1 inhibitor, quercetin. Sugars 28-33 solute carrier family 2 member 1 Homo sapiens 187-192 25855082-6 2015 Genistein, an inhibitor of GLUT1, also inhibited sugar uptake by GLUT12. Sugars 49-54 solute carrier family 2 member 1 Homo sapiens 27-32 25715702-11 2015 Caffeine binding to GLUT1 mimics the action of ATP but not cytochalasin B on sugar transport. Sugars 77-82 solute carrier family 2 member 1 Homo sapiens 20-25 27688191-9 2017 The results from this study demonstrate the usefulness of glucose, mannose and galactose as alternative sugar motif on glycoconjugation for GLUT mediated drug design and pharmaceutical R&D, and the obtained fundamental results also support the potential of the GLUT targeted platinum(II)-sugar conjugates as lead compounds for further pre-clinical evaluation. Sugars 104-109 solute carrier family 2 member 1 Homo sapiens 140-144 27688191-9 2017 The results from this study demonstrate the usefulness of glucose, mannose and galactose as alternative sugar motif on glycoconjugation for GLUT mediated drug design and pharmaceutical R&D, and the obtained fundamental results also support the potential of the GLUT targeted platinum(II)-sugar conjugates as lead compounds for further pre-clinical evaluation. Sugars 104-109 solute carrier family 2 member 1 Homo sapiens 265-269 27688191-9 2017 The results from this study demonstrate the usefulness of glucose, mannose and galactose as alternative sugar motif on glycoconjugation for GLUT mediated drug design and pharmaceutical R&D, and the obtained fundamental results also support the potential of the GLUT targeted platinum(II)-sugar conjugates as lead compounds for further pre-clinical evaluation. Sugars 292-297 solute carrier family 2 member 1 Homo sapiens 265-269 27836974-0 2016 WZB117 (2-Fluoro-6-(m-hydroxybenzoyloxy) Phenyl m-Hydroxybenzoate) Inhibits GLUT1-mediated Sugar Transport by Binding Reversibly at the Exofacial Sugar Binding Site. Sugars 91-96 solute carrier family 2 member 1 Homo sapiens 76-81 27836974-0 2016 WZB117 (2-Fluoro-6-(m-hydroxybenzoyloxy) Phenyl m-Hydroxybenzoate) Inhibits GLUT1-mediated Sugar Transport by Binding Reversibly at the Exofacial Sugar Binding Site. Sugars 146-151 solute carrier family 2 member 1 Homo sapiens 76-81 27992462-7 2016 RESULTS: In response to short term changes in extracellular glucose and glucose/fructose concentrations (2.5mM to 75mM) carrier-mediated sugar uptake mediated by SGLT1 and/or the facilitative hexose transporters (GLUT1,2,3 and 5) was increased. Sugars 137-142 solute carrier family 2 member 1 Homo sapiens 213-228 27128978-1 2016 The human Glucose Transporter 1 (hGLUT1 or SLC2A1) is a facilitative membrane transporter found in the liver, intestines, kidney, and brain, where it transports sugars such as d-glucose and d-galactose. Sugars 161-167 solute carrier family 2 member 1 Homo sapiens 33-39 27128978-1 2016 The human Glucose Transporter 1 (hGLUT1 or SLC2A1) is a facilitative membrane transporter found in the liver, intestines, kidney, and brain, where it transports sugars such as d-glucose and d-galactose. Sugars 161-167 solute carrier family 2 member 1 Homo sapiens 43-49 25919356-6 2015 XylE has high sequence homology to human GLUT1 and key residues in the sugar-binding pocket are conserved. Sugars 71-76 solute carrier family 2 member 1 Homo sapiens 41-46 25510392-6 2015 There was a strong positive correlation observed between total sugar intake and glucose transporter 1 (GLUT1) (r = 0.897, p = 0.000, n = 12), and inverse correlations between total sugar and mTOR and IGF1 expression. Sugars 63-68 solute carrier family 2 member 1 Homo sapiens 80-101 25510392-6 2015 There was a strong positive correlation observed between total sugar intake and glucose transporter 1 (GLUT1) (r = 0.897, p = 0.000, n = 12), and inverse correlations between total sugar and mTOR and IGF1 expression. Sugars 63-68 solute carrier family 2 member 1 Homo sapiens 103-108 26098515-4 2015 This article reviews the history, classification, and general features of the MFS proteins; summarizes recent structural progress with a focus on the sugar porter family transporters exemplified by GLUT1; and discusses the molecular mechanisms of substrate binding, alternating access, and cotransport coupling. Sugars 150-155 