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49 results

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Page 1
Engineering amino acid uptake or catabolism promotes CAR T-cell adaption to the tumor environment.
Panetti S, McJannett N, Fultang L, Booth S, Gneo L, Scarpa U, Smith C, Vardon A, Vettore L, Whalley C, Pan Y, Várnai C, Endou H, Barlow J, Tennant D, Beggs A, Mussai F, De Santo C. Panetti S, et al. Blood Adv. 2023 May 9;7(9):1754-1761. doi: 10.1182/bloodadvances.2022008272. Blood Adv. 2023. PMID: 36521029 Free PMC article.
We demonstrate that T cells can be re-engineered to express SLC7A5 or SLC7A11 transmembrane amino acid transporters alongside CARs. Transporter modifications increase CAR T-cell proliferation under low tryptophan or cystine conditions with no loss of C …
We demonstrate that T cells can be re-engineered to express SLC7A5 or SLC7A11 transmembrane amino acid transporters alongside …
Substrate recognition and ATPase activity of the E. coli cysteine/cystine ABC transporter YecSC-FliY.
Sabrialabed S, Yang JG, Yariv E, Ben-Tal N, Lewinson O. Sabrialabed S, et al. J Biol Chem. 2020 Apr 17;295(16):5245-5256. doi: 10.1074/jbc.RA119.012063. Epub 2020 Mar 6. J Biol Chem. 2020. PMID: 32144203 Free PMC article.
We found that the substrate-binding protein FliY binds l-cystine, l-cysteine, and d-cysteine with micromolar affinities. However, binding of the l- and d-enantiomers induced different conformational changes of FliY, where the l- enantiomer-substrate-binding p …
We found that the substrate-binding protein FliY binds l-cystine, l-cysteine, and d-cysteine with micromolar affinities …
Regulation of SLC7A11 as an unconventional checkpoint in tumorigenesis through ferroptosis.
Su Z, Liu Y, Wang L, Gu W. Su Z, et al. Genes Dis. 2024 Mar 2;12(1):101254. doi: 10.1016/j.gendis.2024.101254. eCollection 2025 Jan. Genes Dis. 2024. PMID: 39569390 Free PMC article. Review.
It is well accepted that ferroptosis, an iron-dependent programmed cell death, acts as a new type of tumor suppression mechanism tightly linked with numerous metabolic pathways. SLC7A11 is a transmembrane cystine/glutamate transporter protein that plays a vit …
It is well accepted that ferroptosis, an iron-dependent programmed cell death, acts as a new type of tumor suppression mechanism tightly lin …
xCT/SLC7A11 antiporter function inhibits HIV-1 infection.
Rabinowitz J, Sharifi HJ, Martin H, Marchese A, Robek M, Shi B, Mongin AA, de Noronha CMC. Rabinowitz J, et al. Virology. 2021 Apr;556:149-160. doi: 10.1016/j.virol.2021.01.008. Epub 2021 Jan 20. Virology. 2021. PMID: 33631414 Free PMC article.
Among the tens of genes controlled directly by Nrf2 in macrophages, we found that xCT/SLC7A11, a 12-transmembrane, cystine-glutamate antiporter promotes antiretroviral activity. We show here that depletion of xCT mRNA increases HIV-1 infection. Reconstitution …
Among the tens of genes controlled directly by Nrf2 in macrophages, we found that xCT/SLC7A11, a 12-transmembrane, cystine-glu …
New aspects of the pathogenesis of cystinosis.
Kalatzis V, Antignac C. Kalatzis V, et al. Pediatr Nephrol. 2003 Mar;18(3):207-15. doi: 10.1007/s00467-003-1077-5. Epub 2003 Feb 27. Pediatr Nephrol. 2003. PMID: 12644911 Review.
