| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M011194200 |
| P698 | PubMed publication ID | 11278858 |
| P2093 | author name string | Luirink J | |
| Muller M | |||
| Oudega B | |||
| Harms N | |||
| de Cock H | |||
| Koningstein G | |||
| Dontje W | |||
| P2860 | cites work | The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity | Q28354278 |
| Selection for a periplasmic factor improving phage display and functional periplasmic expression | Q32066800 | ||
| The Sec system | Q33538582 | ||
| Trigger factor depletion or overproduction causes defective cell division but does not block protein export | Q34083081 | ||
| Protein folding in the bacterial periplasm | Q35621918 | ||
| Lipid involvement in protein translocation in Escherichia coli | Q37910873 | ||
| E. coli mutant pleiotropically defective in the export of secreted proteins | Q38356083 | ||
| Role of lipopolysaccharide in assembly of Escherichia coli outer membrane proteins OmpA, OmpC, and OmpF. | Q40344335 | ||
| Requirements for the membrane insertion of signal-anchor type proteins | Q41828297 | ||
| Folding of a bacterial outer membrane protein during passage through the periplasm | Q41924765 | ||
| The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain | Q42068408 | ||
| The Escherichia coli SRP and SecB targeting pathways converge at the translocon | Q42643547 | ||
| Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export | Q45226310 | ||
| OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis | Q48081854 | ||
| Cloning and sequencing of the gene for the DNA-binding 17K protein of Escherichia coli | Q48319278 | ||
| A new set of useful cloning and expression vectors derived from pBlueScript. | Q54162320 | ||
| A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. | Q54592701 | ||
| Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein | Q54682002 | ||
| In vitro trimerization of outer membrane protein PhoE. | Q54717934 | ||
| Periplasmic accumulation of truncated forms of outer-membrane PhoE protein of Escherichia coli K-12. | Q54779308 | ||
| The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro | Q56896185 | ||
| The Escherichia coli K88 periplasmic chaperone FaeE forms a heterotrimeric complex with the minor fimbrial component FaeH and with the minor fimbrial component Fael | Q64450172 | ||
| Lipid-synthesis-dependent biosynthesis (or assembly) of major outer-membrane proteins of Escherichia coli | Q70181641 | ||
| The receptor of bacteriophage lambda: evidence for a biosynthesis dependent on lipid synthesis | Q70565801 | ||
| Identification of the prolyl isomerase domain of Escherichia coli trigger factor | Q71104060 | ||
| Detergent-induced folding of the outer-membrane protein PhoE, a pore protein induced by phosphate limitation | Q72389662 | ||
| Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor | Q77789106 | ||
| Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein | Q77892751 | ||
| Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli | Q77936213 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins | Q78151353 | ||
| P433 | issue | 22 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular chaperones | Q422496 |
| membrane protein | Q423042 | ||
| P304 | page(s) | 18804-18811 | |
| P577 | publication date | 2001-03-05 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane | |
| P478 | volume | 276 |
| Q36343565 | Advances in understanding bacterial outer-membrane biogenesis |
| Q99350128 | Affinity of Skp to OmpC revealed by single-molecule detection |
| Q53507814 | Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System. |
| Q35937989 | Assembling the mitochondrial outer membrane |
| Q30159573 | Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif |
| Q30155422 | Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex |
| Q35130958 | Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. |
| Q30157280 | Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence |
| Q36012621 | Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli |
| Q35004080 | Detecting folding intermediates of a protein as it passes through the bacterial translocation channel |
| Q37019529 | Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins |
| Q33985391 | Dynamic interaction of the sec translocon with the chaperone PpiD |
| Q30152747 | Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins |
| Q47105500 | Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding |
| Q30164981 | Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide |
| Q38020872 | Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies |
| Q37858328 | Integrating protein homeostasis strategies in prokaryotes |
| Q54359354 | Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism. |
| Q36174616 | Interactions between folding factors and bacterial outer membrane proteins |
| Q30152721 | Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM. |
| Q92668069 | Lipid trafficking across the Gram-negative cell envelope |
| Q38194733 | Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date? |
| Q30157374 | Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. |
| Q35082920 | Membrane protein assembly in vivo |
| Q42198344 | Misfolding of a bacterial autotransporter |
| Q34188699 | OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain |
| Q30155248 | Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pylori |
| Q30156004 | PpiD is a player in the network of periplasmic chaperones in Escherichia coli |
| Q37369375 | Protein disorder is positively correlated with gene expression in Escherichia coli |
| Q94503608 | Proteomic profiling of Serratia marcescens by high-resolution mass spectrometry |
| Q36248731 | Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes |
| Q30160137 | Refolding of Escherichia coli outer membrane protein F in detergent creates LPS-free trimers and asymmetric dimers |
| Q37124929 | Role for Skp in LptD assembly in Escherichia coli |
| Q34740748 | Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis |
| Q30155536 | Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain. |
| Q39562461 | Skp is a multivalent chaperone of outer-membrane proteins |
| Q37776043 | Structural biology of periplasmic chaperones. |
| Q54499897 | Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. |
| Q30155481 | The Bam machine: a molecular cooper |
| Q34399330 | The Sec protein-translocation pathway. |
| Q38206834 | The Sec translocon mediated protein transport in prokaryotes and eukaryotes. |
| Q42662047 | The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation. |
| Q30157376 | The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains |
| Q38189243 | The lipopolysaccharide export pathway in Escherichia coli: structure, organization and regulated assembly of the Lpt machinery |
| Q47723207 | The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization |
| Q33214226 | The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition |
| Q38596996 | The β-Barrel Assembly Machinery Complex |
| Q30155419 | Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membrane |
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