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Journal Abstract Search

396 related items for PubMed ID: 17943552

  • 1. Vitamin B12 transport proteins: crystallographic analysis of beta-axial ligand substitutions in cobalamin bound to transcobalamin.
    Wuerges J, Geremia S, Fedosov SN, Randaccio L.
    IUBMB Life; 2007 Nov; 59(11):722-9. PubMed ID: 17943552
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  • 2. Structural basis for mammalian vitamin B12 transport by transcobalamin.
    Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L.
    Proc Natl Acad Sci U S A; 2006 Mar 21; 103(12):4386-91. PubMed ID: 16537422
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  • 4. The binding of vitamin B12 to transcobalamin(II); structural considerations for bioconjugate design--a molecular dynamics study.
    Allis DG, Fairchild TJ, Doyle RP.
    Mol Biosyst; 2010 Sep 21; 6(9):1611-8. PubMed ID: 20379601
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  • 7. Physiological and molecular aspects of cobalamin transport.
    Fedosov SN.
    Subcell Biochem; 2012 Sep 21; 56():347-67. PubMed ID: 22116708
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  • 10. The binding properties of the human receptor for the cellular uptake of vitamin B12.
    Quadros EV, Nakayama Y, Sequeira JM.
    Biochem Biophys Res Commun; 2005 Feb 25; 327(4):1006-10. PubMed ID: 15652495
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  • 14. Structure of the human transcobalamin beta domain in four distinct states.
    Bloch JS, Ruetz M, Kräutler B, Locher KP.
    PLoS One; 2017 Feb 25; 12(9):e0184932. PubMed ID: 28910388
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  • 16. The structure of the rat vitamin B12 transporter TC and its complex with glutathionylcobalamin.
    Bokhove M, Kawamura T, Okumura H, Goto S, Kawano Y, Werner S, Jarczowski F, Klimyuk V, Saito A, Kumasaka T.
    J Biol Chem; 2024 May 25; 300(5):107289. PubMed ID: 38636663
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  • 19. Correction of cobalamin malabsorption in pancreatic insufficiency with a cobalamin analogue that binds with high affinity to R protein but not to intrinsic factor. In vivo evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency.
    Allen RH, Seetharam B, Allen NC, Podell ER, Alpers DH.
    J Clin Invest; 1978 Jun 25; 61(6):1628-34. PubMed ID: 659618
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