Results 71 to 80 of about 43,522 (228)

sj-docx-3-asn-10.1177_17590914231158218 - Supplemental material for Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia

, 2023
Supplemental material, sj-docx-3-asn-10.1177_17590914231158218 for Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia by Michael Ohene-Nyako, Sara R. Nass, Hope T.
Michael Ohene-Nyako (4729965), Sara R. Nass (14766998), Kurt F. Hauser (8201931), Hope T. Richard (14767001), Robert Lukande (602521), Melanie R. Nicol (14767004), MaryPeace McRae (7592366), Pamela E. Knapp (8201928)   +7 more
core   +1 more source

Loss of Protein Kinase Csnk2b/CK2β at Neuromuscular Junctions Affects Morphology and Dynamics of Aggregated Nicotinic Acetylcholine Receptors, Neuromuscular Transmission, and Synaptic Gene Expression

Cells, 2019
The protein kinase Csnk2/CK2 is important for cell proliferation, differentiation, and survival. Previously, we showed that CK2 binds distinctive proteins at neuromuscular junctions (NMJs) of mice and phosphorylates some of them.
Nane Eiber, Michael Rehman, Bojana Kravic, Rüdiger Rudolf, Marco Sandri, Said Hashemolhosseini   +5 more
doaj   +1 more source

Harnessing microbial metabolism and nutrition to target the gut–mammary axis for better livestock production and health

iMetaOmics, EarlyView.
The gut–mammary axis integrates intestinal health with mammary function through neural, endocrine, and immune pathways. Nutritional interventions (probiotics, prebiotics, metabolites) improve gut microecology, generating microbial signals that travel via the axis to the mammary gland. There, they relieve inflammation, enhance milk quality and lactation,
Aolong Zhou, Cheng Guo, Mahmoud M. Abdelsattar, Ahmad R. Musa, Mequanint Biks, Abdullahi A. Musa, Shahnaz Rahman, Abera Teshome Aleli, Pei Zhong, Jiawei Zhang, Junwei Cui, Xiyan Kou, Qingyuan Yu, Caijuan Yue, Qin Li, Dan Zhang, Zixuan Peng, Ao Ren, Ziqi Tian, Ziqi Liu, Yaona Zhang, Lili Zhang, Dina Karmallah, Naifeng Zhang, Tao Ma, Yan Tu, Qiyu Diao, Guijie Zhang, Xiaofeng Xu, Yanliang Bi   +29 more
wiley   +1 more source

sj-docx-2-asn-10.1177_17590914231158218 - Supplemental material for Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia

, 2023
Supplemental material, sj-docx-2-asn-10.1177_17590914231158218 for Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia by Michael Ohene-Nyako, Sara R. Nass, Hope T.
Michael Ohene-Nyako (4729965), Sara R. Nass (14766998), Kurt F. Hauser (8201931), Hope T. Richard (14767001), Robert Lukande (602521), Melanie R. Nicol (14767004), MaryPeace McRae (7592366), Pamela E. Knapp (8201928)   +7 more
core   +1 more source

Casein kinase 2 modulates the spindle assembly checkpoint to orchestrate porcine oocyte meiotic progression

Journal of Animal Science and Biotechnology, 2020
Background CK2 (casein kinase 2) is a serine/threonine-selective protein kinase that has been involved in a variety of cellular processes such as DNA repair, cell cycle control and circadian rhythm regulation.
Xiayan ShiYang, Yilong Miao, Zhaokang Cui, Yajuan Lu, Changyin Zhou, Yu Zhang, Bo Xiong   +6 more
doaj   +1 more source

Mixed lineage kinase 3 mediates SARS‐CoV‐2‐induced kidney injury via the Hsp70‐IL‐17A axis

Interdisciplinary Medicine, EarlyView.
Kidney samples from patients infected with severe acute respiratory syndrome coronavirus 2 (SARS‑CoV‑2) showed upregulated expression and activity of Mixed Lineage Kinase (MLK3). Based on the mechanistic studies, we identified MLK3 as a critical player in promoting SARS‐CoV‐2‐induced kidney injury.
Sandeep Kumar, Sunil Kumar Singh, Piush Srivastava, Sowdhamini Mahendiran, Rakesh Sathish Nair, Harsh Vyas, Saket Jha, Niraj Nag, Navin Viswakarma, Hitesh Kapoor, Swathi Suresh, Periannan Sethupathi, Sang‐Ging Ong, Jerrold S. Levine, Suman Setty, Mathayan Manikannan, Bellur S. Prabhakar, Basabi Rana, Ajay Rana   +18 more
wiley   +1 more source

CSNK2A2 (casein kinase 2 alpha 2)

, 2020
CSNK2A2 gene, 16q21, has a role in regulating the phosphorylation and circulation of old proteasomes by encoding the catalytic α' subunit of casein kinase 2 (CK2α'). Casein kinase 2 is a serine/threonine protein kinase that phosphorylates acidic proteins.
A. Beghini, N. Abazari
core  

Phosphorylation by Casein Kinase 2 Regulates Nap1 Localization and Function [PDF]

Molecular and Cellular Biology, 2008
In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and ...
Meredith E K, Calvert, Kristin M, Keck, Celeste, Ptak, Jeffrey, Shabanowitz, Donald F, Hunt, Lucy F, Pemberton   +5 more
openaire   +2 more sources

Small‐Molecule Kinase Inhibitors Modulating Circadian Rhythms

Medicinal Research Reviews, EarlyView.
ABSTRACT The circadian clock mechanism generates 24‐h rhythms crucial for regulating various physiological processes, and its dysregulation has been implicated in numerous diseases. In cells, the circadian clock operates through a transcriptional‐translational feedback loop, where phosphorylation plays a pivotal role in maintaining accurate circadian ...
Irene Castellino, Manuela Bartolini, Rudolf Andrys, Kamil Musilek   +3 more
wiley   +1 more source

Structural Insights Into the Function of Leishmania major Adenylosuccinate Lyase

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT One of several intriguing aspects of kinetoplastid biochemistry is the complete dependence on host purines and purine recycling due to the lack of a de novo purine biosynthesis pathway. Adenylosuccinate lyase (ASL, EC 4.3.2.2) is a key enzyme in the purine synthesis pathway responsible for the conversion of adenylosuccinate into adenosine ...
Ivan R. e Silva, Monique Mantovani, Maria E. S. D. Lino, Aline O. Albuquerque, João H. M. da Silva, Ronaldo A. P. Nagem, Adriana L. Rojas, Geraldo R. Sartori, Eduardo Horjales, David Campbell, Otavio H. Thiemann   +10 more
wiley   +1 more source