-
2
-
-
0033032592
-
Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
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The combined deletion of the trigger factor and DnaK genes causes synthetic lethality in E. coli. Newly synthesised polypeptides will interact first with trigger factor and then may associate with DnaK. It is hypothesised that the fraction of polypeptides interacting with trigger factor is in the same range as for DnaK (5-10% of the total)
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Teter S.A., Houry W.A., Ang D., Tradler T., Rockabrand D., Fischer G., Blum P., Georgopoulos C., Hartl F.U. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell. 97:1999;755-765. The combined deletion of the trigger factor and DnaK genes causes synthetic lethality in E. coli. Newly synthesised polypeptides will interact first with trigger factor and then may associate with DnaK. It is hypothesised that the fraction of polypeptides interacting with trigger factor is in the same range as for DnaK (5-10% of the total).
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Cell
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Teter, S.A.1
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Ang, D.3
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Rockabrand, D.5
Fischer, G.6
Blum, P.7
Georgopoulos, C.8
Hartl, F.U.9
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3
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0033549770
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Trigger factor and DnaK cooperate in folding of newly synthesised proteins
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This paper reports the synthetic lethality of a trigger factor/DnaK gene double deletion in E. coli. Trigger factor was assigned to act co-translationally. A slight increase in the protein fraction interacting with GroEL occurred in trigger-factor-negative cells. The fraction of newly synthesised polypeptides targeted to DnaK was estimated to be 9-18% in wild-type and 26-39% in trigger-factor-negative cells
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Deuerling E., Schulze-Specking A., Tomoyasu T., Mogk A., Bukau B. Trigger factor and DnaK cooperate in folding of newly synthesised proteins. Nature. 400:1999;693-696. This paper reports the synthetic lethality of a trigger factor/DnaK gene double deletion in E. coli. Trigger factor was assigned to act co-translationally. A slight increase in the protein fraction interacting with GroEL occurred in trigger-factor-negative cells. The fraction of newly synthesised polypeptides targeted to DnaK was estimated to be 9-18% in wild-type and 26-39% in trigger-factor-negative cells.
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Nature
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Deuerling, E.1
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4
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0031554922
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Modular structure of the trigger factor required for high activity in protein
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Zarnt T., Tradler T., Stoller G., Scholz C., Schmid F.X., Fischer G. Modular structure of the trigger factor required for high activity in protein. J Mol Biol. 271:1997;827-837.
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Lyon W.R., Gibson C.M., Caparon M.G. Processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17:1998;6263-6275.
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6
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0033597878
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Oxidative protein folding is driven by the electron transport system
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The source of oxidising equivalents for the oxidative protein folding in the periplasm of E. coli catalysed by the DsbA/DsbB system is localised in the electron transport system. Functional differences between anaerobic conditions (with menaquinone serving as the electron acceptor) and aerobic conditions (with the electron acceptor ubiquinone) are shown
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Bader M., Muse W., Ballou D.P., Gassner C., Bardwell J.C.A. Oxidative protein folding is driven by the electron transport system. Cell. 98:1999;217-227. The source of oxidising equivalents for the oxidative protein folding in the periplasm of E. coli catalysed by the DsbA/DsbB system is localised in the electron transport system. Functional differences between anaerobic conditions (with menaquinone serving as the electron acceptor) and aerobic conditions (with the electron acceptor ubiquinone) are shown.
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Cell
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Bader, M.1
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2+-dependent structural changes in C-type mannose-binding proteins. Biochemistry. 37:1998;17965-17976.
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Biochemistry
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Ng, K.K.-S.1
Park-Snyder, S.2
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0033534719
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Two isoforms of protein disulfide isomerase alter the dimerisation status of E2A proteins by a redox mechanism
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Markus M., Benezra R. Two isoforms of protein disulfide isomerase alter the dimerisation status of E2A proteins by a redox mechanism. J Biol Chem. 274:1999;1040-1049.