Cystinosis is a lysosomal transport disorder characterized by an intra-lysosomal accumulation of cystine, the disulfide of the amino acid cysteine. ...Cystinosin is the lysosomal cystine transporter and its activity is H(+)-driven. A mouse model …
Cystinosis is a lysosomal transport disorder characterized by an intra-lysosomal accumulation of cystine, the disulfide of the …
Amino acid transporters as tetraspanin TM4SF5 binding partners.
Jung JW, Kim JE, Kim E, Lee JW. Jung JW, et al. Exp Mol Med. 2020 Jan;52(1):7-14. doi: 10.1038/s12276-019-0363-7. Epub 2020 Jan 20. Exp Mol Med. 2020. PMID: 31956272 Free PMC article. Review.
Transmembrane 4 L6 family member 5 (TM4SF5) is a tetraspanin that has four transmembrane domains and can be N-glycosylated and palmitoylated. These posttranslational modifications of TM4SF5 enable homophilic or heterophilic binding to diverse membrane prot …
Transmembrane 4 L6 family member 5 (TM4SF5) is a tetraspanin that has four transmembrane domains and can be N-glycosylated and …
Molecular basis of prostaglandin E(2) reuptake by organic anion transporter PGT.
Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. Zhu Z, et al. Nat Commun. 2025 Dec 1;17(1):315. doi: 10.1038/s41467-025-67025-8. Nat Commun. 2025. PMID: 41326388 Free PMC article.
Beyond the canonical MFS-fold, PGT harbours a cystine-rich extracellular segment that incorporates a Kazal-like domain crucial for PGT localization and activity. ...This dimerization would likely increase the mobility of the extracellular region and induces a profou …
Beyond the canonical MFS-fold, PGT harbours a cystine-rich extracellular segment that incorporates a Kazal-like domain crucial for PG …
Erythrocytic metabolism of ATLX-0199: An agent that increases minute ventilation.
Krasinkiewicz JM, Hubbard D, Perez de Guzman N, Masters A, Zhao Y, Gaston H, Gaston B. Krasinkiewicz JM, et al. Biochem Biophys Res Commun. 2023 Nov 5;680:171-176. doi: 10.1016/j.bbrc.2023.09.030. Epub 2023 Sep 15. Biochem Biophys Res Commun. 2023. PMID: 37741264 Free PMC article.
CSNO binding inhibits these channels in the carotid body, leading to increased minute ventilation in vivo. However, only the l-isomer is active in vivo because it requires the l-amino acid transporter (LAT) for transmembrane transport. In rodents and d …
CSNO binding inhibits these channels in the carotid body, leading to increased minute ventilation in vivo. However, only the l-isomer is …
SLC7A11 as a Gateway of Metabolic Perturbation and Ferroptosis Vulnerability in Cancer.
Lee J, Roh JL. Lee J, et al. Antioxidants (Basel). 2022 Dec 11;11(12):2444. doi: 10.3390/antiox11122444. Antioxidants (Basel). 2022. PMID: 36552652 Free PMC article. Review.
SLC7A11 is a cell transmembrane protein composing the light chain of system xc(-), transporting extracellular cystine into cells for cysteine production and GSH biosynthesis. ...A better understanding of cysteine and SLC7A11 functions regulating and interacti …
SLC7A11 is a cell transmembrane protein composing the light chain of system xc(-), transporting extracellular cystine i …
Cystinosin, the protein defective in cystinosis, is a H(+)-driven lysosomal cystine transporter.
Kalatzis V, Cherqui S, Antignac C, Gasnier B. Kalatzis V, et al. EMBO J. 2001 Nov 1;20(21):5940-9. doi: 10.1093/emboj/20.21.5940. EMBO J. 2001. PMID: 11689434 Free PMC article.
Cystinosis is an inherited lysosomal storage disease characterized by defective transport of cystine out of lysosomes. However, the causative gene, CTNS, encodes a seven transmembrane domain lysosomal protein, cystinosin, unrelated to known transporters …
Cystinosis is an inherited lysosomal storage disease characterized by defective transport of cystine out of lysosomes. However …
49 results