Results 271 to 280 of about 3,930,063 (310)

Loss of AMBRA1 activates MAPK and angiogenesis signaling pathways in melanoma cells

open access: yesFEBS Open Bio, EarlyView.
Loss of AMBRA1 in melanoma cells activates multiple oncogenic pathways associated with tumor progression. Transcriptomic and protein network analyses revealed that AMBRA1 depletion enhances MAPK/ERK signaling, angiogenesis, TGF‐β/EMT signaling, and Wnt/axon guidance pathways.
Milad Ibrahim   +4 more
wiley   +1 more source

Effects of IGFBP4 deficiency on human preadipocyte proliferation and differentiation through the IGF1R/AKT pathway

open access: yesFEBS Open Bio, EarlyView.
IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo   +6 more
wiley   +1 more source

MagmaFlow: A desktop platform for artificial intelligence‐driven expression analysis

open access: yesFEBS Open Bio, EarlyView.
MagmaFlow is a free, no‐code platform for gene expression analysis. It generates interactive volcano plots, links genes to literature, pathways, and diseases, prioritizes candidates using millions of publications, identifies affected biological processes, builds network diagrams, and exports publication‐ready figures and reports for macOS and Windows ...
Carlos E. Buss   +7 more
wiley   +1 more source

Conformation of the Backbone in Unfolded Proteins

Chemical Reviews, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Kang Chen   +2 more
exaly   +3 more sources

Conformation spaces of proteins

Proteins: Structure, Function, and Bioinformatics, 2001
We report a simple method for measuring the accessible conformational space explored by an ensemble of protein structures. The method is useful for diverse ensembles derived from molecular dynamics trajectories, molecular modeling, and molecular structure determinations. It can be used to examine a wide range of time scales.
D C, Sullivan, I D, Kuntz
openaire   +2 more sources

Conformational spectra — probing protein conformational changes

Biophysical Chemistry, 1999
Stafford [Biophys. J. 17 (1996) MP452] has shown that it is possible, using the analytical ultracentrifuge in sedimentation velocity mode, to calculate the molecular weights of proteins with a precision of approximately 5%, by fitting Gaussian distributions to g(s*) profiles so long as partial specific volume and the radial position of the meniscus are
N, Errington, O, Byron, A J, Rowe
openaire   +2 more sources

Protein conformational prediction

Trends in Biochemical Sciences, 1989
The prediction of the secondary and tertiary structure of globular and membrane proteins is reviewed. Prospects are encouraging for future developments, but present algorithms require cautious interpretation.
openaire   +2 more sources

Conformation of Polypeptides and Proteins

1968
Publisher Summary This chapter deals with the recent developments regarding the description and nature of the conformation of proteins and polypeptides with special reference to the stereochemical aspects of the problem. This chapter considers the parameters that are required for an adequate description of a polypeptide chain.
Ramachandran, GN, Sasisekharan, V
openaire   +2 more sources

Characterizing Intermediate Conformations in Protein Conformational Space

2013
In this paper we present a novel parallel coordinate based clustering method using Gaussian mixture distribution models to characterize the conformational space of proteins. We detect highly populated regions which may correspond to intermediate states that are difficult to detect experimentally.
Rosanne Vetro   +2 more
openaire   +2 more sources

Conformational stability of globular proteins

Trends in Biochemical Sciences, 1990
The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
openaire   +2 more sources

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