Results 21 to 30 of about 117,832 (333)

Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A [PDF]

, 2017
Ribosomal translation factors are fundamental for protein synthesis and highly conserved in all kingdoms of life. The essential eukaryotic elongation factor 1A (eEF1A) delivers aminoacyl tRNAs to the A-site of the translating 80S ribosome.
Aktories, Klaus, Andersen, Gregers Rom, Belyi, Yury, Dengjel, Jörn, Hu, Zehan, Hunte, Carola, Jank, Thomas, Rospert, Sabine, Schlosser, Andreas, Tzivelekidis, Tina, Wirth, Christophe   +10 more
core   +1 more source

Site-selective protein modification via disulfide rebridging for fast tetrazine/trans-cyclooctene bioconjugation [PDF]

, 2020
An inverse electron demand Diels–Alder reaction between tetrazine and trans-cyclooctene (TCO) holds great promise for protein modification and manipulation.
Chudasama, V., Kuan, S., Nogueira, J., Raabe, M., Weil, T., Xu, L., Zegota, M.   +6 more
core   +1 more source

Dynamics of Posttranslational Modifications of p53 [PDF]

Computational and Mathematical Methods in Medicine, 2014
The latest experimental evidence indicates that acetylation of p53 at K164 (lysine 164) and K120 may induce directly cell apoptosis under severe DNA damage. However, previous cell apoptosis models only studied the effects of active and/or inactive p53, that is, phosphorylation/dephosphorylation of p53.
Qing-Duan Fan, Guang Wu, Zeng-rong Liu
openaire   +2 more sources

Targeted Quantification of Phosphorylation Sites Identifies STRIPAK-Dependent Phosphorylation of the Hippo Pathway-Related Kinase SmKIN3

mBio, 2021
Phosphorylation and dephosphorylation of proteins are fundamental posttranslational modifications that determine the fine-tuning of their biological activity.
Valentina Stein, Bernhard Blank-Landeshammer, Ramona Märker, Albert Sickmann, Ulrich Kück   +4 more
doaj   +1 more source

Nitric oxide-induced calcium release: activation of type 1 ryanodine receptor, a calcium release channel, through non-enzymatic posttranslational modification by nitric oxide

Frontiers in Endocrinology, 2013
Nitric oxide (NO) is a typical gaseous messenger involved in a wide range of biological processes. In our classical knowledge, effects of NO are largely achieved by activation of soluble guanylyl cyclase to form cyclic guanosine-3’, 5’-monophosphate ...
Sho eKakizawa
doaj   +1 more source

Posttranslational modifications of fibromodulin.

Journal of Biological Chemistry, 1991
Tyrosine sulfate residues were identified in fibromodulin produced by tracheal chondrocytes, by tendon and sclera fibroblasts in primary culture, as well as in Chinese hamster ovary cells transfected with a construct containing fibromodulin cDNA. The tyrosine sulfate residues were located in the N-terminal part of fibromodulin.
Dick Heinegård, Per Antonsson, Åke Oldberg   +2 more
openaire   +3 more sources

Arginine Methylation Regulates MEIS2 Nuclear Localization to Promote Neuronal Differentiation of Adult SVZ Progenitors

Stem Cell Reports, 2018
Summary: Adult neurogenesis is regulated by stem cell niche-derived extrinsic factors and cell-intrinsic regulators, yet the mechanisms by which niche signals impinge on the activity of intrinsic neurogenic transcription factors remain poorly defined ...
Jasmine Kolb, Marie Anders-Maurer, Tanja Müller, Ann-Christin Hau, Britta Moyo Grebbin, Wiebke Kallenborn-Gerhardt, Christian Behrends, Dorothea Schulte   +7 more
doaj   +1 more source

Posttranslational modifications of GLUT4 affect its subcellular localization and translocation [PDF]

, 2013
The facilitative glucose transporter type 4 (GLUT4) is expressed in adipose and muscle and plays a vital role in whole body glucose homeostasis. In the absence of insulin, only ~1% of cellular GLUT4 is present at the plasma membrane, with the vast ...
Bayer, Begum, Birnbaum, Bogan, Bogan, Bogan, Bryant, Cassie Welburn, Chang, Fujita, Garvey, Gill, Giorgino, Govers, Grasbon-Frodl, Gwyn Gould, Haga, Hardy, Herrmann, Hicke, Huang, Ing, James, James, Jessica Sadler, Jeyaraj, Karylowski, Kupriyanova, Lamb, Lau, Lawrence, Lawrence, Leto, Li, Liu, Livingstone, Mahajan, Marsh, Marshall, Marshall, Martin, Matunis, McCormick, Muller, Nia Bryant, Perera, Pessin, Pilch, Piper, Ren, Reusch, Saltiel, Semiz, Shi, Shi, Stöckli, Toh, Urbe, Vannucci, Varki, Watson, Williams, Yang, Yu, Zaarour   +64 more
core   +3 more sources

The dawn of succinylation: a posttranslational modification [PDF]

American Journal of Physiology-Cell Physiology, 2018
Posttranslational modifications affect almost all proteins and are critical to a well-functioning and diverse proteome; however, many modifications remain relatively unknown and unstudied. This paper will give a perspective on the rapidly developing, novel posttranslational modification called succinylation.
Narasaiah Kolliputi, Matthew Alleyn, Richard F. Lockey, Mason Breitzig   +3 more
openaire   +3 more sources

Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover. [PDF]

, 2012
Protein turnover through cullin-3 is tightly regulated by posttranslational modifications, the COP9 signalosome, and BTB/POZ-domain proteins that link cullin-3 to specific substrates for ubiquitylation.
Chen, Ju, Lange, Stephan, Perera, Sue, Teh, Phildrich   +3 more
core   +2 more sources