selenocysteine and guanosine triphosphate

selenocysteine has been researched along with guanosine triphosphate in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's1 (14.29)29.6817
2010's5 (71.43)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Böck, A; Hüttenhofer, A1
Bock, A; Goody, RS; Thanbichler, M1
Copeland, PR; Donovan, J1
Copeland, PR; DeMong, LW; Gonzalez-Flores, JN; Gupta, N1
Itoh, Y; Sekine, S; Yokoyama, S1
Casini, A; Cinellu, MA; Gerner, C; Keppler, BK; Meier, SM1
Chakravarthy, S; Copeland, PR; Dobosz-Bartoszek, M; Otwinowski, Z; Pinkerton, MH; Simonović, M; Söll, D1

Reviews

1 review(s) available for selenocysteine and guanosine triphosphate

ArticleYear
Threading the needle: getting selenocysteine into proteins.
    Antioxidants & redox signaling, 2010, Apr-01, Volume: 12, Issue:7

    Topics: Animals; Codon; Guanosine Triphosphate; Humans; Models, Molecular; Nucleic Acid Conformation; Protein Conformation; Protein Isoforms; Proteins; Ribosomes; RNA; RNA Stability; RNA-Binding Proteins; RNA, Transfer, Amino Acyl; Selenocysteine

2010

Other Studies

6 other study(ies) available for selenocysteine and guanosine triphosphate

ArticleYear
Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SelB.
    Biochemistry, 1998, Jan-20, Volume: 37, Issue:3

    Topics: Bacterial Proteins; Base Sequence; Escherichia coli; GTP Phosphohydrolases; Guanosine Triphosphate; Hydrolysis; Kinetics; Nucleic Acid Conformation; Ribosomes; RNA, Bacterial; RNA, Transfer, Amino Acyl; Selenocysteine

1998
Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA.
    The Journal of biological chemistry, 2000, Jul-07, Volume: 275, Issue:27

    Topics: Bacterial Proteins; Base Sequence; Binding Sites; Binding, Competitive; Escherichia coli; Fluorescence; Fluorescent Dyes; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Molecular Sequence Data; Nucleic Acid Conformation; ortho-Aminobenzoates; Peptide Elongation Factors; RNA, Messenger; RNA, Transfer, Amino Acid-Specific; RNA, Transfer, Amino Acyl; Selenocysteine; Tryptophan

2000
The selenocysteine-specific elongation factor contains a novel and multi-functional domain.
    The Journal of biological chemistry, 2012, Nov-09, Volume: 287, Issue:46

    Topics: Amino Acid Sequence; Animals; Binding Sites; Codon; Codon, Terminator; Cross-Linking Reagents; Guanosine Triphosphate; Hydrolysis; Mice; Molecular Sequence Data; Peptide Elongation Factors; Protein Biosynthesis; Protein Structure, Tertiary; Rats; Recombinant Proteins; Ribosomes; RNA-Binding Proteins; RNA, Transfer, Amino Acyl; Selenocysteine; Sequence Homology, Amino Acid

2012
Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB.
    Nucleic acids research, 2015, Oct-15, Volume: 43, Issue:18

    Topics: Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Guanosine Triphosphate; Models, Molecular; Peptide Elongation Factors; Ribosomes; RNA, Messenger; RNA, Transfer, Amino Acid-Specific; Selenocysteine

2015
Mass Spectrometry Uncovers Molecular Reactivities of Coordination and Organometallic Gold(III) Drug Candidates in Competitive Experiments That Correlate with Their Biological Effects.
    Inorganic chemistry, 2016, 05-02, Volume: 55, Issue:9

    Topics: Adenosine Triphosphate; Animals; Cattle; Cytochromes c; Drug Stability; Guanine; Guanosine Triphosphate; Horses; Organogold Compounds; Selenocysteine; Spectrometry, Mass, Electrospray Ionization; Thioredoxin Reductase 1; Ubiquitin; Water

2016
Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.
    Nature communications, 2016, 10-06, Volume: 7

    Topics: Codon, Terminator; Crystallography, X-Ray; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Peptide Elongation Factors; Phylogeny; Protein Biosynthesis; Protein Domains; Protein Structure, Secondary; Ribosomes; RNA, Transfer, Amino Acyl; Selenocysteine; Selenoproteins

2016