Crossref
journal-article
Elsevier BV
Current Opinion in Cell Biology (78)
References
102
Referenced
52
10.1002/cm.20381
/ Cell Motil Cytoskeleton / Dynamics of bacterial cytoskeletal elements by Graumann (2009)10.1146/annurev-genet-102108-134845
/ Annu Rev Genet / The bacterial cytoskeleton by Cabeen (2010)10.1111/j.1574-6976.2011.00316.x
/ FEMS Microbiol Rev / A growing family: the expanding universe of the bacterial cytoskeleton by Ingerson-Mahar (2012)10.1016/j.mib.2011.09.015
/ Curr Opin Microbiol / Self-assembling enzymes and the origins of the cytoskeleton by Barry (2011)10.1016/S0091-679X(10)96002-0
/ Methods Cell Biol / Bacterial TEM: new insights from cryo-microscopy by Pilhofer (2010)10.1038/nature04382
/ Nature / An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria by Scheffel (2006)10.1126/science.1123231
/ Science / Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK by Komeili (2006)10.1111/j.1365-2958.2010.07202.x
/ Mol Microbiol / Loss of the actin-like protein MamK has pleiotropic effects on magnetosome formation and chain assembly in Magnetospirillum gryphiswaldense by Katzmann (2010)10.1111/j.1365-2958.2011.07815.x
/ Mol Microbiol / MamK, a bacterial actin, forms dynamic filaments in vivo that are regulated by the acidic proteins MamJ and LimJ by Draper (2011)10.1111/j.1365-2958.2011.07874.x
/ Mol Microbiol / Magnetosome chains are recruited to cellular division sites and split by asymmetric septation by Katzmann (2011)10.1128/MMBR.00021-10
/ Microbiol Mol Biol Rev / FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one by Erickson (2010)10.1016/j.mib.2011.09.011
/ Curr Opin Microbiol / New(s) to the (Z-)ring by Kirkpatrick (2011)10.1038/sj.emboj.7601895
/ EMBO J / The structure of FtsZ filaments in vivo suggests a force-generating role in cell division by Li (2007)10.1126/science.1154520
/ Science / Reconstitution of contractile FtsZ rings in liposomes by Osawa (2008)10.1038/emboj.2009.277
/ EMBO J / Curved FtsZ protofilaments generate bending forces on liposome membranes by Osawa (2009)10.1111/j.1365-2958.2011.07716.x
/ Mol Microbiol / Inside-out Z rings – constriction with and without GTP hydrolysis by Osawa (2011)10.1073/pnas.1120761109
/ Proc Natl Acad Sci USA / Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations by Hsin (2012){'key': '10.1016/j.ceb.2012.10.019_bib0090', 'first-page': 'e12682', 'article-title': 'In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)', 'volume': '5', 'author': 'Guo', 'year': '2010', 'journal-title': 'PLoS ONE'}
/ PLoS ONE / In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM) by Guo (2010)10.1002/cphc.201100686
/ Chemphyschem / Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism by Biteen (2012)10.1371/journal.pbio.1001389
/ PLoS Biol / 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis by Strauss (2012)10.1016/j.bpj.2012.05.035
/ Biophys J / Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments by Milam (2012)10.1128/JB.182.1.164-170.2000
/ J Bacteriol / Straight and curved conformations of FtsZ are regulated by GTP hydrolysis by Lu (2000)10.1111/j.1365-2958.2005.04522.x
/ Mol Microbiol / Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA by Pichoff (2005)10.1038/emboj.2012.76
/ EMBO J / FtsA forms actin-like protofilaments by Szwedziak (2012)10.1038/emboj.2010.345
/ EMBO J / Large ring polymers align FtsZ polymers for normal septum formation by Gundogdu (2011)10.1038/nrmicro2425
/ Nat Rev Microbiol / The ParMRC system: molecular mechanisms of plasmid segregation by actin-like filaments by Salje (2010)10.1093/emboj/cdf672
/ EMBO J / F-actin-like filaments formed by plasmid segregation protein ParM by van den Ent (2002)10.1038/nsmb1300
