ArticleJournal of bacteriology2003
Electron microscopic analysis of membrane assemblies formed by the bacterial chemotaxis receptor Tsr.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 67 citations in OpenAlex.
- Alternative Architecture of theBiomolecules · 2021Article
- Spatial Restrictions in Chemotaxis Signaling Arrays: A Role for Chemoreceptor Flexible Hinges across Bacterial Diversity.International journal of molecular sciences · 2019Article
- Baseplate variability ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Ectopic Neo-Formed Intracellular Membranes inBiomolecules · 2018Review
- Flexible Hinges in Bacterial Chemoreceptors.Journal of bacteriology · 2018Article
- His-Tag-Mediated Dimerization of Chemoreceptors Leads to Assembly of Functional Nanoarrays.Biochemistry · 2017Article
- Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Journal of molecular biology · 2015Article
- Preformed Soluble Chemoreceptor Trimers That Mimic Cellular Assembly States and Activate CheA Autophosphorylation.Biochemistry · 2015Article
- The role of membrane-mediated interactions in the assembly and architecture of chemoreceptor lattices.PLoS computational biology · 2014Article
- New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography.Biochemistry · 2014Article
- Chemoreceptors and flagellar motors are subterminally located in close proximity at the two cell poles in spirochetes.Journal of bacteriology · 2011Article
- Chemotaxis kinase CheA is activated by three neighbouring chemoreceptor dimers as effectively as by receptor clusters.Molecular microbiology · 2011Article
- A dynamic-signaling-team model for chemotaxis receptors in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Electron cryotomography.Cold Spring Harbor perspectives in biology · 2010Review
- Article
- Kinase-active signaling complexes of bacterial chemoreceptors do not contain proposed receptor-receptor contacts observed in crystal structures.Biochemistry · 2010Article
- Universal architecture of bacterial chemoreceptor arrays.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex.Biochemistry · 2009Article
- Polar chemoreceptor clustering by coupled trimers of dimers.Biophysical journal · 2009Article
- Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The serine receptor (Tsr) from Escherichia coli is representative of a large family of transmembrane receptor proteins that mediate bacterial chemotaxis by influencing cell motility through signal transduction pathways. Tsr and other chemotaxis receptors form patches in the inner membrane that are often localized at the poles of the bacteria. In an effort to understand the structural constraints that dictate the packing of receptors in the plane of the membrane, we have used electron microscopy to examine ordered assemblies of Tsr in membrane extracts isolated from cells engineered to overproduce the receptor. Three types of assemblies were observed: ring-like "micelles" with a radial arrangement of receptor subunits, two-dimensional crystalline arrays with approximate hexagonal symmetry, and "zippers," which are receptor bilayers that result from the antiparallel interdigitation of cytoplasmic domains. The registration among Tsr molecules in the micelle and zipper assemblies was sufficient for identification of the receptor domains and for determination of their contributions to the total receptor length. The overall result of this analysis is compatible with an atomic model of the receptor dimer that was constructed primarily from the X-ray crystal structures of the periplasmic and cytoplasmic domains. Significantly, the micelle and zipper structures were also observed in fixed, cryosectioned cells expressing the Tsr receptor at high abundance, suggesting that the modes of Tsr assembly found in vitro are relevant to the situation in the cell.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.