Proteins involved in the transport of NUCLEOTIDES across cellular membranes.
A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.
A glycoside of a kaurene type diterpene that is found in some plants including Atractylis gummifera (ATRACTYLIS); COFFEE; XANTHIUM, and CALLILEPIS. Toxicity is due to inhibition of ADENINE NUCLEOTIDE TRANSLOCASE.
Adenine nucleotides are molecules that consist of an adenine base attached to a ribose sugar and one, two, or three phosphate groups, including adenosine monophosphate (AMP), adenosine diphosphate (ADP), and adenosine triphosphate (ATP), which play crucial roles in energy transfer and signaling processes within cells.
An antibiotic produced by Pseudomonas cocovenenans. It is an inhibitor of MITOCHONDRIAL ADP, ATP TRANSLOCASES. Specifically, it blocks adenine nucleotide efflux from mitochondria by enhancing membrane binding.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
The mitochondria of the myocardium.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
A broad category of membrane transport proteins that specifically transport FREE FATTY ACIDS across cellular membranes. They play an important role in LIPID METABOLISM in CELLS that utilize free fatty acids as an energy source.
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)
The rate dynamics in chemical or physical systems.
The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Transport proteins that carry specific substances in the blood or across cell membranes.
A large group of membrane transport proteins that shuttle MONOSACCHARIDES across CELL MEMBRANES.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane.
The movement of ions across energy-transducing cell membranes. Transport can be active, passive or facilitated. Ions may travel by themselves (uniport), or as a group of two or more ions in the same (symport) or opposite (antiport) directions.
Membrane proteins whose primary function is to facilitate the transport of negatively charged molecules (anions) across a biological membrane.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The directed transport of ORGANELLES and molecules along nerve cell AXONS. Transport can be anterograde (from the cell body) or retrograde (toward the cell body). (Alberts et al., Molecular Biology of the Cell, 3d ed, pG3)
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A single nucleotide variation in a genetic sequence that occurs at appreciable frequency in the population.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Membrane transporters that co-transport two or more dissimilar molecules in the same direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Proteins found in any species of bacterium.
Guanine nucleotides are cyclic or linear molecules that consist of a guanine base, a pentose sugar (ribose in the cyclic form, deoxyribose in the linear form), and one or more phosphate groups, playing crucial roles in signal transduction, protein synthesis, and regulation of enzymatic activities.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
Purines attached to a RIBOSE and a phosphate that can polymerize to form DNA and RNA.
Proteins obtained from ESCHERICHIA COLI.
A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The functional hereditary units of BACTERIA.
A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Proteins that bind to and are involved in the metabolism of phosphate ions.

Uracil-induced down-regulation of the yeast uracil permease. (1/109)

In Saccharomyces cerevisiae the FUR4-encoded uracil permease catalyzes the first step of the pyrimidine salvage pathway. The availability of uracil has a negative regulatory effect upon its own transport. Uracil causes a decrease in the level of uracil permease, partly by decreasing the FUR4 mRNA level in a promoter-independent fashion, probably by increasing its instability. Uracil entry also triggers more rapid degradation of the existing permease by promoting high efficiency of ubiquitination of the permease that signals its internalization. A direct binding of intracellular uracil to the permease is possibly involved in this feedback regulation, as the behavior of the permease is similar in mutant cells unable to convert intracellular uracil into UMP. We used cells impaired in the ubiquitination step to show that the addition of uracil produces rapid inhibition of uracil transport. This may be the first response prior to the removal of the permease from the plasma membrane. Similar down-regulation of uracil uptake, involving several processes, was observed under adverse conditions mainly corresponding to a decrease in the cellular content of ribosomes. These results suggest that uracil of exogenous or catabolic origin down-regulates the cognate permease to prevent buildup of excess intracellular uracil-derived nucleotides.  (+info)

Membrane topology of the mammalian CMP-sialic acid transporter. (2/109)

