| P2093 | author name string | Costa Georgopoulos | |
| | France Keppel | |
| | Monique Rychner | |
| P2860 | cites work | Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 | Q25938983 |
| | Detection of specific sequences among DNA fragments separated by gel electrophoresis | Q25939003 |
| | Interplay of structure and disorder in cochaperonin mobile loops | Q27733719 |
| | Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage | Q27741079 |
| | An efficient recombination system for chromosome engineering in Escherichia coli | Q29615038 |
| | Genetic analysis of bacteriophage-encoded cochaperonins | Q34090783 |
| | Host participation in bacteriophage lambda head assembly | Q34699367 |
| | Cleavage of head and tail proteins during bacteriophage T5 assembly: Selective host involvement in the cleavage of a tail protein | Q34699415 |
| | The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures | Q36174913 |
| | Conserved sequence motifs in bacterial and bacteriophage chaperonins | Q36718389 |
| | Genomic polymorphism in the T-even bacteriophages. | Q40793103 |
| | Role of the major heat shock proteins as molecular chaperones | Q40800614 |
| | Mutational analysis of the phage T4 morphogenetic 31 gene, whose product interacts with the Escherichia coli GroEL protein | Q42636037 |
| | Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31. | Q42638510 |
| | Purification and properties of the groES morphogenetic protein of Escherichia coli | Q45075329 |
| | In vitro insertional mutagenesis with a selectable DNA fragment | Q48387759 |
| | A new set of useful cloning and expression vectors derived from pBlueScript. | Q54162320 |
| | Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. | Q54635587 |
| | Characterization of a functionally important mobile domain of GroES. | Q54654548 |
| | Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction | Q56896714 |
| | The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding | Q58007398 |
| | The crystal structure of the GroES co-chaperonin at 2.8 Å resolution | Q59072776 |
| P433 | issue | 9 | |
| P921 | main subject | Escherichia coli | Q25419 |
| | bacteriophage | Q165028 |
| P304 | page(s) | 893-898 | |
| P577 | publication date | 2002-08-16 | |
| P1433 | published in | EMBO Reports | Q5323356 |
| P1476 | title | Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein | |
| P478 | volume | 3 | |