Results 271 to 280 of about 71,707 (290)

Posttranslational modifications in GPCR internalization

American Journal of Physiology-Cell Physiology, 2022
G protein-coupled receptors (GPCRs) are the largest family of membrane receptors that serve as the most important drug targets. Classically, GPCR internalization has been considered to lead to receptor desensitization. However, many studies over the past decade have reported that internalized membrane receptors can trigger distinct signal activation ...
Xueqing Tang, Jingwei Bian, Zijian Li
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Posttranslational Modifications of Axonemal Tubulin

Journal of Protein Chemistry, 1997
Axonemal tubulin exhibits a high degree of heterogeneity mostly due to several posttranslational modifications (PTM). The aim of this work was to chemically characterize the different PTM occurring in the C-terminal tail of axonemal tubulin purified from sea urchin, Paracentrotus lividus, spermatozoa.
Jérôme Rossier, J.P. Le Caer, Jean Yves Mary, Virginie Redeker, J.-M. Schmitter   +4 more
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Posttranslational Modifications of Self‐Antigens

Annals of the New York Academy of Sciences, 2005
Abstract: Although the immune system has developed mechanisms to distinguish “self” from “non‐self,” the presence of autoimmune diseases demonstrates that these mechanisms can be bypassed. The posttranslational modification of self‐antigens is one way in which “new” antigens are created for which immune tolerance does not exist.
Hester A. Doyle, Mark J. Mamula
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Posttranslational Modifications of Histones by Methylation

2004
Publisher Summary This chapter demonstrates that an RNA polymerase II elongation factor—the Paf1 complex—is required for the recruitment of histone methyltransferases to the elongating RNA polymerase and suggests that it is possible that modification by methylation may serve as a mark of transcriptional memory for transcribed genes.
Ali Shilatifard, Adam Wood
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Posttranslational modifications of caseins

2020
The caseins exhibit a high degree of heterogeneity as a result of posttranslational modifications (PTMs). Phosphorylation of the αs1-, αs2-, and β-caseins and glycosylation of κ-casein are the best-known modifications and are critical for the formation and stability of casein micelles.
Bijl, Etske, Holland, John W., Boland, Mike   +2 more
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Cofactors in and as posttranslational protein modifications

The FASEB Journal, 1988
A symposium at the FASEB meeting in Las Vegas in May 1988 will be devoted to the role of cofactors (vitamins, coenzymes, prosthetic groups) in and as posttranslational protein modifications; the symposium is part of a thematic focus on metabolic regulation.
Robert B. Rucker, Finn Wold
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Posttranslational Modification of Proteins

2015
Proteins are subject to continuous reversible and irreversible modifications. These posttranslational modifications directly influence the stability and/or the function of proteins. Aging results in an increased half-life of proteins, which is associated with enhanced oxidative modifications of amino acid residues.
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Histone Posttranslational Modifications in Schizophrenia

2017
Schizophrenia is a complex neuropsychiatric disorder with high heritability; however, family and twin studies have indicated that environmental factors also play important roles in the etiology of disease. Environmental triggers exert their influence on behavior via epigenetic mechanisms.
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Thioredoxin-1 and Posttranslational Modifications

Antioxidants & Redox Signaling, 2006
Thioredoxin-1 is a 12 kDa protein that consists of a redox regulatory domain containing the active cysteine residues 32 and 35. These cysteines are conserved from bacteria to human. Unlike thioredoxins from lower species, mammalian thioredoxin-1 contains three additional nonactive cysteine residues at positions 62, 69, and 73 (for human thioredoxin-1).
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Posttranslational Modifications of Tubulin

2012
Recent studies have highlighted the potential importance of posttranslational modifications of tubulin in dictating response to antitumor drugs and disease progression. These modifications include glutamylation, glycylation, phosphorylation, acetylation, and tyrosination.
Suzan K. Chao, Susan Band Horwitz, Chia Ping H. Yang   +2 more
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