LEADER 02097nam  2200577 a 450 
001 9910967836603321
005 20251116181734.0
010   $a1-61668-459-3
035   $a(CKB)2550000001042478
035   $a(EBL)3020246
035   $a(SSID)ssj0000883473
035   $a(PQKBManifestationID)11485374
035   $a(PQKBTitleCode)TC0000883473
035   $a(PQKBWorkID)10924762
035   $a(PQKB)10812390
035   $a(MiAaPQ)EBC3020246
035   $a(Au-PeEL)EBL3020246
035   $a(CaPaEBR)ebr10676407
035   $a(OCoLC)834603851
035   $a(BIP)28923363
035   $a(EXLCZ)992550000001042478
100   $a20100203d2010      uy         0
101 0 $aeng
135   $aur|n|---|||||
181   $ctxt
182   $cc
183   $acr
200 10$aMolecular chaperones of the endoplasmic reticulum /$fMartin Schro?der
205   $a1st ed.
210   $aNew York $cNova Science Publishers, Inc.$dc2010
215   $a1 online resource (136 p.)
225 1 $aProtein science and engineering
300   $aDescription based upon print version of record.
311 08$a1-61668-173-X 
320   $aIncludes bibliographical references (p. [71]-119) and index.
327   $aPhysicochemical principles governing protein folding -- The ER -- Molecular chaperones of the ER.
330   $aAn important function of the endoplasmic reticulum is the folding of newly synthesised polypeptide chains. Several general and specialized chaperones operate in the endoplasmic reticulum to assist protein folding. This book reviews our current knowledge of molecular chaperones of the ER.
410  0$aProtein science and engineering.
606   $aMolecular chaperones
606   $aEndoplasmic reticulum
615  0$aMolecular chaperones.
615  0$aEndoplasmic reticulum.
676   $a571.6/5
700   $aSchro?der$b Martin$f1954-$01867391
801  0$bMiAaPQ
801  1$bMiAaPQ
801  2$bMiAaPQ
906   $aBOOK
912   $a9910967836603321
996   $aMolecular chaperones of the endoplasmic reticulum$94474933
997   $aUNINA