Nucleotide sugar transporters form a family of distantly related membrane proteins of the Golgi apparatus and the endoplasmic reticulum. The first transporter sequences have been identified within the last 2 years. However, information about the secondary and tertiary structure for these molecules has been limited to theoretical considerations. In the present study, an epitope-insertion approach was used to investigate the membrane topology of the CMP-sialic acid transporter. Immunofluorescence studies were carried out to analyze the orientation of the introduced epitopes in semipermeabilized cells. Both an amino-terminally introduced FLAG sequence and a carboxyl-terminal hemagglutinin tag were found to be oriented toward the cytosol. Results obtained with CMP-sialic acid transporter variants that contained the hemagglutinin epitope in potential intermembrane loop structures were in good correlation with the presence of 10 transmembrane regions. This building concept seems to be preserved also in other mammalian and nonmammalian nucleotide sugar transporters. Moreover, the functional analysis of the generated mutants demonstrated that insertions in or very close to membrane-spanning regions inactivate the transport process, whereas those in hydrophilic loop structures have no detectable effect on the activity. This study points the way toward understanding structure-function relationships of nucleotide sugar transporters.  (+info)

Only one of the charged amino acids located in membrane-spanning regions is important for the function of the Saccharomyces cerevisiae uracil permease. (3/109)

The transport of uracil into the yeast Saccharomyces cerevisiae is mediated by uracil permease, a specific co-transporter encoded by the FUR4 gene. Uracil permease is a multispan membrane protein that is delivered to the plasma membrane via the secretory pathway. Experimental results led to the proposal of a two-dimensional model of the protein's topology. According to this model, the membrane domain of Fur4p contains three charged amino acid residues (Glu-243, Lys-272 and Glu-539) that are conserved in the members of the FUR family of yeast transporters. We have previously shown that a mis-sense mutation leading to the replacement of Lys-272 by Glu severely impairs the function of uracil permease. In the present paper, the role of the three charged residues present in the membrane-spanning regions of Fur4p was further investigated by using site-directed mutagenesis. The variant permeases were correctly targeted to the plasma membrane and their stabilities were similar to that of the wild-type permease. The effect of the mutations was studied by measuring the uptake constants for uracil on whole cells and equilibrium binding parameters on plasma membrane-enriched fractions. We found no evidence for ionic interaction between either of the glutamic residues in transmembrane segments 3 and 9 and the lysine residue in transmembrane segment 4. Of the three charged residues, only Lys-272 was important for the transport activity of the transporter. Its replacement by Ala, Glu or even Arg strongly impaired both the binding and the translocation of uracil.  (+info)

Transport of organic anions by the lysosomal sialic acid transporter: a functional approach towards the gene for sialic acid storage disease. (4/109)

Transport of sialic acid through the lysosomal membrane is defective in the human sialic acid storage disease. The mammalian sialic acid carrier has a wide substrate specificity for acidic monosaccharides. Recently, we showed that also non-sugar monocarboxylates like L-lactate are substrates for the carrier. Here we report that other organic anions, which are substrates for carriers belonging to several anion transporter families, are recognized by the sialic acid transporter. Hence, the mammalian system reveals once more novel aspects of solute transport, including sugars and a wide array of non-sugar compounds, apparently unique to this system. These data suggest that the search for the sialic acid storage disease gene can be initiated by a functional selection of genes from a limited number of anion transporter families. Among these, candidates will be identified by mapping to the known sialic acid storage disease locus.  (+info)

Expression and activity of chimeric molecules between human UDP-galactose transporter and CMP-sialic acid transporter. (5/109)

Human UDP-galactose transporter (hUGT1) and CMP-sialic acid transporter (hCST) are related Golgi proteins with eight putative transmembrane helices predicted by computer analysis. We constructed chimeric molecules in which segments of various lengths from the C- or N-terminus of hUGT1 were replaced by corresponding portions of hCST. The chimeras were transiently expressed in UGT-deficient mutant Lec8 cells, and their UGT activity was assessed by the binding of GS-II lectin to the transfected cells. The replacement of either the N- or C-terminal cytoplasmic segment by that of hCST did not affect the expression or activity of hUGT1. A chimera in which the eighth helix and the C-terminal tail were replaced also retained the UGT activity, indicating that this helix is not involved in the determination of substrate specificity. In contrast, three types of chimeras, in which the first helix, the first and the second helices, and a segment from the seventh helix to the C-terminus were replaced, respectively, were expressed very infrequently in the transfected cells, and had no UGT activity. They are likely folded incorrectly and degraded by a quality-control system, since the amounts of their mRNAs were normal and the proteins were mainly localized in the ER. The first and the seventh helices are important for the stability of the transporter protein.  (+info)

HRD gene dependence of endoplasmic reticulum-associated degradation. (6/109)

