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Posttranslational modifications in systems biology

2021
The biological complexity cannot be captured by genes or proteins alone. The protein posttranslational modifications (PTMs) impart functional diversity to the proteome and regulate protein structure, activity, localization and interactions. Their dynamics drive cellular signaling, growth and development while their dysregulation causes many diseases ...
Suruchi, Aggarwal   +3 more
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Posttranslational Modifications of Enzymes

1978
Publisher Summary This chapter describes enzyme alterations in some selected systems. The isocitrate lyase from old Turbatrix aceti ( T. aceti ) consists of a mixture of active and inactive molecules. The nematode T. aceti , the eye lens, and red blood cells are the systems that allow recognition of the most frequent and unequivocal postsynthetic ...
J C, Dreyfus, A, Kahn, F, Schapira
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Probing Posttranslational Redox Modifications

2017
Reactive molecular species (RMS) can damage DNA, lipids, and proteins but as signaling molecules they also affect the regulatory state of the cell. RMS consist of reactive oxygen (ROS), nitrogen (RNS), and carbonyl species (RCS). Besides their potentially destructive nature, RMS are able to modify proteins at the posttranslational level, resulting in ...
Treffon, Patrick   +4 more
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Posttranslational modification of prothyroid hormone

Canadian Journal of Biochemistry and Cell Biology, 1983
Posttranslational processing of thyroglobulin may influence its role as the prothyroid hormone. We have examined the role of glycosylation in the subsequent export and iodination of thyroglobulin. We find that glycosylation is necessary both for the movement of thyroglobulin through the cell and for iodination.
M C, Eggo   +3 more
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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.
J, Mary   +4 more
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ANTIBIOTICS SYNTHESIZED BY POSTTRANSLATIONAL MODIFICATION

Annual Review of Microbiology, 1993
Peptides that have antimicrobial activity are synthesized by many prokaryotic and eukaryotic organisms. Antimicrobial peptides commonly contain unusual amino acids that contribute to their properties and functions. Although bacteria synthesize most of these peptides by nonribosomal mechanisms, this review focuses on those that are synthesized by ...
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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 Modification

2013
At the later stages of protein biosynthesis, after their transcription, many proteins undergo intensive chemical alterations, collectively known as protein posttranslational modifications (PTMs). These modifications are many and range from the proteolytic cleavage to the covalent attachment of diverse functional groups or even proteins to specific side
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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 Modification of Sodium Channels

2017
Voltage-gated sodium channels (VGSCs) are critical determinants of excitability. The properties of VGSCs are thought to be tightly controlled. However, VGSCs are also subjected to extensive modifications. Multiple posttranslational modifications that covalently modify VGSCs in neurons and muscle have been identified.
Zifan, Pei   +2 more
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