solute carrier family 2 member 1 Homo sapiens 198-203 24847886-7 2014 Structure-based analysis of these mutations provides an insight into the alternating access mechanism of GLUT1 and other members of the sugar porter subfamily. Sugars 136-141 solute carrier family 2 member 1 Homo sapiens 105-110 22132964-4 2011 R198C and R380W occur in highly conserved amino acid motifs in the "sugar transport proteins signatures" that are observed in GLUT family transporters. Sugars 68-73 solute carrier family 2 member 1 Homo sapiens 126-130 24598365-2 2014 A recent study suggests that RBC GLUT1 transports DHA as its primary substrate and that only a subpopulation of GLUT1 transports sugars. Sugars 129-135 solute carrier family 2 member 1 Homo sapiens 112-117 23093404-2 2012 GLUT1 exhibits trans-acceleration, in which the presence of intracellular sugar stimulates the rate of unidirectional sugar uptake. Sugars 74-79 solute carrier family 2 member 1 Homo sapiens 0-5 23093404-2 2012 GLUT1 exhibits trans-acceleration, in which the presence of intracellular sugar stimulates the rate of unidirectional sugar uptake. Sugars 118-123 solute carrier family 2 member 1 Homo sapiens 0-5 23093404-7 2012 We propose that GLUT1 transmembrane domain 6 restrains import when intracellular sugar is absent by slowing transport-associated conformational changes. Sugars 81-86 solute carrier family 2 member 1 Homo sapiens 16-21 23177983-10 2012 For SGLT1 and GLUT1, the extensive hydrophilic and hydrophobic interactions between sugars and binding sites of the various intramembrane helices occur and lead to different substrate specificities and inhibitor affinities of the two transporters. Sugars 84-90 solute carrier family 2 member 1 Homo sapiens 14-19 22427993-3 2012 Sequence analysis revealed that Glut1 is a member of a large superfamily of transporters and that it is most closely related to evolutionary branches of this superfamily, branches that function to transport this sugar. Sugars 212-217 solute carrier family 2 member 1 Homo sapiens 32-37 21384913-1 2011 Cytochalasin B (CB) and forskolin (FSK) inhibit GLUT1-mediated sugar transport in red cells by binding at or close to the GLUT1 endofacial sugar binding site. Sugars 63-68 solute carrier family 2 member 1 Homo sapiens 48-53 21384913-1 2011 Cytochalasin B (CB) and forskolin (FSK) inhibit GLUT1-mediated sugar transport in red cells by binding at or close to the GLUT1 endofacial sugar binding site. Sugars 63-68 solute carrier family 2 member 1 Homo sapiens 122-127 21384913-1 2011 Cytochalasin B (CB) and forskolin (FSK) inhibit GLUT1-mediated sugar transport in red cells by binding at or close to the GLUT1 endofacial sugar binding site. Sugars 139-144 solute carrier family 2 member 1 Homo sapiens 48-53 21384913-1 2011 Cytochalasin B (CB) and forskolin (FSK) inhibit GLUT1-mediated sugar transport in red cells by binding at or close to the GLUT1 endofacial sugar binding site. Sugars 139-144 solute carrier family 2 member 1 Homo sapiens 122-127 21384913-11 2011 We discuss this result within the context of models for GLUT1-mediated sugar transport and GLUT1 quaternary structure, and we evaluate the major determinants of ligand binding affinity and cooperativity. Sugars 71-76 solute carrier family 2 member 1 Homo sapiens 56-61 18981181-12 2008 These observations provide experimental support for the proposed GLUT1 architecture; indicate that the proposed topology of membrane helices 5, 6, and 12 requires adjustment; and suggest that the metastable conformations of transmembrane helices 1 and 8 within the GLUT1 scaffold destabilize a sugar translocation intermediate. Sugars 294-299 solute carrier family 2 member 1 Homo sapiens 265-270 19166280-0 2009 The role of GLUT1 in the sugar-induced dielectric response of human erythrocytes. Sugars 25-30 solute carrier family 2 member 1 Homo sapiens 12-17 20231288-1 2010 GLUT1-catalyzed equilibrative sugar transport across the mammalian blood-brain barrier is stimulated during acute and chronic metabolic stress; however, the mechanism of acute transport regulation is unknown. Sugars 30-35 solute carrier family 2 member 1 Homo sapiens 0-5 19690067-6 2009 We then review GLUT1 topology, subunit architecture, and oligomeric structure and examine a new model for