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Volumn 11, Issue 3, 2001, Pages 112-115

Ribosome exchange revisited: A mechanism for translation-coupled ribosome detachment from the ER membrane

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MESSENGER RNA; POLYPEPTIDE; TRANSFER RNA;

EID: 0035279056     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(00)01905-X     Document Type: Review
Times cited : (44)

References (27)
  • 3
    • 0017769888 scopus 로고
    • Three-dimensional model of membrane-bound ribosomes obtained by electron microscopy
    • (1977) Nature , vol.269 , pp. 118-122
    • Unwin, P.N.1
  • 4
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1
  • 5
    • 0015549345 scopus 로고
    • Ribosome-membrane interaction: Non-destructive disassembly of rat liver rough microsomes into ribosomal and membranous components
    • (1973) J. Cell Biol. , vol.56 , pp. 206-229
    • Adelman, M.R.1
  • 6
    • 0015924609 scopus 로고
    • In vitro exchange of ribosomal subunits between free and membrane-bound ribosomes
    • (1973) J. Mol. Biol. , vol.74 , pp. 415-438
    • Borgese, D.1
  • 8
    • 0014010396 scopus 로고
    • Synthesis and transfer of amylase in pigeon pancreatic microsomes
    • (1966) J. Biol. Chem. , vol.241 , pp. 1150-1158
    • Redman, C.M.1
  • 9
    • 0014661234 scopus 로고
    • Preferential synthesis of ferritin and albumin by different populations of liver polysomes
    • (1969) Science , vol.164 , pp. 584-585
    • Hicks, S.J.1
  • 11
    • 0016754860 scopus 로고
    • Membrane-bound ribosomes of myeloma cells II. Kinetic studies on the entry of newly made ribosomal subunits into the free and the membrane-bound ribosomal particles
    • (1975) J. Cell Biol. , vol.75 , pp. 16-24
    • Mechler, B.1    Vassalli, P.2
  • 12
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 13
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes II. Reconstitution of functional rough microsomes from heterologous components
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 15
    • 0021014636 scopus 로고
    • Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation
    • (1983) Cell , vol.35 , pp. 677-685
    • Gilmore, R.1    Blobel, G.2
  • 16
    • 0023026186 scopus 로고
    • Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein
    • (1986) J. Cell Biol. , vol.103 , pp. 2253-2261
    • Connolly, T.1    Gilmore, R.2
  • 17
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a non-cytoplasmic aqueous environment at the ER membrane early in translocation
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1
  • 18
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1
  • 19
    • 0030782178 scopus 로고    scopus 로고
    • Membrane protein biogenesis: Regulated complexity at the endoplasmic reticulum
    • (1997) Cell , vol.91 , pp. 575-582
    • Hegde, R.1    Lingappa, V.2
  • 21
    • 0031473345 scopus 로고    scopus 로고
    • Alignment of conduits for the nascent polypeptide chain in the ribosome-sec61 complex
    • (1997) Science , vol.278 , pp. 2123-2126
    • Beckmann, R.1
  • 25
    • 0033634670 scopus 로고    scopus 로고
    • Periodic conformational changes in rRNA: Monitoring the dynamics of translating ribosomes
    • (2000) Mol. Cell , vol.6 , pp. 159-171
    • Polacek, N.1
  • 26


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.