Results 61 to 70 of about 114,998 (297)

miRNA‐29 regulates epidermal and mesenchymal functions in skin repair

open access: yesFEBS Letters, EarlyView.
miRNA‐29 inhibits cell‐to‐cell and cell‐to‐matrix adhesion by silencing mRNA targets. Adhesion is controlled by complex interactions between many types of molecules coded by mRNAs. This is crucial for keeping together the layers of the skin and for regenerating the skin after wounding.
Lalitha Thiagarajan   +10 more
wiley   +1 more source

Autophagy in cancer and protein conformational disorders

open access: yesFEBS Letters, EarlyView.
Autophagy plays a crucial role in numerous biological processes, including protein and organelle quality control, development, immunity, and metabolism. Hence, dysregulation or mutations in autophagy‐related genes have been implicated in a wide range of human diseases.
Sergio Attanasio
wiley   +1 more source

Nucleation of amyloid fibrils [PDF]

open access: yesJ. Chem. Phys. 132, 215101 (2010), 2010
We consider nucleation of amyloid fibrils in the case when the process occurs by the mechanism of direct polymerization of practically fully extended protein segments, i.e. beta-strands, into beta-sheets. Applying the classical nucleation theory, we derive a general expression for the work to form a nanosized amyloid fibril (protofilament) constituted ...
arxiv   +1 more source

The atypical KRASQ22K mutation directs TGF‐β response towards partial epithelial‐to‐mesenchymal transition in patient‐derived colorectal cancer tumoroids

open access: yesMolecular Oncology, EarlyView.
TGF‐β has a complex role in cancer, exhibiting both tumor‐suppressive and tumor‐promoting properties. Using a series of differentiated tumoroids, derived from different stages and mutational background of colorectal cancer patients, we replicate this duality of TGF‐β in vitro. Notably, the atypical but highly aggressive KRASQ22K mutation rendered early‐
Theresia Mair   +17 more
wiley   +1 more source

Modeling generic aspects of ideal fibril formation [PDF]

open access: yesJ. Chem. Phys. 144, 035101 (2016), 2016
Many different proteins self-aggregate into insoluble fibrils growing apically by reversible addition of elementary building blocks. But beyond this common principle, the modalities of fibril formation are very disparate, with various intermediate forms which can be reshuffled by minor modifications of physico-chemical conditions or amino-acid ...
arxiv   +1 more source

Relationships between the tensile strength and diameter of collagen fibrils isolated from mouse tail tendons

open access: yesJournal of Biomechanical Science and Engineering, 2017
The purpose of the present study is to determine the tensile properties of the single collagen fibrils with various diameters using our original tensile test method. The fibrils were directly isolated from mouse tail tendons.
Noritaka YAMAMOTO, Shun NAKAMURA
doaj   +1 more source

Spatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrils. [PDF]

open access: yesPLoS ONE, 2011
Formation of large protein fibrils with a characteristic cross β-sheet architecture is the key indicator for a wide variety of systemic and neurodegenerative amyloid diseases.
Shannon E Hill   +3 more
doaj   +1 more source

Escape from TGF‐β‐induced senescence promotes aggressive hallmarks in epithelial hepatocellular carcinoma cells

open access: yesMolecular 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

Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]

open access: yes, 2015
The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio   +9 more
core   +2 more sources

Targeting the AKT/mTOR pathway attenuates the metastatic potential of colorectal carcinoma circulating tumor cells in a murine xenotransplantation model

open access: yesMolecular Oncology, EarlyView.
Dual targeting of AKT and mTOR using MK2206 and RAD001 reduces tumor burden in an intracardiac colon cancer circulating tumor cell xenotransplantation model. Analysis of AKT isoform‐specific knockdowns in CTC‐MCC‐41 reveals differentially regulated proteins and phospho‐proteins by liquid chromatography coupled mass spectrometry. Circulating tumor cells
Daniel J. Smit   +19 more
wiley   +1 more source

Home - About - Disclaimer - Privacy