sugar transport that combines structural and kinetic analyses to satisfactorily reproduce GLUT1 behavior in human erythrocytes. Sugars 106-111 solute carrier family 2 member 1 Homo sapiens 196-201 15709778-0 2005 Quench-flow analysis reveals multiple phases of GluT1-mediated sugar transport. Sugars 63-68 solute carrier family 2 member 1 Homo sapiens 48-53 18177733-5 2008 As a proof of concept that this sensor can be used to screen for proteins playing a role in sugar flux and its control, we used siRNA inhibition of GLUT family members and show that GLUT1 is the major glucose transporter in HepG2 cells and that GLUT9 contributes as well, however to a lower extent. Sugars 92-97 solute carrier family 2 member 1 Homo sapiens 148-152 18177733-5 2008 As a proof of concept that this sensor can be used to screen for proteins playing a role in sugar flux and its control, we used siRNA inhibition of GLUT family members and show that GLUT1 is the major glucose transporter in HepG2 cells and that GLUT9 contributes as well, however to a lower extent. Sugars 92-97 solute carrier family 2 member 1 Homo sapiens 182-187 15823019-1 2005 Human erythrocyte hexose transfer is mediated by the glucose transport protein GLUT1 and is characterized by a complexity that is unexplained by available hypotheses for carrier-mediated sugar transport [Cloherty, E. K., Heard, K. S., and Carruthers, A. Sugars 187-192 solute carrier family 2 member 1 Homo sapiens 79-84 15823019-6 2005 GLUT1-HA-H6 confers GLUT1-specific sugar transport characteristics to transfected RE700A, including inhibition by cytochalasin B and high-affinity transport of the nonmetabolized sugar 3-O-methylglucose. Sugars 35-40 solute carrier family 2 member 1 Homo sapiens 0-5 15823019-6 2005 GLUT1-HA-H6 confers GLUT1-specific sugar transport characteristics to transfected RE700A, including inhibition by cytochalasin B and high-affinity transport of the nonmetabolized sugar 3-O-methylglucose. Sugars 35-40 solute carrier family 2 member 1 Homo sapiens 20-25 15823019-9 2005 Unlike transport in human red cells or transport in human embryonic kidney cells transfected with GLUT1-HA-H6, unidirectional sugar uptake in RE700A-GLUT1-HA-H6 is not inhibited by reductant and is not stimulated by intracellular sugar. Sugars 126-131 solute carrier family 2 member 1 Homo sapiens 149-160 15823019-9 2005 Unlike transport in human red cells or transport in human embryonic kidney cells transfected with GLUT1-HA-H6, unidirectional sugar uptake in RE700A-GLUT1-HA-H6 is not inhibited by reductant and is not stimulated by intracellular sugar. Sugars 230-235 solute carrier family 2 member 1 Homo sapiens 149-160 10715121-4 2000 Sugar binding assays using cells and membrane protein fractions indicate that sugar binding to erythrocytes is quantitatively accounted for by sugar binding to the hexose transport protein, GluT1. Sugars 0-5 solute carrier family 2 member 1 Homo sapiens 190-195 12379105-8 2002 In HEK cells, both parental GluT1- and GluT1.HA.H6-mediated sugar transport are acutely sensitive to cellular metabolic inhibition. Sugars 60-65 solute carrier family 2 member 1 Homo sapiens 28-33 12379105-8 2002 In HEK cells, both parental GluT1- and GluT1.HA.H6-mediated sugar transport are acutely sensitive to cellular metabolic inhibition. Sugars 60-65 solute carrier family 2 member 1 Homo sapiens 39-44 12379105-12 2002 It is proposed that cooperative nucleotide binding to GluT1 and nucleotide modulation of GluT1-mediated sugar transport are regulated by a proton-sensitive saltbridge (Glu329-Arg333/334). Sugars 104-109 solute carrier family 2 member 1 Homo sapiens 89-94 12379106-2 2002 When complexed with cytosolic ATP, GluT1 exhibits increased affinity for the sugar export site ligand cytochalasin B, prolonged substrate occlusion, reduced net sugar import capacity, and diminished reactivity with carboxyl terminal peptide-directed antibodies. Sugars 77-82 solute carrier family 2 member 1 Homo sapiens 35-40 12379106-2 2002 When complexed with cytosolic ATP, GluT1 exhibits increased affinity for the sugar export site ligand cytochalasin B, prolonged substrate occlusion, reduced net sugar import capacity, and diminished reactivity with carboxyl terminal peptide-directed antibodies. Sugars 161-166 