/ Nat Struct Mol Biol / The structure of bacterial ParM filaments by Orlova (2007)10.1038/sj.emboj.7601978
/ EMBO J / Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability by Popp (2008)10.1016/j.str.2009.07.008
/ Structure / Structural polymorphism of the ParM filament and dynamic instability by Galkin (2009)10.1016/j.jmb.2012.08.006
/ J Mol Biol / Are ParM filaments polar or bipolar? by Galkin (2012)10.1016/j.jmb.2012.05.019
/ J Mol Biol / Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix by Erickson HP (2012)10.1126/science.1164346
/ Science / Electron cryomicroscopy of E. coli reveals filament bundles involved in plasmid DNA segregation by Salje (2009)10.1038/sj.emboj.7601443
/ EMBO J / DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development by Becker (2006)10.1128/JB.00676-09
/ J Bacteriol / The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation by Polka (2009)10.1016/j.jmb.2010.02.010
/ J Mol Biol / Polymeric structures and dynamic properties of the bacterial actin AlfA by Popp (2010)10.1111/j.1365-2958.2009.06771.x
/ Mol Microbiol / Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A by Derman (2009)10.1074/jbc.M110.203828
/ J Biol Chem / Architecture and assembly of a divergent member of the ParM family of bacterial actin-like proteins by Rivera (2011)10.1101/gad.1546107
/ Genes Dev / Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis by Larsen (2007)10.1111/j.1365-2958.2007.06100.x
/ Mol Microbiol / GTP-dependent polymerization of the tubulin-like RepX replication protein encoded by the pXO1 plasmid of Bacillus anthracis by Anand (2008)10.1073/pnas.1003817107
/ Proc Natl Acad Sci USA / Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition by Ni (2010)10.1073/pnas.1010176107
/ Proc Natl Acad Sci USA / Filament structure of bacterial tubulin homologue TubZ by Aylett (2010)10.1073/pnas.1121546109
/ Proc Natl Acad Sci USA / Tubulin homolog TubZ in a phage-encoded partition system by Oliva (2012)10.1016/j.cell.2012.04.034
/ Cell / A phage tubulin assembles dynamic filaments by an atypical mechanism to center viral DNA within the host cell by Kraemer (2012)10.1073/pnas.1018724108
/ Proc Natl Acad Sci USA / Dynamic instability-driven centering/segregating mechanism in bacteria by Drew (2011)10.1016/j.biocel.2008.08.010
/ Int J Biochem Cell Biol / Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes by Lowe (2008)10.1016/j.mib.2011.09.008
/ Curr Opin Microbiol / ParA ATPases can move and position DNA and subcellular structures by Szardenings (2011)10.1016/j.tim.2012.05.002
/ Trends Microbiol / The ParA/MinD family puts things in their place by Lutkenhaus (2012)10.1128/MMBR.58.3.387-400.1994
/ Microbiol Rev / Do prokaryotes contain microtubules by Bermudes (1994)10.1371/journal.pbio.1001213
/ PLoS Biol / Microtubules in bacteria: ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton by Pilhofer (2011)10.1093/molbev/msm069
/ Mol Biol Evol / Coexistence of tubulins and ftsZ in different Prosthecobacter species by Pilhofer (2007)10.1128/JB.01797-07
/ J Bacteriol / Characterization and evolution of cell division and cell wall synthesis genes in the bacterial phyla Verrucomicrobia, Lentisphaerae, Chlamydiae, and Planctomycetes and phylogenetic comparison with rRNA genes by Pilhofer (2008)10.1073/pnas.012516899
/ Proc Natl Acad Sci USA / Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter by Jenkins (2002)10.1073/pnas.0502859102
/ Proc Natl Acad Sci USA / Structure of bacterial tubulin BtubA/B: evidence for horizontal gene transfer by Schlieper (2005)10.1074/jbc.M111.230094
/ J Biol Chem / Bacterial tubulin distinct loop sequences and primitive assembly properties support its origin from a eukaryotic tubulin ancestor by Martin-Galiano (2011)10.1083/jcb.200410027