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J Biol Chem
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Markus, M.1
Benezra, R.2
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10
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0033555681
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A protein folding intermediate of ribonuclease T-1 characterised at high resolution by 1D and 2D real-time NMR spectroscopy
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The consequences of an incorrect prolyl bond for the structure of a polypeptide chain in various folding states were investigated by real-time NMR spectroscopy of a ribonuclease T1 variant containing a single proline residue. Cis/trans isomerisation of the Try38-Pro39 moiety affects not only amide protons in close proximity to proline, but also those throughout the entire protein
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Balbach J., Steegborn C., Schindler T., Schmid F.X. A protein folding intermediate of ribonuclease T-1 characterised at high resolution by 1D and 2D real-time NMR spectroscopy. J Mol Biol. 285:1999;829-842. The consequences of an incorrect prolyl bond for the structure of a polypeptide chain in various folding states were investigated by real-time NMR spectroscopy of a ribonuclease T1 variant containing a single proline residue. Cis/trans isomerisation of the Try38-Pro39 moiety affects not only amide protons in close proximity to proline, but also those throughout the entire protein.
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J Mol Biol
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Balbach, J.1
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0032776419
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Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerisation by human cytosolic cyclophilin (Cyp18)
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Golbik R., Fischer G., Fersht A.R. Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerisation by human cytosolic cyclophilin (Cyp18). Protein Sci. 8:1999;1505-1514.
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Protein Sci
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Golbik, R.1
Fischer, G.2
Fersht, A.R.3
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12
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0033569502
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Folding and association of the antibody domain CH3: Prolyl isomerisation precedes dimerisation
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Thies M.J.W., Mayer J., Augustine J.G., Frederick C.A., Lilie H., Buchner J. Folding and association of the antibody domain CH3: prolyl isomerisation precedes dimerisation. J Mol Biol. 293:1999;67-79.
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J Mol Biol
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Thies, M.J.W.1
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13
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2442761708
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The protein disulphide-isomerase family: Unravelling a string of folds
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This paper provides an overview of the PDI family and the relation between the structural organisation and catalytic function of these enzymes. It focuses on the properties of mammalian PDI
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Ferrari D.M., Soling H.D. The protein disulphide-isomerase family: unravelling a string of folds. Biochem J. 339:1999;1-10. This paper provides an overview of the PDI family and the relation between the structural organisation and catalytic function of these enzymes. It focuses on the properties of mammalian PDI.
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Biochem J
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Ferrari, D.M.1
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14
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0033548441
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Identification of protein-disulfide isomerase activity in fibronectin
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Langenbach K.J., Sottile J. Identification of protein-disulfide isomerase activity in fibronectin. J Biol Chem. 274:1999;7032-7038.
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J Biol Chem
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Richarme G. Protein-disulfide isomerase activity of elongation factor EF-Tu. Biochem Biophys Res Commun. 252:1998;156-161.
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Functional properties of the two redox-active sites in yeast protein disulfide isomerase in vitro and in vivo
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Westphal V., Darby N.J., Winther J.R. Functional properties of the two redox-active sites in yeast protein disulfide isomerase in vitro and in vivo. J Mol Biol. 286:1999;1229-1239.
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J Mol Biol
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Westphal, V.1
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0033028924
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Identifying and characterising a second structural domain of protein disulfide isomerase
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Darby N.J., van Straaten M., Penka E., Vincentelli R., Kemmink J. Identifying and characterising a second structural domain of protein disulfide isomerase. FEBS Lett. 448:1999;167-172.
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Darby, N.J.1
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18
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0032897837
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The structure in solution of the b domain of protein disulfide isomerase
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Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M., Darby N.J. The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR. 13:1999;357-368.
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J Biomol NMR
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Kemmink, J.1
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Nilges, M.6
Darby, N.J.7
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19
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0032481380
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The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
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Klappa P., Ruddock L.W., Darby N.J., Freedman R.B. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 7:1998;927-935.
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Klappa, P.1
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0033525640
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Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
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Hennecke J., Sebbel P., Glockshuber R. Random circular permutation of DsbA reveals segments that are essential for protein folding and stability. J Mol Biol. 286:1999;1197-1215.
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J Mol Biol
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Hennecke, J.1
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On the role of the cis-proline residue in the active site of DsbA
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Charonnier J.B., Belin P., Moutiez M., Stura E.A., Quemeneur E. On the role of the cis-proline residue in the active site of DsbA. Protein Sci. 8:1999;96-105.
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22
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0033564233
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Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalysed protein folding in the bacterial periplasm
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DsbA deficiency was complemented by secreted thioredoxin variants with different redox potentials. The authors clarified that the in vivo function of DsbA in the periplasm of E. coli depends directly on the redox potential of the final oxidant of the polypeptides
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Jonda S., Huber-Wunderlich M., Glockshuber R., Mossner E. Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalysed protein folding in the bacterial periplasm. EMBO J. 18:1999;3271-3281. DsbA deficiency was complemented by secreted thioredoxin variants with different redox potentials. The authors clarified that the in vivo function of DsbA in the periplasm of E. coli depends directly on the redox potential of the final oxidant of the polypeptides.