Work from several laboratories has indicated that many different proteins are subject to endoplasmic reticulum (ER) degradation by a common ER-associated machinery. This machinery includes ER membrane proteins Hrd1p/Der3p and Hrd3p and the ER-associated ubiquitin-conjugating enzymes Ubc7p and Ubc6p. The wide variety of substrates for this degradation pathway has led to the reasonable hypothesis that the HRD (Hmg CoA reductase degradation) gene-encoded proteins are generally involved in ER protein degradation in eukaryotes. We have tested this model by directly comparing the HRD dependency of the ER-associated degradation for various ER membrane proteins. Our data indicated that the role of HRD genes in protein degradation, even in this highly defined subset of proteins, can vary from absolute dependence to complete independence. Thus, ER-associated degradation can occur by mechanisms that do not involve Hrd1p or Hrd3p, despite their apparently broad envelope of substrates. These data favor models in which the HRD gene-encoded proteins function as specificity factors, such as ubiquitin ligases, rather than as factors involved in common aspects of ER degradation.  (+info)

Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease. (7/109)

Uracil uptake by Saccharomyces cerevisiae is mediated by the FUR4-encoded uracil permease. The modification of uracil permease by phosphorylation at the plasma membrane is a key mechanism for regulating endocytosis of this protein. This modification in turn facilitates its ubiquitination and internalization. Following endocytosis, the permease is targeted to the lysosome/vacuole for proteolysis. We have previously shown that uracil permease is phosphorylated at several serine residues within a well characterized N-terminal PEST sequence. In this report, we provide evidence that lysine residues 38 and 41, adjacent to the PEST sequence, are the target sites for ubiquitination of the permease. Conservative substitutions at both Lys(38) and Lys(41) give variant permeases that are phosphorylated but fail to internalize. The PEST sequence contains potential phosphorylation sites conforming to the consensus sequences for casein kinase 1. Casein kinase 1 (CK1) protein kinases, encoded by the redundant YCKI and YCK2 genes, are located at the plasma membrane. Either alone supports growth, but loss of function of both is lethal. Here, we show that in CK1-deficient cells, the permease is poorly phosphorylated and poorly ubiquitinated. Moreover, CK1 overproduction rescued the defective endocytosis of a mutant permease in which the serine phosphoacceptors were replaced by threonine (a less effective phosphoacceptor), which suggests that Yck activity may play a direct role in phosphorylating the permease. Permease internalization was not greatly affected in CK1-deficient cells, despite the low level of ubiquitination of the protein. This may be due to CK1 having a second counteracting role in endocytosis as shown by the higher turnover of variant permeases with unphosphorylatable versions of the PEST sequence.  (+info)

WW domains of Rsp5p define different functions: determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae. (8/109)

Rsp5p, ubiquitin-protein ligase, an enzyme of the ubiquitination pathway, contains three WW domains that mediate protein-protein interactions. To determine if these domains adapt Rsp5p to a subset of substrates involved in numerous cellular processes, we generated mutations in individual or combinations of the WW domains. The rsp5-w1, rsp5-w2, and rsp5-w3 mutant alleles complement RSP5 deletions at 30 degrees. Thus, individual WW domains are not essential. Each rsp5-w mutation caused temperature-sensitive growth. Among variants with mutations in multiple WW domains, only rsp5-w1w2 complemented the deletion. Thus, the WW3 domain is sufficient for Rsp5p essential functions. To determine whether rsp5-w mutations affect endocytosis, fluid phase and uracil permease (Fur4p) endocytosis was examined. The WW3 domain is important for both processes. WW2 appears not to be important for fluid phase endocytosis whereas it is important for Fur4p endocytosis. In contrast, the WW1 domain affects fluid phase endocytosis, but it does not appear to function in Fur4p endocytosis. Thus, various WW domains play different roles in the endocytosis of these two substrates. Rsp5p is located in the cytoplasm in a punctate pattern that does not change during the cell cycle. Altering WW domains does not change the location of Rsp5p.  (+info)

Nucleotide transport proteins are specialized membrane-bound proteins that facilitate the passive or active transport of nucleotides, such as adenosine triphosphate (ATP), guanosine triphosphate (GTP), and their precursors, across biological membranes. These proteins play a crucial role in maintaining the intracellular concentration of nucleotides, which are essential for various cellular processes, including energy metabolism, biosynthesis, and signal transduction.