/ J Cell Biol / In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB by Sontag (2005)10.1093/nar/gkm836
/ Nucleic Acids Res / Characterization of bacterial operons consisting of two tubulins and a kinesin-like gene by the novel Two-Step Gene Walking method by Pilhofer (2007)10.1016/j.chom.2010.06.012
/ Cell Host Microbe / Type VI secretion: not just for pathogenesis anymore by Jani (2010)10.1038/nature10846
/ Nature / Type VI secretion requires a dynamic contractile phage tail-like structure by Basler (2012)10.1038/emboj.2008.269
/ EMBO J / Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion by Bonemann (2009)10.1074/jbc.M111.253377
/ J Biol Chem / Molecular basis for the unique role of the AAA(+) chaperone ClpV in type VI protein secretion by Pietrosiuk (2011)10.1126/science.1222901
/ Science / Type 6 secretion dynamics within and between bacterial cells by Basler (2012)10.1016/j.mib.2008.01.006
/ Curr Opin Microbiol / Type VI secretion: a beginner's guide by Bingle (2008)10.1073/pnas.0813360106
/ Proc Natl Acad Sci USA / Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin by Leiman (2009)10.1038/emboj.2009.358
/ EMBO J / Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus by Kuhn (2010)10.1111/j.1365-2958.2011.07629.x
/ Mol Microbiol / BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape by Koch (2011)10.1038/ncb2087
/ Nat Cell Biol / The metabolic enzyme CTP synthase forms cytoskeletal filaments by Ingerson-Mahar (2010)10.1111/j.1365-2958.2006.05355.x
/ Mol Microbiol / Multiple large filament bundles observed in Caulobacter crescentus by electron cryotomography by Briegel (2006)10.1016/S0092-8674(03)00935-8
/ Cell / The bacterial cytoskeleton: an intermediate filament-like function in cell shape by Ausmees (2003)10.1038/emboj.2009.61
/ EMBO J / Bacterial cell curvature through mechanical control of cell growth by Cabeen (2009)10.1101/gad.1795509
/ Genes Dev / Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin by Charbon (2009)10.1371/journal.pone.0008855
/ PLoS ONE / Dynamics of the bacterial intermediate filament crescentin in vitro and in vivo by Esue (2010)10.1002/cm.20505
/ Cytoskeleton (Hoboken) / The domain organization of the bacterial intermediate filament-like protein crescentin is important for assembly and function by Cabeen (2011)10.1111/j.1365-2958.2008.06473.x
/ Mol Microbiol / Intermediate filament-like proteins in bacteria and a cytoskeletal function in Streptomyces by Bagchi (2008)10.1371/journal.ppat.1000669
/ PLoS Pathog / A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori by Waidner (2009)10.1074/jbc.M110.154427
/ J Biol Chem / Phosphorylation of a novel cytoskeletal protein (RsmP) regulates rod-shaped morphology in Corynebacterium glutamicum by Fiuza (2010)10.1128/JB.00231-11
/ J Bacteriol / Helicobacter pylori possesses four coiled-coil-rich proteins that form extended filamentous structures and control cell shape and motility by Specht (2011)10.1016/j.molcel.2008.05.030
/ Mol Cell / ATP-driven self-assembly of a morphogenetic protein in Bacillus subtilis by Ramamurthi (2008)10.1016/j.cell.2011.07.029
/ Cell / Peptidoglycan remodeling and conversion of an inner membrane into an outer membrane during sporulation by Tocheva (2011)10.1111/j.1365-2958.2007.05910.x
/ Mol Microbiol / The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes by Divakaruni (2007)10.1038/emboj.2011.358
/ EMBO J / A widespread family of bacterial cell wall assembly proteins by Kawai (2011)10.1016/S0092-8674(01)00287-2
/ Cell / Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis by Jones (2001)10.1093/emboj/cdg504
/ EMBO J / Dysfunctional MreB inhibits chromosome segregation in Escherichia coli by Kruse (2003)10.1073/pnas.1232225100
