| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/S0076-6879(07)23002-2 |
| P8608 | Fatcat ID | release_kwtobyfb3nhg3e7xvbhm37z7my |
| P932 | PMC publication ID | 2896970 |
| P698 | PubMed publication ID | 17609126 |
| P2093 | author name string | Susan L Gloor | |
| Joseph J Falke | |||
| Scott L Butler | |||
| Randal B Bass | |||
| Stephen A Chervitz | |||
| P2860 | cites work | Crosslinking snapshots of bacterial chemoreceptor squads | Q36604915 |
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| A piston model for transmembrane signaling of the aspartate receptor | Q41689679 | ||
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| Transmembrane signaling by the aspartate receptor: engineered disulfides reveal static regions of the subunit interface | Q42169879 | ||
| Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor | Q42736552 | ||
| Adaptation mechanism of the aspartate receptor: electrostatics of the adaptation subdomain play a key role in modulating kinase activity | Q42738440 | ||
| Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor | Q45235964 | ||
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| Adaptational modification and ligand occupancy have opposite effects on positioning of the transmembrane signalling helix of a chemoreceptor. | Q54458668 | ||
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| Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor | Q30333668 | ||
| Structure of a bacterial sensory receptor. A site-directed sulfhydryl study. | Q30403483 | ||
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| Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor | Q33932303 | ||
| Detection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning | Q33962309 | ||
| Lock On/Off Disulfides Identify the Transmembrane Signaling Helix of the Aspartate Receptor | Q33973426 | ||
| The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes | Q33973438 | ||
| Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping | Q33973489 | ||
| Structure of a conserved receptor domain that regulates kinase activity: the cytoplasmic domain of bacterial taxis receptors | Q33988248 | ||
| Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies | Q33988261 | ||
| Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor | Q33997083 | ||
| Collaborative signaling by mixed chemoreceptor teams in Escherichia coli | Q34068339 | ||
| Acetylcholine receptor channel structure probed in cysteine-substitution mutants. | Q34250941 | ||
| The HAMP domain structure implies helix rotation in transmembrane signaling | Q34564404 | ||
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | transmembrane protein | Q424204 |
| chemotaxis | Q658145 | ||
| P304 | page(s) | 25-51 | |
| P577 | publication date | 2007-01-01 | |
| P1433 | published in | Methods in Enzymology | Q2076903 |
| P1476 | title | Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis. | |
| P478 | volume | 423 |
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| Q42162963 | Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: a disulfide mapping study |
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