There are two main types of nucleotide transport proteins: equilibrative nucleoside transporters (ENTs) and concentrative nucleoside transporters (CNTs). ENTs facilitate the passive diffusion of nucleosides and some nucleotides down their concentration gradient, while CNTs actively transport these molecules against their concentration gradient using energy derived from sodium or proton gradients.

These proteins are vital for cellular homeostasis and have been implicated in several diseases, including cancer and neurological disorders. Understanding the structure, function, and regulation of nucleotide transport proteins can provide valuable insights into their role in health and disease, potentially leading to the development of novel therapeutic strategies.

Mitochondrial ADP/ATP translocases, also known as adenine nucleotide translocators (ANT), are a group of proteins located in the inner mitochondrial membrane that play a crucial role in cellular energy production. These translocases facilitate the exchange of adenosine diphosphate (ADP) and adenosine triphosphate (ATP) across the mitochondrial membrane, which is essential for oxidative phosphorylation and thus, energy homeostasis in the cell.

In more detail, during oxidative phosphorylation, ATP is produced within the mitochondria as a result of the electron transport chain's activity. This ATP must be exported to the cytosol for use by the cell's various processes. Simultaneously, the mitochondria need a continuous supply of ADP to sustain the production of ATP. The mitochondrial ADP/ATP translocases facilitate this exchange, allowing for the import of ADP into the mitochondria and the export of ATP to the cytosol.

There are multiple isoforms of the ADP/ATP translocase in humans (ANT1, ANT2, ANT3, and ANT4), encoded by different genes, with varying tissue distributions and functions. Dysfunction of these translocases has been implicated in several pathological conditions, including neurodegenerative diseases, ischemia-reperfusion injury, and cancer.

Atractyloside is a toxic diterpene compound that can be found in various plants, including Atractylis gummifera (commonly known as gum cistus or rabbit-ear cistus) and other members of the Asteraceae family. This toxin is known to inhibit the mitochondrial ADP/ATP translocase, which plays a crucial role in cellular energy production.

Inhibition of this translocase leads to a disruption in the balance of adenine nucleotides inside the mitochondria, resulting in a decrease in ATP synthesis and an increase in the formation of reactive oxygen species (ROS). This can ultimately cause cell damage and even cell death.

Atractyloside poisoning can lead to various symptoms, such as gastrointestinal distress, liver and kidney damage, neurological issues, and, in severe cases, multi-organ failure. It is essential to seek immediate medical attention if atractyloside poisoning is suspected.

Adenine nucleotides are molecules that consist of a nitrogenous base called adenine, which is linked to a sugar molecule (ribose in the case of adenosine monophosphate or AMP, and deoxyribose in the case of adenosine diphosphate or ADP and adenosine triphosphate or ATP) and one, two, or three phosphate groups. These molecules play a crucial role in energy transfer and metabolism within cells.

AMP contains one phosphate group, while ADP contains two phosphate groups, and ATP contains three phosphate groups. When a phosphate group is removed from ATP, energy is released, which can be used to power various cellular processes such as muscle contraction, nerve impulse transmission, and protein synthesis. The reverse reaction, in which a phosphate group is added back to ADP or AMP to form ATP, requires energy input and often involves the breakdown of nutrients such as glucose or fatty acids.

In addition to their role in energy metabolism, adenine nucleotides also serve as precursors for other important molecules, including DNA and RNA, coenzymes, and signaling molecules.

Bongkrekic acid is a toxic compound that is produced by certain strains of the bacterium Pseudomonas cocovenenans. This bacterium can contaminate foods, particularly coconut products such as tempeh, a traditional Indonesian soybean fermented food. Bongkrekic acid inhibits the function of the mitochondria, the energy-producing structures in cells, leading to cell death and potentially serious illness or death in humans. Consumption of food contaminated with bongkrekic acid can cause a severe form of food poisoning known as bongkrek fever, which is characterized by symptoms such as nausea, vomiting, diarrhea, abdominal pain, and neurological symptoms such as confusion, seizures, and coma. Bongkrek fever is often fatal if not treated promptly and effectively. It is important to handle and store food properly to prevent contamination with bongkrekic acid and other harmful bacteria.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

I'm happy to help! However, it seems like there are two terms combined into one request: "Mitochondria" and "Heart." I will provide separate definitions for each.

