Transport proteins: A series
of transport proteins (multi drug resistant proteins, or MRPs) are responsible for getting the conjugated mercury out of your cells and into your blood, as well as from your blood into your liver and small intestine, and into other places so it can be eliminated
New supercomputer simulations have revealed the role
of transport proteins called efflux pumps in creating drug - resistance in bacteria, research that could lead to improving the drugs» effectiveness against life - threatening diseases and restoring the efficacy of defunct antibiotics.
People with the transthyretin amyloidosis have mutations in the DNA of the transthyretin gene, which causes abnormal buildup and deposits
of a transport protein called transthyretin in nerve and heart cells.
Two key events enabled organelles to develop: The precursor bacteria transferred many of their genes to the host's genome, and they developed a method
of transporting the proteins produced by these and other genes back inside their own membranes.
The flowers of petunias that made normal amounts
of the transport protein PhABCG1 (top row) are larger and healthier than the flowers of petunias engineered to produce less of the protein.
Hartnup's disease is a hereditary (autosomal recessive) disorder in which the absorption of tryptophan and certain other amino acids in the small intestine and their reabsorption in the kidneys is reduced due to a lack
of a transport protein, which may lead to tryptophan deficiency and this in turn to vitamin B3 (niacin) deficiency [6].
Fructose absorption depends on the amount
of transport protein GLUT5 in the small intestinal wall.
Not exact matches
Amino acids are the building blocks
of protein, assisting with the maintenance
of lean muscle mass,
transport of nutrients, tissue repair and immunity.
He eats the
protein truffles one bite at a time and is
transported to the land
of deliciousness.
When considering the
protein source, for example, one must not only consider whether an animal - or plant - based
protein will be used, but the specific organism from which it is derived (e.g., animal: chicken, beef, lamb, pork, etc.; fish: salmon, menhaden, etc.; plant: corn gluten meal, soybean meal, etc.), what part (s)
of that organism will be included (e.g., plant: whole wheat vs. wheat germ vs. wheat bran; animal: entire animal vs. skeletal muscle vs. organ meats), and the form in which it will be added (animals: frozen, fresh, meal), all
of which affect the diet in terms
of cost, nutrient composition and stability, manufacturing requirements, and ingredient handling,
transport, and storage.
Because triglycerides and cholesterol can't dissolve in blood, they circulate throughout your body with the help
of proteins that
transport the lipids (lipoproteins).
Genes significantly expressed across all stages
of lactation are associated with making, modifying,
transporting, and packaging milk
proteins.
But in 2013, a research scientist in El - Naggar's laboratory, Sahand Pirbadian, discovered that these projections, referred to as «nanowires,» were actually extensions
of the cell membrane covered in cytochromes —
proteins containing iron that facilitate electron
transport.
When looking for genes that might play important roles in the metabolism
of healthy and cancerous liver cells, Wang and his colleagues became interested in a gene called SLC13A5, which produces a
protein that
transports citrate into cells.
Francis Barr, a junior research group leader at the Max Plank Institute
of Biochemistry, studies
protein transport.
These include more sensitive mass spectrometry for detecting, identifying and quantifying
protein molecules, electron microscopy for visualizing an assortment
of components
of the nano - machine that
transports toxins, and fluorescence confocal microscopy, which can label
proteins with light emitting dyes.
Columbia researchers have uncovered new roles for
proteins of the electron
transport chain that implicate them in utilization
of phenazines.
They found that the electron
transport chain so critical to the conversion
of electrons to energy can and is operating deep down in the oxygen - deprived biofilm and that in these environments, the bacterium depends on a specific part
of the chain's terminal oxidase — a
protein called CcoN4 — to access oxygen and grow normally.
Over the past 15 years, the GFP gene has enabled scientists to watch a plethora
of previously murky biological processes in action: how nerve cells develop in the brain, how insulin - producing beta cells form in the pancreas
of an embryo, how
proteins are
transported within cells, and how cancer cells metastasize through the body.
«Synthetic
proteins help solve structure
of the fluoride ion channel: Unexpected double - barreled «channsporter» structure suggests new mechanism for ion
transport.»
The focus
of their research is «exosomes», small virus - like particles that serve as «
transport packages» for genetic material and
proteins transmitted between cells.
The task
of HLAs is to bind to fragments
of proteins that are broken down in the cells,
transport the fragments to the cell surface and present them to the T - lymphocytes.
A group
of LMU physicists led by Professor Erwin Frey, in collaboration with Professor Stefan Diez (Technical University
of Dresden and Max Planck Institute for Molecular Cell Biology and Genetics, Dresden), has now developed a model in which the motor
proteins that are responsible for the
transport of cargo along protofilaments also serve to regulate microtubule lengths.