solute carrier family 2 member 1 Homo sapiens 35-40 12379106-11 2002 The effects of ATP on GluT1-mediated sugar transport may be determined by the number of ATP molecules complexed with the transporter. Sugars 37-42 solute carrier family 2 member 1 Homo sapiens 22-27 11882521-1 2002 The recent identification of several additional members of the family of sugar transport facilitators (gene symbol SLC2A, protein symbol GLUT) has created a heterogeneous and, in part, confusing nomenclature. Sugars 73-78 solute carrier family 2 member 1 Homo sapiens 137-141 10821868-1 2000 GLUT8 is a novel glucose transporter-like protein that exhibits significant sequence similarity with the members of the sugar transport facilitator family (29.4% of amino acids identical with GLUT1). Sugars 120-125 solute carrier family 2 member 1 Homo sapiens 192-197 15449578-3 2004 The human GLUT family consists of 14 members, of which 11 have been shown to catalyze sugar transport. Sugars 86-91 solute carrier family 2 member 1 Homo sapiens 10-14 12379105-1 2002 Intracellular ATP inhibits human erythrocyte net sugar transport by binding cooperatively to the glucose transport protein (GluT1). Sugars 49-54 solute carrier family 2 member 1 Homo sapiens 124-129 12379105-4 2002 (2002) Biochemistry 41, 12639-12651) demonstrates that reduced intracellular pH promotes high-affinity ATP binding to GluT1 but inhibits ATP-modulation of GluT1-mediated sugar transport. Sugars 170-175 solute carrier family 2 member 1 Homo sapiens 155-160 10715121-4 2000 Sugar binding assays using cells and membrane protein fractions indicate that sugar binding to erythrocytes is quantitatively accounted for by sugar binding to the hexose transport protein, GluT1. Sugars 78-83 solute carrier family 2 member 1 Homo sapiens 190-195 10715121-4 2000 Sugar binding assays using cells and membrane protein fractions indicate that sugar binding to erythrocytes is quantitatively accounted for by sugar binding to the hexose transport protein, GluT1. Sugars 143-148 solute carrier family 2 member 1 Homo sapiens 190-195 10715121-5 2000 Kinetic analysis of net sugar fluxes indicates that GluT1 sugar binding sites are cytoplasmic. Sugars 24-29 solute carrier family 2 member 1 Homo sapiens 52-57 10715121-5 2000 Kinetic analysis of net sugar fluxes indicates that GluT1 sugar binding sites are cytoplasmic. Sugars 58-63 solute carrier family 2 member 1 Homo sapiens 52-57 10715121-6 2000 Intracellular ATP increases GluT1 sugar binding capacity from 1 to 2 mol of 3-O-methylglucose/mol GluT1 and inhibits the release of bound sugar into cytosol. Sugars 34-39 solute carrier family 2 member 1 Homo sapiens 28-33 10715121-6 2000 Intracellular ATP increases GluT1 sugar binding capacity from 1 to 2 mol of 3-O-methylglucose/mol GluT1 and inhibits the release of bound sugar into cytosol. Sugars 34-39 solute carrier family 2 member 1 Homo sapiens 98-103 10715121-6 2000 Intracellular ATP increases GluT1 sugar binding capacity from 1 to 2 mol of 3-O-methylglucose/mol GluT1 and inhibits the release of bound sugar into cytosol. Sugars 138-143 solute carrier family 2 member 1 Homo sapiens 28-33 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 16-21 solute carrier family 2 member 1 Homo sapiens 38-43 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 16-21 solute carrier family 2 member 1 Homo sapiens 125-130 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 68-73 solute carrier family 2 member 1 Homo sapiens 38-43 10715121-8 2000 We propose that sugar uptake involves GluT1-mediated, extracellular sugar translocation into an ATP-dependent cage formed by GluT1 cytoplasmic domains. Sugars 68-73 solute carrier family 2 member 1 Homo sapiens 125-130 9724536-1 1998 Human erythrocyte sugar transport is mediated by the integral membrane protein GLUT1 and is regulated by cytosolic ATP [Carruthers, A., and Helgerson, A. L. (1989) Biochemistry 28, 8337-8346]. Sugars 18-23 solute carrier family 2 member 1 Homo sapiens 79-84 10350483-0 1999 Stop-flow analysis of cooperative interactions between GLUT1 sugar import and export sites. Sugars 61-66 solute carrier family 2 member 1 Homo sapiens 55-60 10350483-7 1999 Low concentrations of maltose, D-glucose, 3-O-methylglucose, and other GLUT1 import-site reactive sugars