| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/S0076-6879(07)23013-7 |
| P698 | PubMed publication ID | 17609137 |
| P2093 | author name string | Gerald L Hazelbauer | |
| Wing-Cheung Lai | |||
| P2860 | cites work | Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm | Q24644906 |
| Transmembrane signaling in bacterial chemoreceptors | Q28362211 | ||
| Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor | Q30333668 | ||
| Analysis of protein structure in intact cells: crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor | Q30426545 | ||
| Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping | Q33973489 | ||
| The helical hydrophobic moment: a measure of the amphiphilicity of a helix | Q34056948 | ||
| Disulphide bridges in globular proteins | Q34284906 | ||
| Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli | Q34303463 | ||
| Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo | Q34441018 | ||
| Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer. | Q34513727 | ||
| Catalysis of disulfide bond formation and isomerization in Escherichia coli | Q34545621 | ||
| Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm | Q35951953 | ||
| Quantitative approaches to utilizing mutational analysis and disulfide crosslinking for modeling a transmembrane domain | Q36279185 | ||
| Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues | Q36519382 | ||
| Crosslinking snapshots of bacterial chemoreceptor squads | Q36604915 | ||
| Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo | Q37258332 | ||
| The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding | Q37583326 | ||
| Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity | Q41986533 | ||
| Signalling substitutions in the periplasmic domain of chemoreceptor Trg induce or reduce helical sliding in the transmembrane domain | Q43636725 | ||
| Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex. | Q53859237 | ||
| The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. | Q54563918 | ||
| Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. | Q54646876 | ||
| 11 Diamide: An oxidant probe for thiols | Q71999701 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | transmembrane protein | Q424204 |
| chemoreceptor cell | Q1069641 | ||
| P304 | page(s) | 299-316 | |
| P577 | publication date | 2007-01-01 | |
| P1433 | published in | Methods in Enzymology | Q2076903 |
| P1476 | title | Analyzing transmembrane chemoreceptors using in vivo disulfide formation between introduced cysteines. | |
| P478 | volume | 423 |
| Q37503508 | Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor Aer |
| Q36890483 | Determination of the physiological dimer interface of the PhoQ sensor domain |
| Q35139646 | Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain |
| Q35041385 | Dynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system. |
| Q44830698 | Oxygen and redox sensing by two-component systems that regulate behavioral responses: behavioral assays and structural studies of aer using in vivo disulfide cross-linking |
| Q28492377 | The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex |
| Q35598682 | The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers |
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