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EMBO J
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Jonda, S.1
Huber-Wunderlich, M.2
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0033057483
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The role of immunophilins in mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis
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This paper reports a link between a fatal progressive neuroregenerative disease targeting neurons and Cyp18. Apparently, PPIases are required to help cells survive oxidative stress. The ability of Cyp18 to perform protection was shown to depend strictly on its catalytic function because the R55A Cyp18 variant, which is nearly devoid of PPIase activity, was not able to substitute for wild-type Cyp18
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Lee J-P., Palfrey H.C., Bindokas V.P., Ghadge G.D., Ma L., Miller R.J., Roos R.P. The role of immunophilins in mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA. 96:1999;3251-3256. This paper reports a link between a fatal progressive neuroregenerative disease targeting neurons and Cyp18. Apparently, PPIases are required to help cells survive oxidative stress. The ability of Cyp18 to perform protection was shown to depend strictly on its catalytic function because the R55A Cyp18 variant, which is nearly devoid of PPIase activity, was not able to substitute for wild-type Cyp18.
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Proc Natl Acad Sci USA
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Lee, J.-P.1
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Ma, L.5
Miller, R.J.6
Roos, R.P.7
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Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins
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Human T cell cyclophilin 18 binds to the thiol-specific antioxidant protein Aop1 and stimulates its activity
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Jaschke A., Mi H.F., Tropschug M. Human T cell cyclophilin 18 binds to the thiol-specific antioxidant protein Aop1 and stimulates its activity. J Mol Biol. 277:1998;763-769.
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Doyle V., Virji S., Crompton M. Evidence that cyclophilin-A protects cells against oxidative stress. Biochem J. 341:1999;127-132.
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0033524943
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Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
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The crystal structure of a unphosphorylated TβR-I fragment-FKBP12 complex represents the first example of a putative protein substrate bound to FKBP12. It was found that the location of FKBP12 adjacent to the regulatory GS region of the receptor chain might impede the approach of a TβR-II kinase domain. Leu196 of TβR-I occupies the binding region of the pipecolinyl ring of FK506 in their respective complexes
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Huse M., Chen Y.G., Massagué J., Kuriyan J. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell. 96:1999;425-436. The crystal structure of a unphosphorylated TβR-I fragment-FKBP12 complex represents the first example of a putative protein substrate bound to FKBP12. It was found that the location of FKBP12 adjacent to the regulatory GS region of the receptor chain might impede the approach of a TβR-II kinase domain. Leu196 of TβR-I occupies the binding region of the pipecolinyl ring of FK506 in their respective complexes.
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The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
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Binding experiments demonstrated the specific interaction of the hyperphosphorylated τ-protein and Pin1. Interacting regions of both proteins were localised. Functional restoration of hyperphosphorylated τ-protein can be performed by Pin1, but not cyclophilin, in a PPIase-activity-dependent manner
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Lu P.J., Wulf G., Zhou X.Z., Davies P., Lu K.P. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature. 399:1999;784-788. Binding experiments demonstrated the specific interaction of the hyperphosphorylated τ-protein and Pin1. Interacting regions of both proteins were localised. Functional restoration of hyperphosphorylated τ-protein can be performed by Pin1, but not cyclophilin, in a PPIase-activity-dependent manner.
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Nature
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2+ regulation of interactions between endoplasmic reticulum chaperones. J Biol Chem. 274:1999;6203-6211.
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The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
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Koivunen P., Pirneskoski A., Karvonen P., Ljung J., Helaakoski T., Notbohm H., Kivirikko K.I. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide. EMBO J. 18:1999;65-74.
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Saito T., Niwa Y., Ashida H., Tanaka K., Kawamukai M., Matsuda H., Nakagawa T. Expression of a gene for cyclophilin which contains an amino-terminal endoplasmic reticulum-targeting signal. Plant Cell Physiol. 40:1999;77-87.
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Kurek I., Aviezer K., Erel N., Herman E., Breiman A. The wheat peptidyl prolyl cis-trans-isomerase FKBP77 is heat induced and developmentally regulated. Plant Physiol. 119:1999;693-703.
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Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J-U. Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase. FEBS Lett. 446:1999;278-282.
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Rulten S., Thorpe J., Kay J. Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases. Biochem Biophys Res Commun. 259:1999;557-562.
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