| scholarly article | Q13442814 |
| P50 | author | Ulrich Weininger | Q28050819 |
| Jochen Balbach | Q28050821 | ||
| Roman P Jakob | Q58231292 | ||
| Franz X. Schmid | Q62056389 | ||
| Michael Kovermann | Q90215544 | ||
| P2860 | cites work | NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein | Q27626801 |
| Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana | Q27639234 | ||
| Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins | Q27639946 | ||
| Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding | Q27641101 | ||
| The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues | Q27647943 | ||
| Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulins | Q27654271 | ||
| NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function | Q27654594 | ||
| The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer | Q27732612 | ||
| Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent | Q27739821 | ||
| Using NMRView to visualize and analyze the NMR spectra of macromolecules | Q27860567 | ||
| AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR | Q27860778 | ||
| NMRPipe: a multidimensional spectral processing system based on UNIX pipes | Q27860859 | ||
| MOLMOL: a program for display and analysis of macromolecular structures | Q27860873 | ||
| Protein backbone angle restraints from searching a database for chemical shift and sequence homology | Q27861108 | ||
| Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides | Q28267643 | ||
| The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity | Q28354278 | ||
| SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities | Q28485735 | ||
| Primary structure effects on peptide group hydrogen exchange | Q29614750 | ||
| Intrinsic dynamics of an enzyme underlies catalysis | Q29616406 | ||
| Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants | Q29617228 | ||
| ARIA: automated NOE assignment and NMR structure calculation | Q29620311 | ||
| Membrane protein folding on the example of outer membrane protein A of Escherichia coli. | Q30164479 | ||
| The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. | Q30176862 | ||
| Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases | Q30320453 | ||
| The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase. | Q30321311 | ||
| Stability of protein structure and hydrophobic interaction. | Q30403599 | ||
| A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases | Q33507146 | ||
| Role of the Escherichia coli SurA protein in stationary-phase survival. | Q33739792 | ||
| A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli | Q33889129 | ||
| Enzyme dynamics during catalysis | Q34115429 | ||
| Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli | Q34124391 | ||
| The structural basis of protein targeting and translocation in bacteria. | Q34261907 | ||
| SurA assists the folding of Escherichia coli outer membrane proteins | Q35604222 | ||
| surA, an Escherichia coli gene essential for survival in stationary phase | Q36254871 | ||
| Catalysis of protein folding by parvulin | Q36889249 | ||
| The disulfide bond formation (Dsb) system | Q37136271 | ||
| Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide binding | Q38297173 | ||
| Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli | Q39505348 | ||
| Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions | Q40488942 | ||
| Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. | Q40818804 | ||
| Backbone and side-chain dynamics of residues in a partially folded beta-sheet peptide from platelet factor-4. | Q42845736 | ||
| Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases. | Q43095107 | ||
| High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. | Q43655302 | ||
| Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme | Q43677989 | ||
| SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins | Q44025126 | ||
| The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities | Q44088884 | ||
| Energetic coupling between native-state prolyl isomerization and conformational protein folding | Q44913453 | ||
| Molecular determinants of a native-state prolyl isomerization | Q44984446 | ||
| The dual histidine motif in the active site of Pin1 has a structural rather than catalytic role | Q46324112 | ||
| Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins | Q47344205 | ||
| Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin | Q48079055 | ||
| Kinetic Analysis of Cyclophilin-Catalyzed Prolyl Cis/Trans Isomerization by Dynamic NMR Spectroscopy | Q52326716 | ||
| Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine. | Q53751977 | ||
| The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon. | Q54423305 | ||
| Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding. | Q54444088 | ||
| A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. | Q54635381 | ||
| Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases. | Q54677445 | ||
| The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro | Q56896185 | ||
| Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds | Q72858649 | ||
| A TROSY CPMG sequence for characterizing chemical exchange in large proteins | Q73289769 | ||
| The mode of action of peptidyl prolyl cis/trans isomerases in vivo: binding vs. catalysis | Q74582891 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| Periplasmic chaperones--new structural and functional insights | Q78507732 | ||
| NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis | Q82725784 | ||
| P433 | issue | 1 | |
| P304 | page(s) | 6-18 | |
| P577 | publication date | 2010-01-01 | |
| P1433 | published in | Protein Science | Q7251445 |
| P1476 | title | The prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activity | |
| P478 | volume | 19 |
| Q39244663 | An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding |
| Q35055492 | Dimeric Structure of the Bacterial Extracellular Foldase PrsA. |
| Q33985391 | Dynamic interaction of the sec translocon with the chaperone PpiD |
| Q35046397 | Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence |
| Q34297821 | Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets |
| Q36062775 | NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase |
| Q30156004 | PpiD is a player in the network of periplasmic chaperones in Escherichia coli |
| Q38940176 | Protein folding in the cell envelope of Escherichia coli. |
| Q64119172 | Structural Analysis of the 42 kDa Parvulin of |
| Q47827642 | Structure-Function Analysis of the Periplasmic Escherichia coli Cyclophilin PpiA in Relation to Biofilm Formation. |
| Q30155481 | The Bam machine: a molecular cooper |
| Q37723502 | The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity |
| Q42145472 | The Remorin C-terminal Anchor was shaped by convergent evolution among membrane binding domains |
| Q35065149 | The virulence factor PEB4 (Cj0596) and the periplasmic protein Cj1289 are two structurally related SurA-like chaperones in the human pathogen Campylobacter jejuni |
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