Mitochondrion (singular) or Mitochondria (plural): These are specialized structures found in the cytoplasm of most eukaryotic cells (cells with a true nucleus), including human cells. They are often referred to as the "powerhouse" of the cell because they generate energy in the form of ATP (adenosine triphosphate) through a process called oxidative phosphorylation. Mitochondria contain their own DNA, which is distinct from the nuclear DNA, and are believed to have originated from ancient bacteria that established a symbiotic relationship with primitive eukaryotic cells.

Heart: In human anatomy, the heart is a muscular organ responsible for pumping blood throughout the body. It is located in the thoracic cavity, slightly left of the center, and is enclosed by the pericardium, a double-walled sac that provides protection and lubrication for the heart's movement. The human heart is divided into four chambers: two atria on the top and two ventricles on the bottom. The right side of the heart receives deoxygenated blood from the body and pumps it to the lungs, while the left side receives oxygenated blood from the lungs and pumps it to the rest of the body. The heart's pumping action is regulated by electrical signals that originate in a group of specialized cardiac muscle cells called the sinoatrial node (SA node).

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

Fatty acid transport proteins (FATPs) are a group of membrane-bound proteins that play a crucial role in the uptake and transport of long-chain fatty acids across the plasma membrane of cells. They are widely expressed in various tissues, including the heart, muscle, adipose tissue, and liver.

FATPs have several domains that enable them to perform their functions, including a cytoplasmic domain that binds to fatty acids, a transmembrane domain that spans the plasma membrane, and an ATP-binding cassette (ABC) domain that hydrolyzes ATP to provide energy for fatty acid transport.

FATPs also play a role in the regulation of intracellular lipid metabolism by modulating the activity of enzymes involved in fatty acid activation, desaturation, and elongation. Mutations in FATP genes have been associated with various metabolic disorders, including congenital deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), a rare autosomal recessive disorder that affects fatty acid oxidation.

In summary, fatty acid transport proteins are essential for the uptake and metabolism of long-chain fatty acids in cells and have implications in various metabolic disorders.

Membrane transport proteins are specialized biological molecules, specifically integral membrane proteins, that facilitate the movement of various substances across the lipid bilayer of cell membranes. They are responsible for the selective and regulated transport of ions, sugars, amino acids, nucleotides, and other molecules into and out of cells, as well as within different cellular compartments. These proteins can be categorized into two main types: channels and carriers (or pumps). Channels provide a passive transport mechanism, allowing ions or small molecules to move down their electrochemical gradient, while carriers actively transport substances against their concentration gradient, requiring energy usually in the form of ATP. Membrane transport proteins play a crucial role in maintaining cell homeostasis, signaling processes, and many other physiological functions.

I'd be happy to help! However, I believe there might be a slight misunderstanding in your question. Mitochondria are organelles found in the cells of all complex living organisms, including humans, while the liver is a large, solid organ located in the upper right portion of the abdomen. They don't have a medical definition together. I can certainly provide you with separate definitions for each:

1. Mitochondria: These are double-membrane-bound cellular organelles that generate most of the chemical energy needed to power the cell's biochemical reactions. Commonly known as the "powerhouse of the cell," mitochondria convert organic substrates, such as glucose, fatty acids, and amino acids, into adenosine triphosphate (ATP) through a process called oxidative phosphorylation. Mitochondria are dynamic structures that can change their shape, size, and number through fission (division) and fusion (merging) processes. They play essential roles in various cellular functions, including calcium signaling, apoptosis (programmed cell death), and the regulation of cellular metabolism.

2. Liver: The liver is a large, lobulated organ that lies mainly in the upper right portion of the abdominal cavity, just below the diaphragm. It plays a crucial role in various physiological functions, such as detoxification, protein synthesis, metabolism, and nutrient storage. The liver is responsible for removing toxins from the bloodstream, producing bile to aid in digestion, regulating glucose levels, synthesizing plasma proteins, and storing glycogen, vitamins, and minerals. It also contributes to the metabolism of carbohydrates, lipids, and amino acids, helping maintain energy homeostasis in the body.

I hope this clarifies any confusion! If you have any further questions or need more information, please don't hesitate to ask.

