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MARC Record from marc_columbia

Record ID marc_columbia/Columbia-extract-20221130-003.mrc:399453836:3236
Source marc_columbia
Download Link /show-records/marc_columbia/Columbia-extract-20221130-003.mrc:399453836:3236?format=raw

LEADER: 03236mam a2200397 a 4500
001 1429426
005 20220602033231.0
008 931018s1993 enka b 101 0 eng d
010 $agb 93055993
015 $aGB93-55993
020 $a0412550601
035 $a(OCoLC)ocm29254551
035 $9AHU5701CU
035 $a(NNC)1429426
035 $a1429426
040 $aUKM$cUKM$dIAY
082 04 $a574.19245$220
245 00 $aMolecular chaperones :$ba discussion meeting /$cedited by R.J. Ellis and R.A. Laskey and G.H. Lorimer.
260 $aLondon :$bChapman & Hall, on behalf of the Royal Society,$c1993.
300 $aix, 121 pages :$billustrations ;$c30 cm
336 $atext$2rdacontent
337 $aunmediated$2rdamedia
338 $avolume$2rdacarrier
500 $a"This volume results from the Royal Society discussion meeting on molecular chaperones held Sept. [23-24], 1992"--P. 4 of cover.
504 $aIncludes bibliographical references and index.
505 2 $a1. The general concept of molecular chaperones / R. J. Ellis -- 2. The role of nucleoplasmin in chromatin assembly and disassembly / R. A. Laskey, A. D. Mills, A. Philpott, G. H. Leno, S. M. Dilworth and C. Dingwall -- 3. The Escherichia coli chaperones involved in DNA replication / M. Zylicz -- 4. The role of heat-shock proteins in thermotolerance / D. A. Parsell, J. Taulien and S. Lindquist -- 5. What does protein refolding in vitro tell us about protein folding in the cell? / R. Jaenicke -- 6. Chaperonins and protein folding: unity and disunity of mechanisms / G. H. Lorimer, M. J. Todd and P. V. Viitanen -- 7. A chaperonin from a thermophilic bacterium, Thermus thermophilus / M. Yoshida, N. Ishii, E. Muneyuki and H. Taguchi -- 8. Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1 / A. L. Horwich and K. Willison -- 9. Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells / W. J. Welch.
505 0 $a10. The role of molecular chaperones in protein transport into the endoplasmic reticulum / T. Dierks, P. Klappa, H. Wiech and R. Zimmerman -- 11. Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export / S. J. S. Hardy and L. L. Randall -- 12. Roles of molecular chaperones in protein targeting to mitochondria / W. Neupert and N. Pfanner -- 13. Molecular chaperones and the immune response / D. Young, E. Roman, C. Moreno, R. O'Brien and W. Born -- 14. Tumour suppressor genes and molecular chaperones / D. P. Lane, C. Midgley and T. Hupp.
653 0 $aOrganisms$aProteins
650 0 $aProtein binding$vCongresses.$0http://id.loc.gov/authorities/subjects/sh2010108691
650 0 $aCooperative binding (Biochemistry)$vCongresses.
650 0 $aLigand binding (Biochemistry)$vCongresses.
700 1 $aEllis, R. J.$q(Reginald John),$d1935-$0http://id.loc.gov/authorities/names/n84018141
700 1 $aLaskey, R. A.$0http://id.loc.gov/authorities/names/n85342217
700 1 $aLorimer, G. H.$q(George H.)$0http://id.loc.gov/authorities/names/n93803439
710 2 $aRoyal Society (Great Britain).$bDiscussion Meeting$d(1992 September 23-24 :$cLondon, England)
852 00 $boff,bio$hQP551$i.M614 1993g