메뉴 건너뛰기




Volumn 381, Issue 4, 2009, Pages 712-716

Structural and functional studies on the stalk of the transferrin receptor

Author keywords

Iron release; Receptor stalk; Single particle electron microscopy; Transferrin; Transferrin receptor

Indexed keywords

CARRIER PROTEIN; FERRIC ION; IRON BINDING PROTEIN; TRANSFERRIN RECEPTOR;

EID: 62649088857     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.02.133     Document Type: Article
Times cited : (9)

References (16)
  • 1
    • 0000154631 scopus 로고
    • Structure and reactivity of transferrins
    • Baker E.N. Structure and reactivity of transferrins. Adv. Inorg. Chem. 41 (1994) 389-463
    • (1994) Adv. Inorg. Chem. , vol.41 , pp. 389-463
    • Baker, E.N.1
  • 2
    • 0037388042 scopus 로고    scopus 로고
    • Dealing with iron: common structural principles in proteins that transport iron and heme
    • Baker H.M., Anderson B.F., and Baker E.N. Dealing with iron: common structural principles in proteins that transport iron and heme. Proc. Natl. Acad. Sci. USA 100 (2003) 3579-3583
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3579-3583
    • Baker, H.M.1    Anderson, B.F.2    Baker, E.N.3
  • 3
  • 5
    • 0023282177 scopus 로고
    • Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site
    • Jing S.Q., and Trowbridge I.S. Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site. EMBO J. 6 (1987) 327-331
    • (1987) EMBO J. , vol.6 , pp. 327-331
    • Jing, S.Q.1    Trowbridge, I.S.2
  • 6
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng Y., Zak O., Aisen P., Harrison S.C., and Walz T. Structure of the human transferrin receptor-transferrin complex. Cell 116 (2004) 565-576
    • (2004) Cell , vol.116 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 7
    • 42449146663 scopus 로고    scopus 로고
    • Monolayer purification-a rapid method for isolating protein complexes for single particle electron microscopy
    • Kelly D.F., Dukovski D., and Walz T. Monolayer purification-a rapid method for isolating protein complexes for single particle electron microscopy. Proc. Natl. Acad. Sci. USA 105 (2008) 4703-4708
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4703-4708
    • Kelly, D.F.1    Dukovski, D.2    Walz, T.3
  • 8
    • 0019891047 scopus 로고
    • The effect of salts on the kinetics of iron release from N-terminal and C-terminal monoferric transferrins
    • Baldwin D.A., and de Sousa D.M. The effect of salts on the kinetics of iron release from N-terminal and C-terminal monoferric transferrins. Biochem. Biophys. Res. Commun. 99 (1981) 1101-1107
    • (1981) Biochem. Biophys. Res. Commun. , vol.99 , pp. 1101-1107
    • Baldwin, D.A.1    de Sousa, D.M.2
  • 9
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • Grigorieff N. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 157 (2007) 117-125
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 10
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., and Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386 (1997) 88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 11
    • 0027181635 scopus 로고
    • The anion requirement for iron release from transferrin is preserved in the receptor-transferrin complex
    • Egan T.J., Zak O., and Aisen P. The anion requirement for iron release from transferrin is preserved in the receptor-transferrin complex. Biochemistry 32 (1993) 8162-8167
    • (1993) Biochemistry , vol.32 , pp. 8162-8167
    • Egan, T.J.1    Zak, O.2    Aisen, P.3
  • 12
    • 0027976177 scopus 로고
    • Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor
    • Rutledge E.A., Root B.J., Lucas J.J., and Enns C.A. Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor. Blood 83 (1994) 580-586
    • (1994) Blood , vol.83 , pp. 580-586
    • Rutledge, E.A.1    Root, B.J.2    Lucas, J.J.3    Enns, C.A.4
  • 13
    • 0026069823 scopus 로고
    • Receptor-modulated iron release from transferrin: differential effects on N- and C-terminal sites
    • Bali P.K., and Aisen P. Receptor-modulated iron release from transferrin: differential effects on N- and C-terminal sites. Biochemistry 30 (1991) 9947-9952
    • (1991) Biochemistry , vol.30 , pp. 9947-9952
    • Bali, P.K.1    Aisen, P.2
  • 14
    • 0018671415 scopus 로고
    • Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects
    • Leibman A., and Aisen P. Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects. Blood 53 (1979) 1058-1065
    • (1979) Blood , vol.53 , pp. 1058-1065
    • Leibman, A.1    Aisen, P.2
  • 15
    • 0018849946 scopus 로고
    • The distribution of iron between the metal-binding sites of transferrin in human serum
    • Williams J., and Moreton K. The distribution of iron between the metal-binding sites of transferrin in human serum. Biochem. J. 185 (1980) 483-488
    • (1980) Biochem. J. , vol.185 , pp. 483-488
    • Williams, J.1    Moreton, K.2
  • 16
    • 0142095049 scopus 로고    scopus 로고
    • Iron release from transferrin, its C-lobe, and their complexes with transferrin receptor: presence of N-lobe accelerates release from C-lobe at endosomal pH
    • Zak O., and Aisen P. Iron release from transferrin, its C-lobe, and their complexes with transferrin receptor: presence of N-lobe accelerates release from C-lobe at endosomal pH. Biochemistry 42 (2003) 12330-12334
    • (2003) Biochemistry , vol.42 , pp. 12330-12334
    • Zak, O.1    Aisen, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.