Nucleotides are the basic structural units of nucleic acids, such as DNA and RNA. They consist of a nitrogenous base (adenine, guanine, cytosine, thymine or uracil), a pentose sugar (ribose in RNA and deoxyribose in DNA) and one to three phosphate groups. Nucleotides are linked together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of another, forming long chains known as polynucleotides. The sequence of these nucleotides determines the genetic information carried in DNA and RNA, which is essential for the functioning, reproduction and survival of all living organisms.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Biological transport, active is the process by which cells use energy to move materials across their membranes from an area of lower concentration to an area of higher concentration. This type of transport is facilitated by specialized proteins called transporters or pumps that are located in the cell membrane. These proteins undergo conformational changes to physically carry the molecules through the lipid bilayer of the membrane, often against their concentration gradient.

Active transport requires energy because it works against the natural tendency of molecules to move from an area of higher concentration to an area of lower concentration, a process known as diffusion. Cells obtain this energy in the form of ATP (adenosine triphosphate), which is produced through cellular respiration.

Examples of active transport include the uptake of glucose and amino acids into cells, as well as the secretion of hormones and neurotransmitters. The sodium-potassium pump, which helps maintain resting membrane potential in nerve and muscle cells, is a classic example of an active transporter.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Monosaccharide transport proteins are a type of membrane transport protein that facilitate the passive or active transport of monosaccharides, such as glucose, fructose, and galactose, across cell membranes. These proteins play a crucial role in the absorption, distribution, and metabolism of carbohydrates in the body.

There are two main types of monosaccharide transport proteins: facilitated diffusion transporters and active transporters. Facilitated diffusion transporters, also known as glucose transporters (GLUTs), passively transport monosaccharides down their concentration gradient without the need for energy. In contrast, active transporters, such as the sodium-glucose cotransporter (SGLT), use energy in the form of ATP to actively transport monosaccharides against their concentration gradient.

Monosaccharide transport proteins are found in various tissues throughout the body, including the intestines, kidneys, liver, and brain. They play a critical role in maintaining glucose homeostasis by regulating the uptake and release of glucose into and out of cells. Dysfunction of these transporters has been implicated in several diseases, such as diabetes, cancer, and neurological disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Cation transport proteins are a type of membrane protein that facilitate the movement of cations (positively charged ions) across biological membranes. These proteins play a crucial role in maintaining ion balance and electrical excitability within cells, as well as in various physiological processes such as nutrient uptake, waste elimination, and signal transduction.

There are several types of cation transport proteins, including:

1. Ion channels: These are specialized protein structures that form a pore or channel through the membrane, allowing ions to pass through rapidly and selectively. They can be either voltage-gated or ligand-gated, meaning they open in response to changes in electrical potential or binding of specific molecules, respectively.

2. Ion pumps: These are active transport proteins that use energy from ATP hydrolysis to move ions against their electrochemical gradient, effectively pumping them from one side of the membrane to the other. Examples include the sodium-potassium pump (Na+/K+-ATPase) and calcium pumps (Ca2+ ATPase).

3. Ion exchangers: These are antiporter proteins that facilitate the exchange of one ion for another across the membrane, maintaining electroneutrality. For example, the sodium-proton exchanger (NHE) moves a proton into the cell in exchange for a sodium ion being moved out.

4. Symporters: These are cotransporter proteins that move two or more ions together in the same direction, often coupled with the transport of a solute molecule. An example is the sodium-glucose cotransporter (SGLT), which facilitates glucose uptake into cells by coupling its movement with that of sodium ions.

Collectively, cation transport proteins help maintain ion homeostasis and contribute to various cellular functions, including electrical signaling, enzyme regulation, and metabolic processes. Dysfunction in these proteins can lead to a range of diseases, such as neurological disorders, cardiovascular disease, and kidney dysfunction.

Ion transport refers to the active or passive movement of ions, such as sodium (Na+), potassium (K+), chloride (Cl-), and calcium (Ca2+) ions, across cell membranes. This process is essential for various physiological functions, including nerve impulse transmission, muscle contraction, and maintenance of resting membrane potential.

Ion transport can occur through several mechanisms, including:

1. Diffusion: the passive movement of ions down their concentration gradient, from an area of high concentration to an area of low concentration.
2. Facilitated diffusion: the passive movement of ions through specialized channels or transporters in the cell membrane.
3. Active transport: the energy-dependent movement of ions against their concentration gradient, requiring the use of ATP. This process is often mediated by ion pumps, such as the sodium-potassium pump (Na+/K+-ATPase).
4. Co-transport or symport: the coupled transport of two or more different ions or molecules in the same direction, often driven by an electrochemical gradient.
5. Counter-transport or antiport: the coupled transport of two or more different ions or molecules in opposite directions, also often driven by an electrochemical gradient.

