eukaryotic cells Search Results


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    Rabbit IgG Monoclonal antibody for Q53EL6 detection Tested positive for WB IHC IF FC in Human Mouse
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    Sino Biological eukaryotic cells
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    ATCC eukaryotic cell lines
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    GBF eukaryotic cells
    Model for the evolution of the Sec7-domain protein family. Based on the phylogenetic analysis of the <t>eukaryotic</t> Sec7-domain proteins, we propose a model for the evolution of the seven groups in fungi, animals, and plants, from a single Sec7 domain progenitor
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    GenScript eukaryotic cells
    Model for the evolution of the Sec7-domain protein family. Based on the phylogenetic analysis of the <t>eukaryotic</t> Sec7-domain proteins, we propose a model for the evolution of the seven groups in fungi, animals, and plants, from a single Sec7 domain progenitor
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    Interchim eukaryotic cells
    Model for the evolution of the Sec7-domain protein family. Based on the phylogenetic analysis of the <t>eukaryotic</t> Sec7-domain proteins, we propose a model for the evolution of the seven groups in fungi, animals, and plants, from a single Sec7 domain progenitor
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    Thermosome eukaryotic cells
    Model of the nucleotide cycle of the <t>eukaryotic</t> chaperonin. (a) In the absence of nucleotide, the open complex can bind to unfolded substrates (U-substrate) through binding sites in the central cavity (red lines). (b) ATP binding alone does not produce closure of the lid and significant folding of the substrate, at least in the case of actin. (c) Formation of the trigonal–bipyramidal transition state of the hydrolysis reaction triggers lid closure and confines the substrate in the central cavity. Folding probably occurs at either this stage of the cycle or following scission of the β–γ phosphate bond. (d) Bond scission or inorganic phosphate (P i ].
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    Valiant eukaryotic cell
    Model of the nucleotide cycle of the <t>eukaryotic</t> chaperonin. (a) In the absence of nucleotide, the open complex can bind to unfolded substrates (U-substrate) through binding sites in the central cavity (red lines). (b) ATP binding alone does not produce closure of the lid and significant folding of the substrate, at least in the case of actin. (c) Formation of the trigonal–bipyramidal transition state of the hydrolysis reaction triggers lid closure and confines the substrate in the central cavity. Folding probably occurs at either this stage of the cycle or following scission of the β–γ phosphate bond. (d) Bond scission or inorganic phosphate (P i ].
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    Thermo Fisher eukaryotic cell culture medium
    Model of the nucleotide cycle of the <t>eukaryotic</t> chaperonin. (a) In the absence of nucleotide, the open complex can bind to unfolded substrates (U-substrate) through binding sites in the central cavity (red lines). (b) ATP binding alone does not produce closure of the lid and significant folding of the substrate, at least in the case of actin. (c) Formation of the trigonal–bipyramidal transition state of the hydrolysis reaction triggers lid closure and confines the substrate in the central cavity. Folding probably occurs at either this stage of the cycle or following scission of the β–γ phosphate bond. (d) Bond scission or inorganic phosphate (P i ].
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    Thermo Fisher t rex cho cell line
    Model of the nucleotide cycle of the <t>eukaryotic</t> chaperonin. (a) In the absence of nucleotide, the open complex can bind to unfolded substrates (U-substrate) through binding sites in the central cavity (red lines). (b) ATP binding alone does not produce closure of the lid and significant folding of the substrate, at least in the case of actin. (c) Formation of the trigonal–bipyramidal transition state of the hydrolysis reaction triggers lid closure and confines the substrate in the central cavity. Folding probably occurs at either this stage of the cycle or following scission of the β–γ phosphate bond. (d) Bond scission or inorganic phosphate (P i ].
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    100 240 V 50 60 Hz electroporator includes main unit CE module for exponential decay or square wave pulses shocking chamber 5 x 0 4 cm sterile electroporation cuvettes cuvette
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    Category Antibodies Polyclonal Antibody EIF3C Polyclonal Antibody Size 60μL Price 129 Synonyms Cell migration inducing protein 17 eIF 3c eIF3 p110 eIF3 p110 eIF3c EIF3C EIF3CL EIF3S8 EIF3S8 protein Eukaryotic
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    Image Search Results


    Model for the evolution of the Sec7-domain protein family. Based on the phylogenetic analysis of the eukaryotic Sec7-domain proteins, we propose a model for the evolution of the seven groups in fungi, animals, and plants, from a single Sec7 domain progenitor

    Journal:

    Article Title: Phylogenetic Analysis of Sec7-Domain-containing Arf Nucleotide Exchangers

    doi: 10.1091/mbc.E03-06-0443

    Figure Lengend Snippet: Model for the evolution of the Sec7-domain protein family. Based on the phylogenetic analysis of the eukaryotic Sec7-domain proteins, we propose a model for the evolution of the seven groups in fungi, animals, and plants, from a single Sec7 domain progenitor

    Article Snippet: Gmh1p has homologues in all eukaryotic cells examined, and it will be interesting to determine whether other GBF/GEA and BIG/SEC7 proteins interact with Gmh1p family members, and whether they serve to recruit these GEF proteins to membranes.

    Techniques:

    Model of the nucleotide cycle of the eukaryotic chaperonin. (a) In the absence of nucleotide, the open complex can bind to unfolded substrates (U-substrate) through binding sites in the central cavity (red lines). (b) ATP binding alone does not produce closure of the lid and significant folding of the substrate, at least in the case of actin. (c) Formation of the trigonal–bipyramidal transition state of the hydrolysis reaction triggers lid closure and confines the substrate in the central cavity. Folding probably occurs at either this stage of the cycle or following scission of the β–γ phosphate bond. (d) Bond scission or inorganic phosphate (P i ].

    Journal: Trends in cell biology

    Article Title: Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets

    doi: 10.1016/j.tcb.2004.09.015

    Figure Lengend Snippet: Model of the nucleotide cycle of the eukaryotic chaperonin. (a) In the absence of nucleotide, the open complex can bind to unfolded substrates (U-substrate) through binding sites in the central cavity (red lines). (b) ATP binding alone does not produce closure of the lid and significant folding of the substrate, at least in the case of actin. (c) Formation of the trigonal–bipyramidal transition state of the hydrolysis reaction triggers lid closure and confines the substrate in the central cavity. Folding probably occurs at either this stage of the cycle or following scission of the β–γ phosphate bond. (d) Bond scission or inorganic phosphate (P i ].

    Article Snippet: By contrast, group II chaperonins, such as TCP-1 ring complex (TRiC, also named CCT for chaperonin-containing TCP1) in eukaryotic cells and the thermosome in archaea, are heterooligomeric complexes, with either eight or nine subunits per ring [ , ].

    Techniques: Binding Assay