Compounds > carbonyl cyanide m-chlorophenyl hydrazone

carbonyl cyanide m-chlorophenyl hydrazone and major coat protein, pseudomonas phage pf3

carbonyl cyanide m-chlorophenyl hydrazone has been researched along with major coat protein, pseudomonas phage pf3 in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Dalbey, RE; Delgado-Partin, VM	1
Kiefer, D; Kuhn, A	1

Other Studies

2 other study(ies) available for carbonyl cyanide m-chlorophenyl hydrazone and major coat protein, pseudomonas phage pf3

Article	Year
The proton motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophobicity of the translocation signal is low. The Journal of biological chemistry, 1998, Apr-17, Volume: 273, Issue:16 Topics: Amino Acid Sequence; Capsid; Capsid Proteins; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cell Membrane; Escherichia coli; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Peptide Mapping; Protein Structure, Secondary; Proton-Motive Force; Pseudomonas Phages; Recombinant Proteins; Sequence Deletion; Spheroplasts	1998
Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control. The EMBO journal, 1999, Nov-15, Volume: 18, Issue:22 Topics: Adenosine Triphosphatases; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Capsid; Capsid Proteins; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Carrier Proteins; Electrochemistry; Escherichia coli; Escherichia coli Proteins; Lipid Bilayers; Membrane Potentials; Membrane Transport Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Biosynthesis; Protein Conformation; Pseudomonas Phages; Recombinant Proteins; SEC Translocation Channels; SecA Proteins; Thermodynamics	1999

Article

Year

The proton motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophobicity of the translocation signal is low.

The Journal of biological chemistry, 1998, Apr-17, Volume: 273, Issue:16

Topics: Amino Acid Sequence; Capsid; Capsid Proteins; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cell Membrane; Escherichia coli; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Peptide Mapping; Protein Structure, Secondary; Proton-Motive Force; Pseudomonas Phages; Recombinant Proteins; Sequence Deletion; Spheroplasts

1998

Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control.

The EMBO journal, 1999, Nov-15, Volume: 18, Issue:22

Topics: Adenosine Triphosphatases; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Capsid; Capsid Proteins; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Carrier Proteins; Electrochemistry; Escherichia coli; Escherichia coli Proteins; Lipid Bilayers; Membrane Potentials; Membrane Transport Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Biosynthesis; Protein Conformation; Pseudomonas Phages; Recombinant Proteins; SEC Translocation Channels; SecA Proteins; Thermodynamics

1999