Abnormalities in ion transport can lead to various medical conditions, such as cystic fibrosis (which involves defective chloride channel function), hypertension (which may be related to altered sodium transport), and certain forms of heart disease (which can result from abnormal calcium handling).

Anion transport proteins are specialized membrane transport proteins that facilitate the movement of negatively charged ions, known as anions, across biological membranes. These proteins play a crucial role in maintaining ionic balance and regulating various physiological processes within the body.

There are several types of anion transport proteins, including:

1. Cl-/HCO3- exchangers (also known as anion exchangers or band 3 proteins): These transporters facilitate the exchange of chloride (Cl-) and bicarbonate (HCO3-) ions across the membrane. They are widely expressed in various tissues, including the red blood cells, gastrointestinal tract, and kidneys, where they help regulate pH, fluid balance, and electrolyte homeostasis.
2. Sulfate permeases: These transporters facilitate the movement of sulfate ions (SO42-) across membranes. They are primarily found in the epithelial cells of the kidneys, intestines, and choroid plexus, where they play a role in sulfur metabolism and absorption.
3. Cl- channels: These proteins form ion channels that allow chloride ions to pass through the membrane. They are involved in various physiological processes, such as neuronal excitability, transepithelial fluid transport, and cell volume regulation.
4. Cation-chloride cotransporters: These transporters move both cations (positively charged ions) and chloride anions together across the membrane. They are involved in regulating neuronal excitability, cell volume, and ionic balance in various tissues.

Dysfunction of anion transport proteins has been implicated in several diseases, such as cystic fibrosis (due to mutations in the CFTR Cl- channel), distal renal tubular acidosis (due to defects in Cl-/HCO3- exchangers), and some forms of epilepsy (due to abnormalities in cation-chloride cotransporters).

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Axonal transport is the controlled movement of materials and organelles within axons, which are the nerve fibers of neurons (nerve cells). This intracellular transport system is essential for maintaining the structural and functional integrity of axons, particularly in neurons with long axonal processes. There are two types of axonal transport: anterograde transport, which moves materials from the cell body toward the synaptic terminals, and retrograde transport, which transports materials from the synaptic terminals back to the cell body. Anterograde transport is typically slower than retrograde transport and can be divided into fast and slow components based on velocity. Fast anterograde transport moves vesicles containing neurotransmitters and their receptors, as well as mitochondria and other organelles, at speeds of up to 400 mm/day. Slow anterograde transport moves cytoskeletal elements, proteins, and RNA at speeds of 1-10 mm/day. Retrograde transport is primarily responsible for recycling membrane components, removing damaged organelles, and transmitting signals from the axon terminal to the cell body. Dysfunctions in axonal transport have been implicated in various neurodegenerative disorders, such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS).

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Single Nucleotide Polymorphism (SNP) is a type of genetic variation that occurs when a single nucleotide (A, T, C, or G) in the DNA sequence is altered. This alteration must occur in at least 1% of the population to be considered a SNP. These variations can help explain why some people are more susceptible to certain diseases than others and can also influence how an individual responds to certain medications. SNPs can serve as biological markers, helping scientists locate genes that are associated with disease. They can also provide information about an individual's ancestry and ethnic background.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

A symporter is a type of transmembrane protein that functions to transport two or more molecules or ions across a biological membrane in the same direction, simultaneously. This process is called co-transport and it is driven by the concentration gradient of one of the substrates, which is usually an ion such as sodium (Na+) or proton (H+).

Symporters are classified based on the type of energy that drives the transport process. Primary active transporters, such as symporters, use the energy from ATP hydrolysis or from the electrochemical gradient of ions to move substrates against their concentration gradient. In contrast, secondary active transporters use the energy stored in an existing electrochemical gradient of one substrate to drive the transport of another substrate against its own concentration gradient.

Symporters play important roles in various physiological processes, including nutrient uptake, neurotransmitter reuptake, and ion homeostasis. For example, the sodium-glucose transporter (SGLT) is a symporter that co-transports glucose and sodium ions across the intestinal epithelium and the renal proximal tubule, contributing to glucose absorption and regulation of blood glucose levels. Similarly, the dopamine transporter (DAT) is a symporter that co-transports dopamine and sodium ions back into presynaptic neurons, terminating the action of dopamine in the synapse.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Guanine nucleotides are molecules that play a crucial role in intracellular signaling, cellular regulation, and various biological processes within cells. They consist of a guanine base, a sugar (ribose or deoxyribose), and one or more phosphate groups. The most common guanine nucleotides are GDP (guanosine diphosphate) and GTP (guanosine triphosphate).