/ Proc Natl Acad Sci USA / Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles by Shih (2003)10.1111/j.1365-2958.2003.03936.x
/ Mol Microbiol / MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus by Figge (2004)10.1016/j.bbrc.2011.03.062
/ Biochem Biophys Res Commun / Long helical filaments are not seen encircling cells in electron cryotomograms of rod-shaped bacteria by Swulius (2011)10.1126/science.1203466
/ Science / Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria by Dominguez-Escobar (2011)10.1126/science.1203285
/ Science / Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis by Garner (2011)10.1073/pnas.1108999108
/ Proc Natl Acad Sci USA / The bacterial actin MreB rotates, and rotation depends on cell-wall assembly by van Teeffelen (2011)10.1128/JB.00505-12
/ J Bacteriol / The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag by Swulius (2012)10.1016/j.molcel.2011.07.008
/ Mol Cell / Direct membrane binding by bacterial actin MreB by Salje (2011)10.1016/j.cell.2008.07.016
/ Cell / A self-associating protein critical for chromosome attachment, division, and polar organization in caulobacter by Ebersbach (2008)10.1016/j.cell.2008.07.015
/ Cell / A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole by Bowman (2008)10.1111/j.1365-2958.2010.07088.x
/ Mol Microbiol / Caulobacter PopZ forms a polar subdomain dictating sequential changes in pole composition and function by Bowman (2010)10.1016/j.jsb.2006.04.010
/ J Struct Biol / Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography by Seybert (2006)10.1111/j.1365-2958.2006.05113.x
/ Mol Microbiol / Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility by Henderson (2006)10.1128/JB.01823-08
/ J Bacteriol / Cytoskeletal asymmetrical dumbbell structure of a gliding mycoplasma, Mycoplasma gallisepticum, revealed by negative-staining electron microscopy by Nakane (2009)10.1146/annurev.micro.112408.134116
/ Annu Rev Microbiol / Unique centipede mechanism of Mycoplasma gliding by Miyata (2010)10.1186/1745-6150-5-33
/ Biol Direct / Two new families of the FtsZ-tubulin protein superfamily implicated in membrane remodeling in diverse bacteria and archaea by Makarova (2010)10.1186/1745-6150-7-10
/ Biol Direct / Archaeal origin of tubulin by Yutin (2012)10.1016/j.jmb.2009.11.019
/ J Mol Biol / Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells by Iancu (2010)10.1016/j.str.2010.10.005
/ Structure / In vivo assembly of an archaeal virus studied with whole-cell electron cryotomography by Fu (2010)
Dates
Type | When |
---|---|
Created | 12 years, 8 months ago (Nov. 23, 2012, 3:30 p.m.) |
Deposited | 1 year, 3 months ago (May 1, 2024, 5:51 p.m.) |
Indexed | 1 month, 2 weeks ago (July 1, 2025, 7:13 p.m.) |
Issued | 12 years, 6 months ago (Feb. 1, 2013) |
Published | 12 years, 6 months ago (Feb. 1, 2013) |
Published Print | 12 years, 6 months ago (Feb. 1, 2013) |
Funders
3
Howard Hughes Medical Institute, NIH
10.13039/100000011
Howard Hughes Medical InstituteRegion: Americas
pri (Research institutes and centers)
Labels
2
- Howard Hughes Medical Institute Inc
- HHMI
Awards
1
- R01 GM094800B
Center for Environmental Biology Interactions at Caltech
Bayerische Forschungsstiftung
10.13039/501100002745
Region: Europe
gov (Local government)
Labels
1
- Bavarian Research Foundation
@article{Pilhofer_2013, title={The bacterial cytoskeleton: more than twisted filaments}, volume={25}, ISSN={0955-0674}, url={http://dx.doi.org/10.1016/j.ceb.2012.10.019}, DOI={10.1016/j.ceb.2012.10.019}, number={1}, journal={Current Opinion in Cell Biology}, publisher={Elsevier BV}, author={Pilhofer, Martin and Jensen, Grant J}, year={2013}, month=feb, pages={125–133} }