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Posttranslational Covalent Modification of Proteins

Science, 1977
A search for derivatized amino acids in proteins has shown that the extent of posttranslational modification of proteins is quite substantial. While only 20 primary amino acids are specified in the genetic code and are involved as monomer building blocks in the assembly of the polypeptide chain, about 140 amino acids and amino acid derivatives have ...
Rosa Uy, Finn Wold
openaire   +1 more source

Covalent Modification of Biomolecules through Maleimide-Based Labeling Strategies.

Bioconjugate chemistry, 2018
Since their first use in bioconjugation more than 50 years ago, maleimides have become privileged chemical partners for the site-selective modification of proteins via thio-Michael addition of biothiols and, to a lesser extent, via Diels-Alder (DA ...
Kévin Renault   +3 more
semanticscholar   +1 more source

Advances of Covalent Chemical Modifications of RNA

Chemistry – A European Journal
ABSTRACT Chemical modification of RNA can endow RNA molecules with novel structures and functions, enabling broader clinical application potential. RNA chemical modification is a systematic and controllable engineering approach, particularly at the cellular or tissue level, requiring precise modification strategies to reduce off ...
Yong Li   +7 more
openaire   +2 more sources

Covalent Modification of G Proteins by Affinity Labeling

2003
The activation of heterotrimeric G-proteins is tightly regulated by the exchange of GTP for GDP in the alpha-subunit; mostly--but not exclusively--seven-transmembrane receptors function as the guanine nucleotide exchange factors (GEFs). A research goal may be to determine which G-protein alpha-subunit is activated by the receptor under investigation ...
Martin, Hohenegger   +2 more
openaire   +3 more sources

Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
Multimeric globins (e.g., hemoglobin) are considered to be the prototypes of allosteric enzymes, whereas monomeric globins (e.g., myoglobin; Mb) usually are assumed to be non-allosteric. However, the modulation of the functional properties of monomeric globins by non-covalent (or allosteric) and covalent modifications casts doubts on this general ...
Ascenzi, P   +10 more
openaire   +4 more sources

Covalent modification and metabolic control analysis

European Journal of Biochemistry, 1990
A study of the sensitivity properties of metabolic systems containing covalently modifiable enzymes and cascades has been carried out with the aid of metabolic control analysis. We have considered how the theorems of metabolic control analysis must be modified to take into account covalently modifiable enzymes, and have used these results to ...
J R, Small, D A, Fell
openaire   +2 more sources

Covalent modification of PTPases

1998
Abstract The large, transmembrane PTPases have been shown in several cases to undergo proteolytic processing of a proprotein that produces protein subunits, including LAR, RPTP-k and RPTP-σ. The site and determinants of LAR proprotein cleavage have recently been evaluated [105, 110, 116].
openaire   +1 more source

Reversible inactivation and superactivation by covalent modification of thermolysin

Biochemical and Biophysical Research Communications, 1973
Abstract Diethylpyrocarbonate (DEP) in the pH range 6.1 – 7.5 inactivates thermolysin by ethoxyformylation. Restoration of activity by hydroxylamine at pH 6.2 correlates with the regeneration of a single histidyl residue. Exposure of the enzyme to DEP together with the reversible inhibitor β-phenylpropionyl-L-phenylalanine, or acylation with the ...
S, Blumberg, B, Holmquist, B L, Vallee
openaire   +2 more sources

Inheritance of a covalent histone modification

Science, 2015
Epigenetics Genomic DNA is the repository of all genetic information and is packaged into chromatin. Chromatin is also a repository of regulatory information in the form of covalent marks added to the histones that package the DNA. These marks can determine tissue- and organ-specific gene expression patterns, which must be transmitted to daughter cells
openaire   +1 more source

Targeting an Intrinsically Disordered Protein by Covalent Modification

2020
Intrinsically disordered proteins (IDPs) play important roles in the regulation of cellular function and in disease, and thus they represent an important group of therapeutic targets. Yet, members of this "disorderome" have not yet been successfully targeted by drugs, primarily because traditional design principles cannot be applied to their highly ...
Nguyen, Hung Huy   +7 more
openaire   +3 more sources

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