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Evolution of the cytoskeleton
scientific article
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instance of
scholarly article
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review article
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stated in
Europe PubMed Central
title
Evolution of the cytoskeleton
(English)
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main subject
cytoskeleton
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author name string
Harold P Erickson
series ordinal
1
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language of work or name
English
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publication date
July 2007
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published in
BioEssays
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volume
29
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page(s)
668-77
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issue
7
0 references
cites work
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27 September 2017
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Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of Escherichia coli FtsA.
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Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter.
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Bacterial actins? An evolutionary perspective
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A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure
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27 September 2017
Tubulin and FtsZ form a distinct family of GTPases
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27 September 2017
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27 September 2017
Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin
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27 September 2017
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27 September 2017
Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
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Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein
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27 September 2017
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27 September 2017
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Systematic mutational analysis of the yeast beta-tubulin gene
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27 September 2017
Guanine nucleotide-dependent assembly of FtsZ into filaments
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27 September 2017
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28 November 2018
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28 November 2018
Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota.
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28 November 2018
Entamoeba histolytica encodes a highly divergent beta-tubulin.
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The real 'domains' of life
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reference URL
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based on heuristic
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The essential bacterial cell-division protein FtsZ is a GTPase
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/17563102
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based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1002/BIES.20601
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2907628
OpenCitations bibliographic resource ID
2907628
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2907628
PMCID
2630885
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2907628
PubMed ID
17563102
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2907628
ResearchGate publication ID
6274114
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