Results 141 to 150 of about 25,429 (197)

Leishmania amazonensis amastigotes invade non-phagocytic cells via highly localized parasite-induced actin remodeling. [PDF]

PLoS Negl Trop Dis
Queiroz-Oliveira T, Rios-Barros LV, Silva-Moreira AL, Santos-Brasil IV, Oliveira-Castro J, Almeida-Silva J, Vannier-Santos MA, Lima-Santos J, Horta MF, Castro-Gomes T.   +9 more
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Macrophage phagocytosis of <i>Coccidioides</i> promotes its differentiation into the parasitic form. [PDF]

mBio
Symington J, Voorhies M, English BC, Dabholkar A, Sil A.   +4 more
europepmc   +1 more source

Integrating Modeling and Microscopy Reveals the Role of Nascent Focal Adhesions in Cell Migration

SALVADORI A, Maini V, Serpelloni M, Raimondi MT, Jacchetti E.   +4 more
europepmc   +1 more source

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Cytochalasin B and the structure of actin gels II. Further evidence for the splitting of F-actin by cytochalasin B

Biochimica Et Biophysica Acta (BBA) - Protein Structure, 1980
Cytochalasin B decreased the flow birefringence and s20,w and increased the extinction angle of actin filaments in salt solutions favoring polymerization of the protein. These changes occurred without a detectable increase in the equilibrium actin monomer concentration determined by a radioassay. These results complement earlier observations indicating
Kosçak Maruyama, John H Hartwig, Thomas P Stossel   +2 more
exaly   +3 more sources

Isolation of cytochalasins A and B fromAscochyta lathyri

Mycotoxin Research, 1992
The possible presence of toxic metabolites in the culture extracts of 24Ascochyta strains, grown on autoclaved wheat, was ascertained by the use of the biological assay on brine shrimps (Artemia salina). Only in the culture extract ofA lathyri, that showed a very high toxicity, the presence of cytochalasins A and B was revealed by tlc,(1)H nmr and fab ...
Vurro M, Zonno MC, Evidente A, Capasso R, Bottaiico A   +4 more
openaire   +4 more sources

Mechanism of action of cytochalasin B on actin

Cell, 1980
Substoichiometric cytochalasin B (CB) inhibits both the rate of actin polymerization and the interaction of actin filaments in solution. The polymerization rate is reduced by inhibition of actin monomer addition to the "barbed" end of the filaments where monomers normally add more rapidly.
S, MacLean-Fletcher, T D, Pollard
openaire   +2 more sources

The structures of cytochalasins A and B

Journal of the Chemical Society C: Organic, 1967
The structures of cytochalasins A and B, metabolites of Helminthosporium dematioideum showing novel effects on mammalian cells, have been determined. Cytochalasin B is identical with phomin. (–)-α-Methyladipic acid is shown to have the R-configuration contrary to a previous assignment; the absolute configurations of the Nupheus alkaloids therefore ...
D. C. Aldridge, J. J. Armstrong, R. N. Speake, W. B. Turner   +3 more
openaire   +1 more source

Cytochalasin B and the structure of actin gels

Journal of Molecular Biology, 1979
Abstract We analyzed the structure of gels formed when macrophage actin-binding protein crosslinks skeletal muscle actin polymers and the effect of the fungal metabolite cytochalasin B on this structure. Measurement of the actin filament length distribution permitted calculation of the critical concentration of crosslinker theoretically required for ...
J H, Hartwig, T P, Stossel
openaire   +2 more sources