Not exact matches
Within the framework of research projects of the German Center for Diabetes Research (DZD), scientists of the Research Unit
Protein Science (PROT) and the Institute of Experimental Genetics (IEG) at Helmholtz Zentrum München (HMGU) have now investigated
how drug treatment affects these
signal carriers.
A team led by Carnegie's Wolf Frommer has revealed
how membrane
proteins were networked with each other and with the
signaling proteins inside the cell.
Researchers still don't know
how this range corresponds to their versatile functions, but being more like a string than like a lump with keyholes means that a
protein can make many contacts with other molecules to regulate the network of
signals that drives the cell.
But little is known about
how ionizing radiation affects the extracellular matrix (ECM), a patchwork of
proteins and other biomolecules that surrounds cells and plays a vital role in their shape, movement and
signaling functions.
Future research will focus on
how this receptor works with ATP, its
protein structure,
how it reacts to pests and
how it may
signal growth.
Now, new research from the Salk Institute shows
how a
protein called p75 is critical for pain
signaling, which could one day have implications for treating neurological disorders as well as trauma such as spinal cord injury.
Researchers from UT Southwestern's Charles and Jane Pak Center for Mineral Metabolism and Clinical Research and Internal Medicine's Division of Nephrology recently published work in Nature that reveals the molecular structure of the so - called «anti-aging»
protein alpha Klotho (a-Klotho) and
how it transmits a hormonal
signal that controls a variety of biologic processes.
«Scientists determine structure of enzyme linked with key cell -
signaling protein: Findings aid understanding of
how modifications to cell -
signaling protein affect its action in turning genes on and off.»
Still unclear is
how the methuselah gene mutation makes flies more stress - resistant, but the amino acid sequence of the
protein it makes may be part of a
signaling pathway that controls
how well cells resist or repair these stresses.
«The computational approach allows us to model, right down to the atomic level,
how small changes in
protein sequence can have a major impact on
signaling,» said MacDermaid, assistant professor of research at Temple's Institute for Computational Molecular Science.
That will require fully characterizing the
protein and figuring out
how DAZAP1 senses external
signals like nutrients or growth factors that regulate its properties.
This study reveals
how lipids control SH2 domain - mediated cellular
protein interaction networks and suggests a new strategy for the therapeutic modulation of pY -
signaling pathways.
«Intracellular
signaling depends on these
protein modifications — so by doing these analysis, we know not only what's in the cell, but also
how the cell organizes and communicates internally.»
By tracking
how the levels of the CA125
protein change over time we might have an early
signal to detect tumours.
Cell receptors will receive a
signal from outside, and when it binds, that information is transmitted through the receptor to other
proteins within the cell, [creating] a chain of events to change
how the gene works in the cell.
The molecular details of
how these viruses self - assemble protective
protein containers around their cognate genomes in a specific and efficient manner have been revealed and illustrate multiple contacts between coat
proteins and dispersed packaging
signals in the viral genome.
To figure out
how signalling pathways work, molecular biologists carry out and validate experiments, sometimes over many years, to characterise the exact interactions taking place between
proteins.
Although Yersinia's molecular syringe for shooting up macrophages was discovered 4 years ago, scientists couldn't figure out
how the bacteria knew what to load into it; the toxins, called Yersinia outer
proteins (Yops), had no apparent amino acid
signal for secretion.
Sartori and his team wanted to find out whether and
how the
signal pathway and the repair
protein CtIP interact with one another.
During the early years of my PhD studies, I was very fascinated by the exciting discoveries in the field of
signal transduction, in particular
how receptor tyrosine kinases are activated to transmit their
signals and
how protein complexes are formed through defined
protein folds (domains) interacting with specific cellular targets.
In a separate study, published in September by the journal eLife, Butler and her colleagues discovered
how signals from a family of
proteins called bone morphogenetic
proteins, or BMPs, influence the development of sensory interneurons in chicken embryos.
It locks onto and deactivates a
protein, Smoothened, that activates the Hedgehog
signaling pathway, which orchestrates
how embryonic stem cells develop.
Researchers have identified a
protein that controls
how breast cancer cells spread around the body, according to a Cancer Research UK - funded study published in Science
Signaling.
For the first time, they have uncovered the structural details of
how some
proteins interact to turn two different
signals into a single integrated output.
Researchers from North Carolina State University and the University of North Carolina at Chapel Hill have discovered
how two important proofreader
proteins know where to look for errors during DNA replication and
how they work together to
signal the body's repair mechanism.
Scientists from The Scripps Research Institute Florida campus have uncovered the structural details of
how some
proteins interact to turn two different
signals into a single integrated output.
To better understand
how insulin
signaling affects beta - cell growth, the Joslin scientists next studied a pathway involving a
protein called FOXM1.
When Walter arrived in Blobel's lab as a fresh - faced apprentice, Blobel and his colleagues had limned the outlines of the so - called
signal hypothesis, which purported to explain
how proteins, which are made in cellular machines called ribosomes, find their pre-destined locations within cells.
Studies are being carried out to determine the functional effects that occur when these receptor - ligands interact; to determine
how these
proteins induce their activities at the molecular level and transmit
signals to T cells; and to determine the significance of these
proteins in several disease scenarios such as asthma, scleroderma, and atopic dermatitis.
«Knowing the subcellular location of a given
protein is of great importance as it indicates the
protein function and leads to a better understanding of
how and why
proteins interact in networks and
signaling pathways.»
It is located on the long arm of chromosome 15 in the LINGO1 gene, which encodes a
protein that has been shown to affect
how neurons are formed and
signal each other.
It will be important, Panne says, to dissect in detail
how scaffold
proteins, such as the CBP and p300 co-activators, contribute to the rich gene regulatory language,
how such chromatin modifiers are targeted to the genome,
how their activity is regulated, and
how chromatin modifications contribute to the
signaling reaction.
Given their close proximity and the tendency of investigators to assign a GWAS hit to the nearest
protein - coding gene, I wonder
how often a genetic
signal from a p - lncRNA is erroneously assigned to the mRNA instead.
Beyond the internal interactions of the
protein itself, these designed oligomers can be used to explore basic questions about
how the structure of
signaling molecules affects the behavior of receptors and cellular response.
The aim of this study is to characterize
how neurons from the mediobasal hypothalamus respond to a
signal of
protein availability: the amino acid l - leucine.
His doctoral thesis revealed
how isoprenylation of MIEN1
protein can regulate its translocation to the plasma membrane and activate
signaling events leading to increased invasive phenotype (JBC, 2011; Mol Can, 2015).
We still don't know
how exactly
protein increases satiety, but some studies have suggested that
protein has an important beneficial influence on the secretion of CCK (cholecystokinin), the hormone responsible for acting as a satiety
signal, and ghrelin, the main hunger hormone in our bodies.
These
signals tell the body
how to metabolize fats,
proteins and carbohydrates, and
how to cope with «environmental stress».
In the following the scientist gives his explanation
how to reverse it: «These new insights into Western diet - mediated mTORC1 - hyperactivity provide a rational basis for dietary intervention in acne by attenuating mTORC1
signaling by reducing (1) total energy intake, (2) hyperglycemic carbohydrates, (3) insulinotropic dairy
proteins and (4) leucine - rich meat and dairy
proteins.