increase k-1(app) and reduce k1(app) for cytochalasin B interaction with GLUT1. Sugars 98-104 solute carrier family 2 member 1 Homo sapiens 71-76 10350483-7 1999 Low concentrations of maltose, D-glucose, 3-O-methylglucose, and other GLUT1 import-site reactive sugars increase k-1(app) and reduce k1(app) for cytochalasin B interaction with GLUT1. Sugars 98-104 solute carrier family 2 member 1 Homo sapiens 178-183 10350483-10 1999 These results are consistent with a fixed-site carrier mechanism in which GLUT1 simultaneously presents cooperative sugar import and export sites. Sugars 116-121 solute carrier family 2 member 1 Homo sapiens 74-79 10430550-3 1999 Furthermore, from the results of inhibition studies by several sugar analogues including maltose and D-mannose, GLUT1 and/or GLUT3 were suggested to take part in the glucose uptake by oral mucosa. Sugars 63-68 solute carrier family 2 member 1 Homo sapiens 112-117 9724536-9 1998 Feedback control of GLUT1 regulation by ATP was investigated by measuring sugar uptake into erythrocyte ghosts containing or lacking ATP and glycolytic intermediates. Sugars 74-79 solute carrier family 2 member 1 Homo sapiens 20-25 9724536-4 1998 (2) Is ATP-GLUT1 interaction sufficient for sugar transport regulation? Sugars 44-49 solute carrier family 2 member 1 Homo sapiens 11-16 9724536-7 1998 Nucleotide binding and sugar transport experiments undertaken with dimeric and tetrameric forms of GLUT1 indicate that only tetrameric GLUT1 binds and is subject to modulation by ATP. Sugars 23-28 solute carrier family 2 member 1 Homo sapiens 99-104 9724536-7 1998 Nucleotide binding and sugar transport experiments undertaken with dimeric and tetrameric forms of GLUT1 indicate that only tetrameric GLUT1 binds and is subject to modulation by ATP. Sugars 23-28 solute carrier family 2 member 1 Homo sapiens 135-140 9724536-8 1998 Reconstitution experiments indicate that nucleotide and tetrameric GLUT1 are sufficient for ATP modulation of sugar transport. Sugars 110-115 solute carrier family 2 member 1 Homo sapiens 67-72 9401960-2 1997 Inhibitors of protein synthesis stimulate sugar transport in mammalian cells through activation of plasma membrane GLUT1, the housekeeping isoform of the glucose transporter. Sugars 42-47 solute carrier family 2 member 1 Homo sapiens 115-120 9374494-0 1997 Identification of an amino acid residue that lies between the exofacial vestibule and exofacial substrate-binding site of the Glut1 sugar permeation pathway. Sugars 132-137 solute carrier family 2 member 1 Homo sapiens 126-131 7626647-6 1995 GLUT1-mediated erythrocyte sugar uptake, transport inhibition by cytochalasin B, and GLUT1 oligomeric structure are unaffected by exofacial GLUT1 proteolysis. Sugars 27-32 solute carrier family 2 member 1 Homo sapiens 0-5 8855962-0 1996 Regulation of GLUT1-mediated sugar transport by an antiport/uniport switch mechanism. Sugars 29-34 solute carrier family 2 member 1 Homo sapiens 14-19 8756697-3 1996 This suggests that transport asymmetry is either an intrinsic catalytic property of human GLUT1 or that factors present in human erythrocytes affect GLUT1-mediated sugar transport. Sugars 164-169 solute carrier family 2 member 1 Homo sapiens 149-154 8756697-15 1996 We conclude either that human erythrocyte sugar transport is mediated by a carrier mechanism that is fundamentally different from those considered previously or that human erythrocyte-specific factors prevent accurate determination of GLUT1-mediated sugar translocation across the cell membrane. Sugars 250-255 solute carrier family 2 member 1 Homo sapiens 235-240 8756697-16 1996 We suggest that GLUT1-mediated sugar transport in all cells is an intrinsically symmetric process but that intracellular sugar complexation in human red cells prevents accurate determination of transport rates. Sugars 31-36 solute carrier family 2 member 1 Homo sapiens 16-21 7626647-12 1995 Studies with reconstituted purified GLUT1 confirm that the action of trypsin on cytochalasin B binding is direct, show that proteolysis increases the apparent affinity of the sugar efflux site for transported sugars, and suggest that the membrane bilayer stabilizes GLUT1 noncovalent structure and catalytic function following GLUT1 proteolysis. Sugars 175-180 