Results 91 to 100 of about 5,878 (170)

HMGA1, Moonlighting Protein Function, and Cellular Real Estate: Location, Location, Location! [PDF]

Biomolecules, 2021
Pujals M, Resar L, Villanueva J.
europepmc   +1 more source

Moonlighting proteins - an approach to systematize the concept

In Silico Biology: Journal of Biological Systems Modeling and Multi-Scale Simulation, 2019
Moonlighting refers to a protein with at least two unrelated, mechanistically different functions. As a concept, moonlighting describes a large and diverse group of proteins which have been discovered in a multitude of organisms. As of today, a systematized view on these proteins is missing. Here, we propose a classification of moonlighting proteins by
Krantz, Maria, Klipp, Edda
openaire   +3 more sources

Nuclear entry of AS160 as a transcriptional regulator of satellite cells for muscle regeneration

Nature Communications
Dysfunction of muscle satellite cells is linked to diabetic myopathy. The mechanisms vitiating muscle satellite cell proliferative activity in diabetes are not well understood.
Xinyu Yang, Ye Cao, Yuwei Zhou, Qing Yao, Ping Rong, Xu Wang, Qiaoli Chen, Weikuan Feng, Li Zhang, Heng Ai, Dahai Zhu, Lei Fang, Tong-Jin Zhao, Xinhua Ye, Hong-Yu Wang, Shuai Chen   +15 more
doaj   +1 more source

Two independent activities define Ccm1p as a moonlighting protein in Saccharomyces cerevisiae

Bioscience Reports, 2012
Ccm1p is a nuclear-encoded PPR (pentatricopeptide repeat) protein that localizes into mitochondria of Saccharomyces cerevisiae. It was first defined as an essential factor to remove the bI4 [COB (cytochrome b) fourth intron)] and aI4 [COX1 (cytochrome c ...
J. Ignacio Moreno, Babu Patlolla, Kerry R. Belton, Brenita C. Jenkins, Polina V. Radchenkova, Marta A. Piva   +5 more
doaj   +1 more source

Enolase 1, a Moonlighting Protein, as a Potential Target for Cancer Treatment. [PDF]

Int J Biol Sci, 2021
Qiao G, Wu A, Chen X, Tian Y, Lin X.
europepmc   +1 more source

Moonlighting on the Fasciola hepatica tegument: Enolase, a glycolytic enzyme, interacts with the extracellular matrix and fibrinolytic system of the host.

PLoS Neglected Tropical Diseases
Enolase is a 47 kDa enzyme that functions within the glycolysis and gluconeogenesis pathways involved in the reversible conversion of D-2-phosphoglycerate (2PGA) to phosphoenolpyruvate (PEP). However, in the context of host-pathogen interactions, enolase
Eve O'Kelly, Krystyna Cwiklinski, Carolina De Marco Verissimo, Nichola Eliza Davies Calvani, Jesús López Corrales, Heather Jewhurst, Andrew Flaus, Richard Lalor, Judit Serrat, John P Dalton, Javier González-Miguel   +10 more
doaj   +1 more source

Functional mapping of the N-terminal region of the yeast moonlighting protein Sis2/Hal3 reveals crucial residues for Ppz1 regulation. [PDF]

FEBS J, 2022
Santolaria C, Velázquez D, Albacar M, Casamayor A, Ariño J.   +4 more
europepmc   +1 more source

Enolase of Staphylococcus lugdunensis Is a Surface-Exposed Moonlighting Protein That Binds to Extracellular Matrix and the Plasminogen/Plasmin System. [PDF]

Front Microbiol, 2022
Hussain M, Kohler C, Becker K.
europepmc   +1 more source

Correction to: Moonlighting protein prediction using physico‑chemical and evolutional properties via machine learning methods. [PDF]

BMC Bioinformatics, 2021
Shirafkan F, Gharaghani S, Rahimian K, Sajedi RH, Zahiri J.   +4 more
europepmc   +1 more source

Moonlighting Proteins [PDF]

Biophysical Journal, 2014
Jeffery, Constance, Mani, Matt, Amblee, Vaishak, Chen, Chang   +3 more
openaire   +1 more source