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Cell, v.93 no.5, 1998년, pp.863 - 873
Vainberg, Irina E (Department of Biochemistry, New York University Medical Center, New York, New York 10016, USA) , Lewis, Sally A (Department of Biochemistry, New York University Medical Center, New York, New York 10016, USA) , Rommelaere, Heidi (Flanders Interuniversity Institute for Biotechnology, University of Ghent, B-9000 Ghent, Belgium) , Ampe, Christophe (Flanders Interuniversity Institute for Biotechnology, University of Ghent, B-9000 Ghent, Belgium) , Vandekerckhove, Joel (Flanders Interuniversity Institute for Biotechnology, University of Ghent, B-9000 Ghent, Belgium) , Klein, Hannah L (Department of Biochemistry, New York University Medical Center, New York, New York 10016, USA) , Cowan, Nicholas J (Department of Biochemistry, New York University Medical Center, New York, New York 10016, USA)
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AbstractWe describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin. Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it. Deletion of the gene encoding a prefoldin subunit in S. cerevisiae re...
Yeast Amberg 11 1275 1996 10.1002/yea.320111307 Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction
Proc. Natl. Acad. Sci. USA Baumann 93 6726 1996 10.1073/pnas.93.13.6726 An archaebacterial homologue of the essential eubacterial cell division protein FtsZ
Science Beckmann 248 850 1990 10.1126/science.2188360 Interaction of Hsp70 with newly synthesized proteins
Trends Cell Biol. Bukau 6 480 1996 10.1016/0962-8924(96)84946-4 Growing up in a dangerous environment
Proc. Natl. Acad. Sci. USA Chen 91 9111 1994 10.1073/pnas.91.19.9111 Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo
J. Cell Biol. Chowdhury 118 561 1992 10.1083/jcb.118.3.561 Osmotic stress and the yeast cytoskeleton
Philos. Trans. R. Soc. Lond. B Biol. Sci. Doolittle 349 235 1995 10.1098/rstb.1995.0107 The origins and evolution of eukaryotic proteins
FASEB J. Ellis 10 20 1996 10.1096/fasebj.10.1.8566542 Protein folding in the cell
Cell Farr 89 927 1997 10.1016/S0092-8674(00)80278-0 Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms
Protein Sci. Fenton 6 743 1997 10.1002/pro.5560060401 GroEL-mediated protein folding
Science Frydman 272 1497 1996 10.1126/science.272.5267.1497 Principles of chaperone-assisted protein folding
EMBO J. Frydman 11 4767 1992 10.1002/j.1460-2075.1992.tb05582.x Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
Cell Gao 69 1043 1992 10.1016/0092-8674(92)90622-J A cytoplasmic chaperonin that catalyzes β-actin folding
J. Cell Biol. Gao 125 989 1994 10.1083/jcb.125.5.989 A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin
Mol. Biol. Cell Geiser 8 1035 1997 10.1091/mbc.8.6.1035 Saccharyomyces cerevisiae genes required in the absence of the CIN 8-encoded spindle motor act in functionally diverse pathways
EMBO J. Geissler 17 952 1998 10.1093/emboj/17.4.952 A novel protein complex promoting formation of functional α- and γ-tubulin
Nature Hartl 381 571 1996 10.1038/381571a0 Molecular chaperones in cellular protein folding
J. Cell Biol. Hayes 132 255 1996 10.1083/jcb.132.3.255 Roles of molecular chaperones in protein degradation
Mol. Cell. Biol. Hoyt 10 223 1990 Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes
Annu. Rev. Genet. Huffaker 21 259 1987 10.1146/annurev.ge.21.120187.001355 Genetic analysis of the yeast cytoskeleton
Cell Johnson 90 201 1997 10.1016/S0092-8674(00)80327-X Protein folding in vivo
Trends Biochem. Sci. Kim 19 543 1994 10.1016/0968-0004(94)90058-2 Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide binding domains
J. Biol. Chem. Komar 272 10646 1997 10.1074/jbc.272.16.10646 Cotranslational folding of globin
Curr. Biol. Kubota 4 89 1994 10.1016/S0960-9822(94)00024-2 Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
Trends Cell Biol. Lewis 7 479 1997 10.1016/S0962-8924(97)01168-9 The α- and β-tubulin folding pathways
FASEB J. Lorimer 10 5 1996 10.1096/fasebj.10.1.8566548 A quantitative assessment of the role of chaperonin proteins in protein folding in vivo
Nature Martin 366 228 1993 10.1038/366228a0 The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
Mol. Cell. Biol. Melki 14 2895 1993 Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
J. Cell Biol. Melki 122 1301 1993 10.1083/jcb.122.6.1301 Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin
Nature Netzer 388 343 1997 10.1038/41024 Recombination of protein domains facilitated by co-translational folding in eukaryotes
Protein Sci. Norcum 5 1366 1996 10.1002/pro.5560050715 Novel isolation method and structural stability of a eukaryotic chaperonin
Cell Novick 40 405 1985 10.1016/0092-8674(85)90154-0 Phenotypic analysis of temperature-sensitive yeast actin mutants
Proc. Natl. Acad. Sci. USA Rommelaere 90 11975 1993 10.1073/pnas.90.24.11975 The eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits
Cell Roseman 87 241 1996 10.1016/S0092-8674(00)81342-2 The chaperonin ATPase cycle
Nature Rye 388 792 1997 10.1038/42047 Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
Science Schatz 271 1519 1996 10.1126/science.271.5255.1519 Common principles of protein translocation
Sherman 1983 Methods in Yeast Genetics
Genetics Stearns 124 251 1990 10.1093/genetics/124.2.251 Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function
Proc. Natl. Acad. Sci. USA Sternlicht 90 9422 1993 10.1073/pnas.90.20.9422 The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo
Nature Tian 375 250 1995 10.1038/375250a0 Specificity in chaperonin-mediated protein folding
Cell. Tian 86 287 1996 10.1016/S0092-8674(00)80100-2 Pathway leading to correctly folded β-tubulin
Science Todd 265 659 1994 10.1126/science.7913555 Dynamics of the chaperonin ATPase cycle
Nature Trent 354 490 1992 10.1038/354490a0 A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
Mol. Cell. Biol. Ursic 11 2629 1991 The yeast homolog to mouse TCP-1 affects microtubule-mediated processes
Mol. Biol. Cell. Ursic 5 1065 1994 10.1091/mbc.5.10.1065 The essential yeast TCP1 protein affects actin and microtubules
Proc. Natl. Acad. Sci. USA Vinh 91 9116 1994 10.1073/pnas.91.19.9116 A yeast TCP-1-like protein is required for actin formation in vivo
Cell Weissman 78 693 1994 10.1016/0092-8674(94)90533-9 GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
Cell Weissman 83 577 1995 10.1016/0092-8674(95)90098-5 Mechanism of GroEL action
Proc. Natl. Acad. Sci. USA Woese 87 4576 1990 10.1073/pnas.87.12.4576 Towards a natural system of organisms
Nature Xu 388 735 1997 10.1038/41944 The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
Nature Yaffe 358 245 1992 10.1038/358245a0 TCP1 complex is a molecular chaperone in tubulin biogenesis
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