Compounds > n,n'-4-phenylenedimaleimide
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n,n'-4-phenylenedimaleimide and n,n'-2-phenylenedimaleimide

n,n'-4-phenylenedimaleimide has been researched along with n,n'-2-phenylenedimaleimide in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's5 (83.33)18.2507
2000's1 (16.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hardy, D; Kaback, HR; Wu, J3
Goto, S; Hashimoto, M; Majima, E; Shinohara, Y; Terada, H1
Kaback, HR; Wang, Q1
Arselin, G; Bathany, K; Brèthes, D; Chaignepain, S; Paumard, P; Schmitter, JM; Vaillier, J; Velours, J1

Other Studies

6 other study(ies) available for n,n'-4-phenylenedimaleimide and n,n'-2-phenylenedimaleimide

ArticleYear
Transmembrane helix tilting and ligand-induced conformational changes in the lactose permease determined by site-directed chemical crosslinking in situ.
    Journal of molecular biology, 1998, Oct-09, Volume: 282, Issue:5

    Topics: Cross-Linking Reagents; Cysteine; Escherichia coli Proteins; Maleimides; Membrane Transport Proteins; Models, Molecular; Monosaccharide Transport Proteins; Protein Conformation; Recombinant Proteins; Symporters

1998
Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situ.
    Biochemistry, 1998, Nov-10, Volume: 37, Issue:45

    Topics: Cross-Linking Reagents; Cysteine; Escherichia coli Proteins; Ligands; Maleimides; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Sulfhydryl Compounds; Symporters; Thiogalactosides

1998
Fluctuation of the first loop facing the matrix of the mitochondrial ADP/ATP carrier deduced from intermolecular cross-linking of Cys56 residues by bifunctional dimaleimides.
    Biochemistry, 1999, Jan-19, Volume: 38, Issue:3

    Topics: Adenosine Diphosphate; Animals; Biological Transport; Cattle; Cross-Linking Reagents; Cysteine; Ethylmaleimide; Glutathione; Maleimides; Mitochondria, Heart; Mitochondrial ADP, ATP Translocases; Protein Conformation; Solutions; Submitochondrial Particles

1999
Site-directed chemical cross-linking demonstrates that helix IV is close to helices VII and XI in the lactose permease.
    Biochemistry, 1999, Feb-09, Volume: 38, Issue:6

    Topics: Amino Acid Sequence; Cross-Linking Reagents; Cysteine; Escherichia coli; Escherichia coli Proteins; Ligands; Maleimides; Membrane Transport Proteins; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Symporters

1999
Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking: helix I is close to helices V and XI.
    Biochemistry, 1999, Mar-09, Volume: 38, Issue:10

    Topics: Biological Transport, Active; Cross-Linking Reagents; Escherichia coli; Escherichia coli Proteins; Maleimides; Membrane Transport Proteins; Methionine; Models, Molecular; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Secondary; Sulfhydryl Compounds; Sulfur Radioisotopes; Symporters

1999
Two ATP synthases can be linked through subunits i in the inner mitochondrial membrane of Saccharomyces cerevisiae.
    Biochemistry, 2002, Aug-20, Volume: 41, Issue:33

    Topics: Amino Acid Sequence; Cross-Linking Reagents; Dimerization; Intracellular Membranes; Maleimides; Mitochondria; Mitochondrial Proton-Translocating ATPases; Molecular Sequence Data; Proton-Translocating ATPases; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

2002