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Showing 1 to 7 of 7 for “"cysteine modification"”.

  1. Dechalcogenative Allylic Selenosulfide And Disulfide Rearrangements For Cysteine Modification And Glycoligation

    … of thiols, and in particular of cysteine and carbohydrate based thiols. Emphasis is placed on the newly invented silver mediated allylic desulfurative rearrangement for the primary modification of thiols and the synthesis of complex oligosaccharide mimics.</p> <p>Chapter one …

    wayne-thes Repository record for Dechalcogenative Allylic Selenosulfide And Disulfide Rearrangements For Cysteine Modification And Glycoligation (opens in a new tab)

  2. Effects of Cysteine Modification on Microtubule-Motor Protein Function and Tubulin Assembly

    Chemical modification is a powerful technique for probing functionally important amino acids. N-ethylmaleimide (NEM) reacts readily with exposed sulfhydryl groups, and has previously been shown to inhibit the activity of MT-motor proteins and tubulin assembly. This project seeks to investigate the …

    vt Repository record for Effects of Cysteine Modification on Microtubule-Motor Protein Function and Tubulin Assembly (opens in a new tab)

  3. The Development of Vinylheteroarene Linkers for Proteinogenic Cysteine Modification and Studies Towards Applying (+)-Discodermolide as a Novel Payload in Antibody-Drug Conjugates

    … of Vinylheteroarene Linkers for Proteinogenic Cysteine Modification and Studies Towards Applying (+)-Discodermolide as a Novel Payload in Antibody-Drug Conjugates Hikaru Seki Antibody-drug conjugates (ADCs) are an emerging class of anticancer agents which combine the cell-targeting properties …

    cambridge Repository record for The Development of Vinylheteroarene Linkers for Proteinogenic Cysteine Modification and Studies Towards Applying (+)-Discodermolide as a Novel Payload in Antibody-Drug Conjugates (opens in a new tab)

  4. Redox Sensing By Yeast Hsp70 Facilitates Modulation of Protein Quality Control and The Cytoprotective Response

    … has been previously shown to be modulated by modification of two key cysteines in the ATPase domain by oxidizing or thiol-modifying compounds. To investigate the biological consequences of cysteine modification on the Hsp70 Ssa1 in budding yeast, I generated cysteine null (cysteine to serine) …

    uthsc Repository record for Redox Sensing By Yeast Hsp70 Facilitates Modulation of Protein Quality Control and The Cytoprotective Response (opens in a new tab)

  5. Site-selective modification of cysteine residues

    … systems. It is desired to install designer modifications on proteins of interest, in a site-selective manner mimicking nature's post-translational modifications, for various biological and therapeutic applications. Towards this goal, efforts were devoted to develop site-selective protein …

    mit Repository record for Site-selective modification of cysteine residues (opens in a new tab)

  6. Molecular mechanisms behind the adjustment of phototrophic light-harvesting and mixotrophic utilization of cellulosic carbon sources in Chlamydomonas reinhardtii

    … factor is controlled by two posttranslational modifications: i) by methylation of arginines in the glycine-arginine rich (GAR) motif of the protein, ii) by the thiol status of two C-terminal cysteines. This work provides evidence that arginine methylation represents a slowly reacting modulator, …

    bielefeld Repository record for Molecular mechanisms behind the adjustment of phototrophic light-harvesting and mixotrophic utilization of cellulosic carbon sources in Chlamydomonas reinhardtii (opens in a new tab)

  7. Chemical Tools for Exploring IFITM3 S-Palmitoylation and Mechanism

    … is a reversible post-translational lipid modification that regulates the trafficking, stability, and activity of proteins in eukaryotes. The detection of fatty-acylated proteins has been challenging but recent advances in chemical labeling methods have enabled more sensitive detection and …

    rockefeller Repository record for Chemical Tools for Exploring IFITM3 S-Palmitoylation and Mechanism (opens in a new tab)