Toward the end
of her postdoc, Chacinska identified a
protein called Mia40, whose role was to
transport precursor
proteins to the space lying between the outer and inner membranes
of mitochondria.
What's more, a tweak Chacinska made to a standard experimental protocol allowed her lab to become the first to discover a mitochondrial
protein transport mechanism based on the recognition
of newly formed disulphide bonds.
Two theorists whose work set the stage for finding the Higgs boson won the Nobel Prize in physics this week, while three biologists who explored various aspects
of how cells package,
transport, and release their internal
proteins earned the physiology or medicine prize.
Meanwhile, the selectors for the physiology or medicine prize honored three biologists who explored various aspects
of how cells package,
transport, and release their internal
proteins.
To function, most
of the newly - produced
proteins first need to be sorted and then
transported within and outside
of the cell.
When the researchers administered drugs to inhibit the movement
of certain «motor»
proteins that
transport mitochondria and other cargo within the cell by traveling along microtubules, the mitochondria accumulated in the axon
of the neuron and never made it to the synaptic terminal.
Nielsen believes the secret is a bacterial pulley system
of sorts: Oxygen - processing bacteria at the top connect to digestive microbes below via long
protein threads that
transport electrons.
Using fluorescence inside living cells as well as biochemistry, they showed that SMN promotes an interaction between the «zipcode» region
of a test RNA and a
transport protein.
Whether in a yeast cell or in a neuron, alpha synuclein directly interfered with the rate
of production
of proteins in the cell, and the
transport of proteins between cellular compartments.
Both groups had unusually low levels
of a
protein that
transports serotonin — a hormone involved in regulating mood — around the brain.
In both trials, levels
of two
proteins that play major roles in
transporting beta - amyloid out
of the brain as well as enzymes that degrade beta - amyloid increased significantly after administering oleocanthal.
Their major hurdle: to come up with a replacement for hemoglobin (an iron - enriched
protein in red blood cells that
transports oxygen from the lungs to the rest
of the body) that can be directly introduced into the human circulatory system.
A
protein that
transports the simple chemical choline plays a major role in vesicle trafficking, ion homeostasis, and growth and development in plants, according to two new studies publishing 28 December in the open - access journal PLOS Biology, by Dai - Yin Chao
of the Shanghai Institutes for Biological Sciences, China, and Sheng Luan
of the University
of California, Berkeley, USA, and co-workers.
Anthrax poisonings, as well as cholera infections, work in part by disrupting the normal
transport mechanisms
of proteins.
The study, «The nuclear
transport receptor Importin - 11 is a tumor suppressor that maintains PTEN
protein,» which will be published online February 13 in The Journal
of Cell Biology, suggests that the loss
of Importin - 11 may destabilize PTEN, leading to the development
of lung, prostate, and other cancers.
Changes to the properties
of the lipid bilayer component
of the cell membrane can alter the function
of proteins embedded in the membrane —
proteins that regulate critical functions such as
transport of materials in and out
of the cell and communication with other cells.
The deficiency, they reasoned, would cause the rats to make more
of the putative iron -
transport protein, making it easier to find.
This small
protein molecule contains a loop which fits, like a key in a lock, into the ion channel
proteins found on nerve cell membranes, which are used to
transport sodium and potassium ions in and out
of the cell.
In 2016, Collins and colleagues published evidence
of proteins on ostrich shells that were almost 4 million years old — the connection to human evolution may not be readily apparent, but such shells have been used by hominins for millions
of years to
transport water and other resources.
Members
of the kinesin superfamily
of motor
proteins are essential for mitotic and meiotic spindle organization, chromosome segregation, organelle and vesicle
transport, and many other processes that require microtubule - based
transport.
The
transport protein contains an ion binding site located at the center
of the membrane that is composed
of conserved amino acids.
As a cofactor
of certain
proteins, it plays an essential role in oxygen
transport and metabolism.
«Structure
of an iron -
transport protein revealed.»
Ines Ehrnstorfer, a PhD student in the group
of Professor Raimund Dutzler at the Department
of Biochemistry
of the University
of Zurich, and her colleagues, have determined the first structure
of an iron
transport protein.
The researchers studied mutations that alter the function
of hemoglobin, the
protein in charge
of transporting oxygen in the blood.
This vaccine uses an inactive herpes virus (stripped
of its viral genes) to
transport a small amount
of Aß as well as another
protein called interleukin - 4 that may help prevent brain inflammation.
In their Perspective, Knepper and Agre discuss an exciting study (Khademi et al.) that reports resolution
of the crystallographic structure
of a bacterial ammonia
transport channel, AmtB, to an astonishing 1.35 angstroms, an amazing feat for an integral membrane
protein.