Page last updated: 2024-08-21

2,4-dinitrothiocyanatobenzene and cysteine

2,4-dinitrothiocyanatobenzene has been researched along with cysteine in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19901 (16.67)18.7374
1990's1 (16.67)18.2507
2000's2 (33.33)29.6817
2010's1 (16.67)24.3611
2020's1 (16.67)2.80

Authors

AuthorsStudies
Huang, PC; Lyu, PC; Pan, PK; Zheng, ZF1
BELMAM, S; EISEN, HN1
Jaiswal, R; Panda, D1
Gardonio, D; Siemann, S1
Arve, B; Cohen, J; D'Antona, A; Ferguson, D; Gatto, S; He, T; Kriz, R; Lin, L; Luan, YT; Ma, W; Prashad, AS; Somers, W; Sousa, E; Tam, AS; Tchistiakova, L; Wang, W; Zhong, X; Zhou, J; Zollner, R1
Badepally, NG; Singh, A; Surolia, A1

Other Studies

6 other study(ies) available for 2,4-dinitrothiocyanatobenzene and cysteine

ArticleYear
Why reversing the sequence of the alpha domain of human metallothionein-2 does not change its metal-binding and folding characteristics.
    European journal of biochemistry, 1999, Volume: 266, Issue:1

    Topics: Amino Acid Sequence; Animals; Cadmium; Circular Dichroism; Cysteine; Dinitrobenzenes; Humans; Metallothionein; Molecular Sequence Data; Peptides; Protein Binding; Protein Structure, Tertiary; Rats

1999
Studies of hypersensitivity to low molecular weight substances. II. Reactions of some allergenic substituted dinitrobenzenes with cysteine or cystine of skin proteins.
    The Journal of experimental medicine, 1953, Volume: 98, Issue:6

    Topics: Allergens; Animals; Cattle; Cysteine; Cystine; Dinitrobenzenes; Dinitrofluorobenzene; Disulfides; Guinea Pigs; Humans; Hypersensitivity; Immune System Diseases; Lysine; Molecular Weight; Nitrobenzenes; Proteins; Skin; Sulfenic Acids; Sulfhydryl Compounds

1953
Cysteine 155 plays an important role in the assembly of Mycobacterium tuberculosis FtsZ.
    Protein science : a publication of the Protein Society, 2008, Volume: 17, Issue:5

    Topics: Anilino Naphthalenesulfonates; Bacterial Proteins; Chelating Agents; Cysteine; Cytoskeletal Proteins; Dinitrobenzenes; Mercuric Chloride; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; Protein Structure, Secondary

2008
Chelator-facilitated chemical modification of IMP-1 metallo-beta-lactamase and its consequences on metal binding.
    Biochemical and biophysical research communications, 2009, Mar-27, Volume: 381, Issue:1

    Topics: beta-Lactamases; Chelating Agents; Cysteine; Dinitrobenzenes; Methods; Methyl Methanesulfonate; Phosphines; Protein Binding; Thiocyanates; Zinc

2009
Mechanistic understanding of the cysteine capping modifications of antibodies enables selective chemical engineering in live mammalian cells.
    Journal of biotechnology, 2017, Apr-20, Volume: 248

    Topics: Animals; Antibodies; CHO Cells; Cricetinae; Cricetulus; Cysteine; Dinitrobenzenes; HEK293 Cells; Humans; Protein Engineering; Recombinant Proteins

2017
Role of a cysteine residue in substrate entry and catalysis in MtHIBADH: Analysis by chemical modifications and site-directed mutagenesis.
    IUBMB life, 2021, Volume: 73, Issue:6

    Topics: Alanine; Alcohol Oxidoreductases; Bacterial Proteins; Catalysis; Cysteine; Dinitrobenzenes; Hydrogen Bonding; Models, Molecular; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; NAD; p-Chloromercuribenzoic Acid; Protein Conformation; Recombinant Proteins; Serine; Structure-Activity Relationship; Substrate Specificity

2021