Results 231 to 240 of about 6,676 (281)
Legionella pneumophila evades host-autophagic clearance using phosphoribosyl-polyubiquitin chains. [PDF]
Nat CommunChoi M, Jeong M, Kang S, Jeon H, Shin D.
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A Simple, Quick, and Scalable Route to Fluorogenic Ubiquitin and Ubiquitin-Like Protein Substrates for Assessing Activities of Deubiquitinases and Ubiquitin-Like Protein-Specific Proteases. [PDF]
ACS Chem BiolChanda S, Pham A, Shi Y, Atla S, Liu WR.
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Mesostructured Water Enhances Stability of ProteinMPNN-Designed Ubiquitin-Fold Proteins. [PDF]
J Am Chem SocChen LY +10 more
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One Ubiquitin, Two Ubiquitin, Three Ubiquitin, Four
Science's STKE, 2007The role of protein ubiquitination is well known in promoting regulated protein degradation. Mukhopadhyay and Riezman review what is known about the contribution of protein ubiquitination in other cellular pathways, including intracellular signaling, endocytosis, and protein sorting. D. Mukhopadhyay, H.
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Ubiquitin and ubiquitin conjugates in human lens
Experimental Eye Research, 1992Ubiquitin, an 8.5 kDa polypeptide found almost universally in plants and animals, is a normal component in the lens. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation. Conjugates for ubiquitin-dependent degradation tend to be of very high molecular mass and are rapidly degraded.
J, Jahngen-Hodge +3 more
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The measurement of ubiquitin and ubiquitinated proteins
Electrophoresis, 1999Ubiquitination of key cellular proteins involved in signal transduction, gene transcription and cell-cycle regulation usually condemns those proteins to proteasomal or lysosomal degradation. Additionally, cycles of reversible ubiquitination regulate the function of certain proteins in a manner analogous to phosphorylation.
E G, Mimnaugh, P, Bonvini, L, Neckers
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In Vitro Ubiquitination: Self-Ubiquitination, Chain Formation, and Substrate Ubiquitination Assays
2016Ubiquitination of proteins in vitro has evolved as an indispensable tool for the functional analysis of this posttranslational modification. In vitro ubiquitination is particularly helpful to study conjugation mechanisms. The efficiency of the ubiquitination reaction depends in part on the quality of the enzymes utilized.
E. Maspero, S. Polo
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Activation of Ubiquitin and Ubiquitin-Like Proteins
2010Attachment of ubiquitin and ubiquitin-like proteins to cellular targets represents a fundamental regulatory strategy within eukaryotes and exhibits remarkably pleiotropic effects on cell function. These posttranslational modifications share a common mechanism comprised of three steps: an activating enzyme to couple ATP hydrolysis to formation of a high-
Frederick C, Streich, Arthur L, Haas
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Analytical Biochemistry, 2017
Ubiquitin, a 76 amino acid protein, is a key component that contributes to cellular protein homeostasis. The specificity of this modification is due to a series of enzymes: ligases, attaching the ubiquitin to a lysine, and deubiquitinases, which remove it. More than a hundred of such proteins are implicated in the regulation of protein turnover.
Marine, Bacchi +9 more
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Ubiquitin, a 76 amino acid protein, is a key component that contributes to cellular protein homeostasis. The specificity of this modification is due to a series of enzymes: ligases, attaching the ubiquitin to a lysine, and deubiquitinases, which remove it. More than a hundred of such proteins are implicated in the regulation of protein turnover.
Marine, Bacchi +9 more
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[Progress in ubiquitin, ubiquitin chain and protein ubiquitination].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2016Protein ubiquitination is one of the most important and widely exist protein post-translational modifications in eukaryotic cells, which takes the ubiquitin and ubiquitin chains as signal molecules to covalently modify other protein substrates. It plays an important roles in the control of almost all of the life processes, including gene transcription ...
Qiuyan, Lan +4 more
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