Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo

scientific article

Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode1995PNAS...92.3391L
P356DOI10.1073/PNAS.92.8.3391
P932PMC publication ID42172
P698PubMed publication ID7724572
P5875ResearchGate publication ID15473760

P2093author name stringA A Lilly
G L Hazelbauer
G F Lee
M R Lebert
P2860cites workAssembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathwayQ42016227
Site-directed cross-linking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxisQ43639766
Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonanceQ45107695
Structure and dynamics of transmembrane signaling by the Escherichia coli aspartate receptorQ45189561
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligandQ46177593
Global flexibility in a sensory receptor: a site-directed cross-linking approach.Q50200558
Purification of receptor protein Trg by exploiting a property common to chemotactic transducers of Escherichia coli.Q50885389
Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg.Q54623661
Affinity-chromatographic purification of sixteen cysteine-substituted maltoporin variants: thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli.Q54693315
Structure-function studies of bacterial chemosensors.Q54756014
Conformations of disulfide bridges in proteinsQ68650895
The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand bindingQ27732156
Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptorQ30333668
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.Q30403483
Transient response to chemotactic stimuli in Escherichia coliQ30941323
Strategies for differential sensory responses mediated through the same transmembrane receptorQ34050091
Protein histidine kinases and signal transduction in prokaryotes and eukaryotesQ34330158
Mutations specifically affecting ligand interaction of the Trg chemosensory transducerQ36248287
Ligand occupancy mimicked by single residue substitutions in a receptor: transmembrane signaling induced by mutationQ37169397
Signal transduction pathways involving protein phosphorylation in prokaryotesQ37285258
Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coliQ37626866
Proteins antigenically related to methyl-accepting chemotaxis proteins of Escherichia coli detected in a wide range of bacterial speciesQ39895569
Signal transduction schemes of bacteriaQ40710183
Mutants in transmission of chemotactic signals from two independent receptors of E. coliQ41062642
Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR studyQ41845827
Intrasubunit signal transduction by the aspartate chemoreceptorQ41966631
P433issue8
P407language of work or nameEnglishQ1860
P921main subjecttransmembrane proteinQ424204
chemoreceptor cellQ1069641
P304page(s)3391-3395
P577publication date1995-04-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleTransmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo
P478volume92

Reverse relations

cites work (P2860)
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