Results 111 to 120 of about 6,845,089 (390)
Frontiers in Microbiology, 2019 The application of D-stereospecific proteases (DSPs) in resolution of racemic amino acids and in the semisynthesis of proteins has been a successful strategy.
Andreas H. Simon +4 more
doaj +1 more source
Molecular Oncology, EarlyView.Integrating ancestry, differential methylation analysis, and machine learning, we identified robust epigenetic signature genes (ESGs) and Core‐ESGs in Black and White women with endometrial cancer. Core‐ESGs (namely APOBEC1 and PLEKHG5) methylation levels were significantly associated with survival, with tumors from high African ancestry (THA) showing ...
Huma Asif, J. Julie Kim
wiley +1 more source
A Conversation on Protein Folding [PDF]
Journal of Biomolecular Structure and Dynamics, 2011 (2011). A Conversation on Protein Folding. Journal of Biomolecular Structure and Dynamics: Vol. 28, No. 4, pp. 587-588.
openaire +3 more sources
Protein folding using contact maps
, 1999 We present the development of the idea to use dynamics in the space of contact maps as a computational approach to the protein folding problem. We first introduce two important technical ingredients, the reconstruction of a three dimensional conformation
A. Bairoch +33 more
core +1 more source
Molecular Oncology, EarlyView.Loss of the frequently mutated chromatin remodeler ARID1A, a subunit of the SWI/SNF cBAF complex, results in less open chromatin, alternative splicing, and the failure to stop cells from progressing through the cell cycle after DNA damage in bladder (cancer) cells. Created in BioRender. Epigenetic regulators, such as the SWI/SNF complex, with important
Rebecca M. Schlösser +11 more
wiley +1 more source
Chaperones and protein folding
Current Opinion in Cell Biology, 1992 Chaperones are centrally involved in the control of protein structure, function, localization and transport. A flurry of scientific activity continues to examine the molecular nature of chaperone-substrate recognition and the role of auxiliary chaperones (cohort proteins) and small molecules that expedite these processes.
Kelley, William, Georgopoulos, C.
openaire +4 more sources
Steric trapping reveals a cooperativity network in the intramembrane protease GlpG. [PDF]
, 2016 Membrane proteins are assembled through balanced interactions among proteins, lipids and water. Studying their folding while maintaining the native lipid environment is necessary but challenging.
Gaffney, Kristen +7 more
core +1 more source
Hydrodynamic Interactions in Protein Folding
, 2008 We incorporate hydrodynamic interactions (HI) in a coarse-grained and structure-based model of proteins by employing the Rotne-Prager hydrodynamic tensor. We study several small proteins and demonstrate that HI facilitate folding.
Dhont J. K. G. +2 more
core +1 more source
Protein Folding and Mechanisms of Proteostasis
International Journal of Molecular Sciences, 2015 Highly sophisticated mechanisms that modulate protein structure and function, which involve synthesis and degradation, have evolved to maintain cellular homeostasis. Perturbations in these mechanisms can lead to protein dysfunction as well as deleterious
José Fernando Díaz-Villanueva +2 more
semanticscholar +1 more source
Molecular Oncology, EarlyView.Chronic TGF‐β exposure drives epithelial HCC cells from a senescent state to a TGF‐β resistant mesenchymal phenotype. This transition is characterized by the loss of Smad3‐mediated signaling, escape from senescence, enhanced invasiveness and metastatic potential, and upregulation of key resistance modulators such as MARK1 and GRM8, ultimately promoting
Minenur Kalyoncu +11 more
wiley +1 more source