Results 61 to 70 of about 72,712 (256)

Nuclear pore links Fob1‐dependent rDNA damage relocation to lifespan control

FEBS Open Bio, EarlyView.
Damaged rDNA accumulates at a specific perinuclear interface that couples nucleolar escape with nuclear envelope association. Nuclear pores at this site help inhibit Fob1‐induced rDNA instability. This spatial organization of damage handling supports a functional link between nuclear architecture, rDNA stability, and replicative lifespan in yeast.
Yamato Okada, Mina Iwaki, Kyosuke Hagiri, Rei Izumi, Masahiko Harata, Chihiro Horigome   +5 more
wiley   +1 more source

The Flagellar Motility of \u3cem\u3eChlamydomonas pf25\u3c/em\u3e Mutant Lacking an AKAP-binding Protein Is Overtly Sensitive to Medium Conditions [PDF]

, 2006
Radial spokes are a conserved axonemal structural complex postulated to regulate the motility of 9 + 2 cilia and flagella via a network of phosphoenzymes and regulatory proteins.
Yang, Chun, Yang, Pinfen
core   +1 more source

A-kinase anchoring proteins and neuronal signaling mechanisms [PDF]

Genes & Development, 2003
The rapid and reversible phosphorylation of proteins catalyzed by protein kinases and protein phosphatases is a well recognized mechanism of regulation in cells. This bidirectional process is a highly flexible method of influencing cellular activity in response to a variety of incoming stimuli. A physiological role for protein phosphorylation was first
Graeme K, Carnegie, John D, Scott
openaire   +2 more sources

Anchorage‐independent and faster growth in clonal population from UV‐irradiated NER‐deficient cells

FEBS Open Bio, EarlyView.
UV‐irradiated cells expressing a DDB2 mutant protein unable to interact with PCNA (DDB2PCNA‐) form clones able to grow without anchorage. Different experimental approaches reveal heterogeneity in cell cycle regulation and drug response within these clones, emphasizing the crucial role of the DDB2‐PCNA interaction in preventing cellular transformation ...
Paola Perucca, Anna Tricarico, Martina Furfaro, Priyam Ghosh, Ennio Prosperi, Lucia Anna Stivala, Ornella Cazzalini   +6 more
wiley   +1 more source

Identification of proteins in the postsynaptic density fraction by mass spectrometry [PDF]

, 2000
Our understanding of the organization of postsynaptic signaling systems at excitatory synapses has been aided by the identification of proteins in the postsynaptic density (PSD) fraction, a subcellular fraction enriched in structures with the morphology ...
Jensen, Ole N., Kennedy, Mary B., Mann, Matthias, Mercer, John A., Provance, D. William, Jr., Walikonis, Randall S.   +5 more
core   +2 more sources

AKAPDB: A-Kinase Anchoring Proteins Database [PDF]

Genomics & Informatics, 2010
Abstract A-kinase-anchoring proteins (AKAPs) are scaffold pro-teins which compartmentalize protein kinase A (PKA, cAMP-dependent protein kinase) and other enzymes to specific subcellular sites. The spatiotemporal control of these enzymes by AKAPs is important for cellular func-tion like cell growth and development etc.
In-Sil Kim, Kyung-Joon Lim, Bok-Ghee Han, Myung-Guen Chung, Kyu-Won Kim   +4 more
openaire   +1 more source

Molecular dynamics simulations of positively selected codons in FcγRI reveal novel biochemical binding properties

FEBS Open Bio, EarlyView.
Evolutionary analysis across 32 placental mammals identified positive selection at residues H148 and W149 in the immune receptor FcγR1. Ancestral reconstruction combined with molecular dynamics simulations reveals how these mutations may influence receptor structure and dynamics, providing insight into the evolution of antibody recognition and immune ...
David A. Young, Omar Arias‐Gaguancela, Fiona Gibson, Morgan Grainger, Jodie Score, Amit Nathubhai, Mauricio Cafiero, Lee Richard Machado   +7 more
wiley   +1 more source

Distribution of A-kinase anchoring proteins in parietal cells

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1995
Recent investigations have suggested that subcellular compartmentalization of second messenger responsive enzyme systems may be responsible for specific patterns of cellular activation. The type II cAMP-dependent kinase (A-kinase) is localized to particular subcellular domains through the binding of the regulatory subunit (RII) dimer to A-kinase ...
Dransfield, Daniel T., Bradford, Alvin J., Goldenring, James R.   +2 more
openaire   +2 more sources

Roles of A-Kinase Anchoring Proteins and Phosphodiesterases in the Cardiovascular System [PDF]

Journal of Cardiovascular Development and Disease, 2018
A-kinase anchoring proteins (AKAPs) and cyclic nucleotide phosphodiesterases (PDEs) are essential enzymes in the cyclic adenosine 3’-5’ monophosphate (cAMP) signaling cascade. They establish local cAMP pools by controlling the intensity, duration and compartmentalization of cyclic nucleotide-dependent signaling.
Ercu, M., Klussmann, E.
openaire   +4 more sources

UiO‐66 metal–organic frameworks in biomedicine: From structural tunability to bioimaging, photodiagnostics, and photodynamic cancer therapy

FEBS Open Bio, EarlyView.
UiO‐66(Zr) metal–organic frameworks are chemically stable, biocompatible, and highly tunable nanomaterials. Their modular structure enables controlled drug delivery, multimodal bioimaging, and light‐activated photodynamic therapy, supporting integrated diagnostic and therapeutic (theranostic) applications in cancer and biomedical research.
Veronika Huntošová, Grigorii Rakhalskii, Miroslav Almáši   +2 more
wiley   +1 more source