As a basic researcher, he has been most interested in looking for ideas that point toward new directions in the field: a new role for a protein or a new understanding of
how cellular proteins drive the immune response.
UCLA scientists have uncovered
how a cellular protein contributes to an aggressive form of leukemia prevalent in young children.
Not exact matches
Actually, science has been able to show
how the very first
proteins and
cellular organism did evolve from non-life.
Ribosomes, the
cellular factories that manufacture
proteins, contain both RNA and
protein, but exactly
how all of the different ribosomal components contribute to
protein synthesis is still not clear.
Allan Jacobson, Ph.D., of the University of Massachusetts Medical School and co-founder of PTC Therapeutics, the company that developed ataluren, and David Bedwell, Ph.D., professor of the UAB Department of Biochemistry and Molecular Genetics, have sought to understand precisely
how ataluren allows the ribosome, the machinery of
cellular protein synthesis, to skip over these inserted stop signs and produce
proteins that have normal or near - normal function.
They used this novel simulation approach to build a model of a sperm cell that demonstrates
cellular movement from individual dynein
protein molecules in the tail all the way up to the whole cell, allowing them to observe
how changes at the atomic level are reflected in larger - scale structures.
In their study, the Salk scientists sought to determine precisely
how the mutated WRN
protein causes so much
cellular mayhem.
However, it was unclear exactly
how the mutated WRN
protein disrupted these critical
cellular processes.
However, the researchers found that a well - known
cellular mechanism — one that controls
how proteins acquire new functions — also plays a major role.
To find out why, computational biologists came up with a computer model to predict
how microbial metabolism and
cellular composition change as cell size varies, using details about
how much space a bacterium needs for its components — DNA,
proteins, and the molecular factories called ribosomes — to function.
New work led by Carnegie's David Ehrhardt hones in on
how one particular organizational
protein influences cytoskeletal and
cellular structure in plants, findings that may also have implications for cytoskeletal organization in animals.
The research team has been using NMR — a technique related to the one used in MRI body scanners and capable of visualising molecules at the smallest scales — to examine
how small components of herpes virus help it to multiply by binding themselves with other large molecules; this produced images of a monkey herpes virus
protein interacting with mouse
cellular protein and viral RNA.
The laboratory of Marcos Malumbres, who is head of the Spanish National Cancer Research Centre's (CNIO) Cell Division & Cancer Group, working alongside Isabel Fariñas» team from the University of Valencia, shows, in a study published today in the journal Nature Communications,
how in mice the elimination of the Cdh1
protein — a sub-unit of the APC / C complex, involved in the control of cell division — prevents
cellular proliferation of rapidly dividing cells.
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.
Now scientists have a clearer view of
how ISRIB works — by pinning together parts of a
protein involved in
cellular stress.
«The longer we study these classes of
proteins, the clearer it becomes
how adept these molecules are at interfering with
cellular growth to such an extent that makes normal control virtually impossible,» says Prof. Slany.
Now, researchers at the University of Missouri have developed a three - dimensional microscope that will yield unparalleled study of membrane
proteins and
how they interact on the
cellular level.
The team of researchers uncovered the molecular basis of the interaction between these
proteins, and
how TACC3 recruits chTOG to the microtubules during
cellular division.
They've learned
how the super-strong and mega-long
protein threads secreted by the eel - like animals are organized at the
cellular level.
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.
Now one team, reporting in the journal ACS Chemical Neuroscience, has identified
how amyloid beta, the
protein fragment strongly associated with Alzheimer's disease, can induce
cellular changes that might lead to Parkinson's.
But until he understands
how the cells are stressed in the first place, he won't know much: «We frankly don't have a clue as to
how much microwave radiation is needed to cause irreversible damage to
cellular proteins.
So far, we know that aspirin inhibits the production of
proteins known as prostaglandins, which help control the
cellular communication that controls
how cells proliferate.
Although some of the key molecular components involved in the formation of
cellular structures and tissue formation are known, we currently lack a bottoms up understanding of
how the behavior of these molecules gives rise to the formation of large structures, partly because of the lack of tools for both studying the spatial regulation of soluble
proteins and biophysically characterizing the behavior of large structures and tissues.
Salk researchers show
how DNA repair
proteins distinguish DNA breaks at
cellular and viral genomes to activate an appropriately scaled response.
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.
Finally, in a collaboration with Frank Jülicher's group at the Max Planck Institute for the Physics of Complex Systems, we are using these data to develop physical models that will help us understand
how local
cellular adhesive, elastic and contractile properties are influenced by PCP
proteins and other molecules, and
how they combine to produce specific packing geometries at a global level.
The Sarma laboratory is interested in the mechanisms of epigenetic gene regulation, or
how the dynamic modifications of the architecture of chromatin, the complex of DNA and
proteins within the nucleus of our cells, impacts gene expression and
cellular function.
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.
Previously a distinguished professor in the University of Minnesota's Department of Biochemistry, Molecular Biology and Biophysics, Kalodimos» research into the
cellular machinery relevant to cancer has led to important insights into
how mutated
proteins can drive the development and spread of the disease.
In the study, the researchers describe the microscopic physical interactions and chemical changes of
proteins associated with several
cellular functions, including disease forms, and
how still - healthy cells could try to temper it.
The study that will be published in the March 21 issue of the science magazine Cell describes
how insulin, through the activity of an enzyme recently described by the Freiburg research team, blocks one of the most important
cellular stress regulators, a
protein called SKN - 1.