Results 41 to 50 of about 941,378 (248)

Mammalian N1-adenosine PARylation is a reversible DNA modification

Nature Communications, 2022
Poly-ADP-ribosylation (PARylation) is a well-known posttranslational modification of proteins. Here the authors show that beyond proteins also mammalian single-stranded DNA is PARylated in vitro and in vivo.
Michael U. Musheev, Lars Schomacher, Amitava Basu, Dandan Han, Laura Krebs, Carola Scholz, Christof Niehrs   +6 more
doaj   +1 more source

Tissue-Specific Posttranslational Modification Allows Functional Targeting of Thyrotropin

Cell Reports, 2014
Thyroid-stimulating hormone (TSH; thyrotropin) is a glycoprotein secreted from the pituitary gland. Pars distalis-derived TSH (PD-TSH) stimulates the thyroid gland to produce thyroid hormones (THs), whereas pars tuberalis-derived TSH (PT-TSH) acts on the
Keisuke Ikegami, Xiao-Hui Liao, Yuta Hoshino, Hiroko Ono, Wataru Ota, Yuka Ito, Taeko Nishiwaki-Ohkawa, Chihiro Sato, Ken Kitajima, Masayuki Iigo, Yasufumi Shigeyoshi, Masanobu Yamada, Yoshiharu Murata, Samuel Refetoff, Takashi Yoshimura   +14 more
doaj   +1 more source

Structure of the planar cell polarity cadherins Fat4 and Dachsous1

Nature Communications, 2023
Fat and Dachsous are large cadherins that regulate planar polarity as a receptor:ligand pair. Here, authors determine the structure of the Fat:Dachsous complex to uncover the molecular determinants of binding and posttranslational modification.
Elliot Medina, Yathreb Easa, Daniel K. Lester, Eric K. Lau, David Sprinzak, Vincent C. Luca   +5 more
doaj   +1 more source

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.
Klaus Aktories, Andersen, Gregers Rom, Christophe Wirth, Jörn Dengjel, Zehan Hu, Hunte, Carola, Jank, Thomas, Tina Tzivelekidis, Carola Hunte, Wirth, Christophe, Aktories, Klaus, Yury Belyi, Hu, Zehan, Dengjel, Jörn, Rospert, Sabine, Andreas Schlosser, Schlosser, Andreas, Sabine Rospert, Thomas Jank, Gregers Rom Andersen, Belyi, Yury, Tzivelekidis, Tina   +21 more
core   +1 more source

The Nervous System Cytoskeleton under Oxidative Stress

Diseases, 2013
Oxidative stress is a key mechanism causing protein aggregation, cell death and neurodegeneration in the nervous system. The neuronal cytoskeleton, that is, microtubules, actin filaments and neurofilaments, plays a key role in defending the nervous ...
John Gardiner, Robyn Overall, Jan Marc
doaj   +1 more source

Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB [PDF]

, 2003
Marquordt C, Fang QH, Will E, Peng JH, Figura von K, Dierks T. Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB.
Figura von, K, von Figura, K., Marquordt, C, Fang, Q., Peng, J. H., Peng, JH, Will, E., Peng, J., Will, E, Marquordt, C., Fang, Q. H., von Figura, Kurt, Dierks, Thomas, Dierks, T., Fang, QH   +14 more
core   +1 more source

An Anti‐Amyloidogenic Approach to Specifically Block Memory Consolidation in Mice for Therapeutic Intervention

Advanced Science, EarlyView.
Functional amyloid conversion of the translation regulator CPEB3 is essential for long‐term memory persistence. This study demonstrates that targeting this molecular switch with the anti‐amyloidogenic peptide QBP1 selectively blocks CPEB3 fibrillation without disrupting phase separation.
Paula López‐García, Kerry R. McGreevy, Maria Eugenia Vaquero, Juan M. Suarez‐Rivero, Antonio Moreno‐Rodríguez, Antonio J. Pérez‐Pulido, Daniel Ramírez de Mingo, Anna Pallé, Helena Akiko Popiel, Andrea Santi, Mario D. Cordero, José Luis Trejo, Yoshitaka Nagai, Mariano Carrión‐Vázquez   +13 more
wiley   +1 more source

Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation. [PDF]

PLoS ONE, 2010
BACKGROUND: Glyoxalase 1 (Glo1) and glyoxalase 2 (Glo2) are ubiquitously expressed cytosolic enzymes that catalyze the conversion of toxic alpha-oxo-aldehydes into the corresponding alpha-hydroxy acids using L-glutathione (GSH) as a cofactor.
Gerd Birkenmeier, Christin Stegemann, Ralf Hoffmann, Robert Günther, Klaus Huse, Claudia Birkemeyer   +5 more
doaj   +1 more source

Regulation of the water channel aquaporin-2 by posttranslational modification

, 2011
The cellular functions of many eukaryotic membrane proteins, including the vasopressin-regulated water channel aquaporin-2 (AQP2), are regulated by posttranslational modifications.
Robert A. Fenton, Emma T. B. Olesen, Hanne B. Moeller   +2 more
core   +1 more source

Site-Specific Modification and Segmental Isotope Labelling of HMGN1 Reveals Long-Range Conformational Perturbations Caused by Posttranslational Modifications [PDF]

, 2020
Interactions between histones, which package DNA in eukaryotes, and nuclear proteins such as the high mobility group nucleosome-binding protein HMGN1 are important for regulating access to DNA.
K. Johan, Rosengren, Anne, Conibear, Christian F. W., Becker, Gerhard, Niederacher, Debra, Urwin, David, J. Tremethick   +5 more
core   +2 more sources