Results 11 to 20 of about 114,928,473 (245)

A proteomic analysis of lipid raft and GPI anchored proteins in Caenorhabditis elegans [PDF]

open access: yes, 2010
Glycosylphosphatidylinositol (GPI) anchored proteins are a unique group of membrane proteins found on the surface and certain intracellular compartments of eukaryotic cells.
Rao, Wei
core   +6 more sources

NAPRT loss promotes lung tumor initiation and growth through AKT signaling independently of NAD<sup>+</sup> biosynthesis. [PDF]

open access: yesMol Oncol
Loss of NAPRT promotes lung tumor initiation and growth through a noncanonical mechanism, independent of its role in NAD+ biosynthesis. Mechanistically, NAPRT depletion activates the mTORC2‐driven AKT/β‐catenin signaling axis to enhance clonogenic and invasive phenotypes. Furthermore, lung‐specific Naprt deletion significantly increases tumor burden in
Oh MJ   +11 more
europepmc   +2 more sources

Re-expression of AKAP12 inhibits progression and metastasis potential of colorectal carcinoma in vivo and in vitro. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: AKAP12/Gravin (A kinase anchor protein 12) is one of the A-kinase scaffold proteins and a potential tumor suppressor gene in human primary cancers.
Weiwei Liu   +4 more
doaj   +1 more source

Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?

open access: yesFrontiers in Oncology, 2020
Cellular functions are regulated by extracellular signals such as hormones, neurotransmitters, matrix ligands, and other chemical or physical stimuli.
Camille Albrecht   +19 more
doaj   +1 more source

cAMP-Dependent Signaling Pathways as Potential Targets for Inhibition of Plasmodium falciparum Blood Stages

open access: yesFrontiers in Microbiology, 2021
We review the role of signaling pathways in regulation of the key processes of merozoite egress and red blood cell invasion by Plasmodium falciparum and, in particular, the importance of the second messengers, cAMP and Ca2+, and cyclic nucleotide ...
Edwin Lasonder   +11 more
doaj   +1 more source

Multiple determinants direct the orientation of signal-anchor proteins : the topogenic role of the hydrophobic signal domain [PDF]

open access: yes, 1997
The orientation of signal-anchor proteins in the endoplasmic reticulum membrane is largely determined by the charged residues flanking the apolar, membrane-spanning domain and is influenced by the folding properties of the NH2-terminal sequence. However,
Martin Spiess   +3 more
core   +1 more source

Mechanism of activation of NDR protein kinase by the HMOB1 protein [PDF]

open access: yes, 2005
Serine/threonine kinases of the nuclear Dbf2-related (NDR) family are highly conserved throughout the eukaryotic world. Members of this kinase family are implicated in various aspects of the regulation of cell division and cell morphology. It has been
Bichsel, Samuel J.
core   +1 more source

A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life. [PDF]

open access: yes, 2012
Selenoproteins serve important functions in many organisms, usually providing essential oxidoreductase enzymatic activity, often for defense against toxic xenobiotic substances.
Dudkiewicz, Małgorzata   +3 more
core   +2 more sources

A dynamic interface between ubiquitylation and cAMP signaling

open access: yesFrontiers in Pharmacology, 2015
Phosphorylation waves drive the propagation of signals generated in response to hormones and growth factors in target cells. cAMP is an ancient second messenger implicated in key biological functions. In mammals, most of the effects elicited by cAMP are
Laura eRinaldi   +3 more
doaj   +1 more source

Virulent and avirulent strains of Toxoplasma gondii which differ in their glycosylphosphatidylinositol content induce similar biological functions in macrophages [PDF]

open access: yes, 2014
Glycosylphosphatidylinositols (GPIs) from several protozoan parasites are thought to elicit a detrimental stimulation of the host innate immune system aside their main function to anchor surface proteins.
Ricardo T. Gazzinelli (164680)   +43 more
core   +2 more sources

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