solute carrier family 2 member 1 Homo sapiens 36-41 7626647-12 1995 Studies with reconstituted purified GLUT1 confirm that the action of trypsin on cytochalasin B binding is direct, show that proteolysis increases the apparent affinity of the sugar efflux site for transported sugars, and suggest that the membrane bilayer stabilizes GLUT1 noncovalent structure and catalytic function following GLUT1 proteolysis. Sugars 175-180 solute carrier family 2 member 1 Homo sapiens 266-271 7626647-12 1995 Studies with reconstituted purified GLUT1 confirm that the action of trypsin on cytochalasin B binding is direct, show that proteolysis increases the apparent affinity of the sugar efflux site for transported sugars, and suggest that the membrane bilayer stabilizes GLUT1 noncovalent structure and catalytic function following GLUT1 proteolysis. Sugars 175-180 solute carrier family 2 member 1 Homo sapiens 266-271 7626647-12 1995 Studies with reconstituted purified GLUT1 confirm that the action of trypsin on cytochalasin B binding is direct, show that proteolysis increases the apparent affinity of the sugar efflux site for transported sugars, and suggest that the membrane bilayer stabilizes GLUT1 noncovalent structure and catalytic function following GLUT1 proteolysis. Sugars 209-215 solute carrier family 2 member 1 Homo sapiens 36-41 8150420-2 1994 Activity of the glucose transporting protein (GLUT-1) was measured by determining the first order rate constant for uptake of sorbose, a sugar transported by GLUT-1. Sugars 137-142 solute carrier family 2 member 1 Homo sapiens 46-52 8150420-2 1994 Activity of the glucose transporting protein (GLUT-1) was measured by determining the first order rate constant for uptake of sorbose, a sugar transported by GLUT-1. Sugars 137-142 solute carrier family 2 member 1 Homo sapiens 158-164 8454616-8 1993 Specific immunodepletion of red cell GLUT1 content results in the subsequent loss of reconstitutable protein-mediated sugar transport. Sugars 118-123 solute carrier family 2 member 1 Homo sapiens 37-42 8454616-9 1993 These findings demonstrate that avian erythrocyte sugar transport is mediated by a GLUT1-like sugar transport protein and that sugar transport stimulation by metabolic depletion results from derepression of cell surface sugar transport proteins. Sugars 50-55 solute carrier family 2 member 1 Homo sapiens 83-88 8454616-9 1993 These findings demonstrate that avian erythrocyte sugar transport is mediated by a GLUT1-like sugar transport protein and that sugar transport stimulation by metabolic depletion results from derepression of cell surface sugar transport proteins. Sugars 94-99 solute carrier family 2 member 1 Homo sapiens 83-88 8454616-9 1993 These findings demonstrate that avian erythrocyte sugar transport is mediated by a GLUT1-like sugar transport protein and that sugar transport stimulation by metabolic depletion results from derepression of cell surface sugar transport proteins. Sugars 94-99 solute carrier family 2 member 1 Homo sapiens 83-88 8454616-9 1993 These findings demonstrate that avian erythrocyte sugar transport is mediated by a GLUT1-like sugar transport protein and that sugar transport stimulation by metabolic depletion results from derepression of cell surface sugar transport proteins. Sugars 94-99 solute carrier family 2 member 1 Homo sapiens 83-88 2173694-7 1990 In such pLENGT fibroblasts expressing human GLUT1 protein, however, the absolute values for insulin-stimulated increases in sugar uptake were no different than in control fibroblasts. Sugars 124-129 solute carrier family 2 member 1 Homo sapiens 44-49 8496948-5 1993 A typical time course for a transportable sugar, such as D-glucose, consists of a zero-time displacement, too fast for us to measure, followed by three rapid reactions whose exponential time courses have rate constants of 0.5-100 sec-1 at 20 degrees C. It is suggested that the zero-time displacement represents the initial bimolecular ligand/GLUT1 association. Sugars 42-47 solute carrier family 2 member 1 Homo sapiens 343-348 2209537-4 1990 It is also homologous to the human HepG2 glucose transporter (28.4%), and other sugar carriers from man, rat, yeast and Escherichia coli. Sugars 80-85 solute carrier family 2 member 1 Homo sapiens 35-60