GTP is hydrolyzed to GDP and inorganic phosphate by certain enzymes called GTPases, releasing energy that drives various cellular functions such as protein synthesis, signal transduction, vesicle transport, and cell division. On the other hand, GDP can be rephosphorylated back to GTP by nucleotide diphosphate kinases, allowing for the recycling of these molecules within the cell.

In addition to their role in signaling and regulation, guanine nucleotides also serve as building blocks for RNA (ribonucleic acid) synthesis during transcription, where they pair with cytosine nucleotides via hydrogen bonds to form base pairs in the resulting RNA molecule.

Vesicular transport proteins are specialized proteins that play a crucial role in the intracellular trafficking and transportation of various biomolecules, such as proteins and lipids, within eukaryotic cells. These proteins facilitate the formation, movement, and fusion of membrane-bound vesicles, which are small, spherical structures that carry cargo between different cellular compartments or organelles.

There are several types of vesicular transport proteins involved in this process:

1. Coat Proteins (COPs): These proteins form a coat around the vesicle membrane and help shape it into its spherical form during the budding process. They also participate in selecting and sorting cargo for transportation. Two main types of COPs exist: COPI, which is involved in transport between the Golgi apparatus and the endoplasmic reticulum (ER), and COPII, which mediates transport from the ER to the Golgi apparatus.

2. SNARE Proteins: These proteins are responsible for the specific recognition and docking of vesicles with their target membranes. They form complexes that bring the vesicle and target membranes close together, allowing for fusion and the release of cargo into the target organelle. There are two types of SNARE proteins: v-SNAREs (vesicle SNAREs) and t-SNAREs (target SNAREs), which interact to form a stable complex during membrane fusion.

3. Rab GTPases: These proteins act as molecular switches that regulate the recruitment of coat proteins, motor proteins, and SNAREs during vesicle transport. They cycle between an active GTP-bound state and an inactive GDP-bound state, controlling the various stages of vesicular trafficking, such as budding, transport, tethering, and fusion.

4. Tethering Proteins: These proteins help to bridge the gap between vesicles and their target membranes before SNARE-mediated fusion occurs. They play a role in ensuring specificity during vesicle docking and may also contribute to regulating the timing of membrane fusion events.

5. Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptors (SNAREs): These proteins are involved in intracellular transport, particularly in the trafficking of vesicles between organelles. They consist of a family of coiled-coil domain-containing proteins that form complexes to mediate membrane fusion events.

Overall, these various classes of proteins work together to ensure the specificity and efficiency of vesicular transport in eukaryotic cells. Dysregulation or mutation of these proteins can lead to various diseases, including neurodegenerative disorders and cancer.

Purine nucleotides are fundamental units of life that play crucial roles in various biological processes. A purine nucleotide is a type of nucleotide, which is the basic building block of nucleic acids such as DNA and RNA. Nucleotides consist of a nitrogenous base, a pentose sugar, and at least one phosphate group.

In purine nucleotides, the nitrogenous bases are either adenine (A) or guanine (G). These bases are attached to a five-carbon sugar called ribose in the case of RNA or deoxyribose for DNA. The sugar and base together form the nucleoside, while the addition of one or more phosphate groups creates the nucleotide.

Purine nucleotides have several vital functions within cells:

1. Energy currency: Adenosine triphosphate (ATP) is a purine nucleotide that serves as the primary energy currency in cells, storing and transferring chemical energy for various cellular processes.
2. Genetic material: Both DNA and RNA contain purine nucleotides as essential components of their structures. Adenine pairs with thymine (in DNA) or uracil (in RNA), while guanine pairs with cytosine.
3. Signaling molecules: Purine nucleotides, such as adenosine monophosphate (AMP) and cyclic adenosine monophosphate (cAMP), act as intracellular signaling molecules that regulate various cellular functions, including metabolism, gene expression, and cell growth.
4. Coenzymes: Purine nucleotides can also function as coenzymes, assisting enzymes in catalyzing biochemical reactions. For example, nicotinamide adenine dinucleotide (NAD+) is a purine nucleotide that plays a critical role in redox reactions and energy metabolism.

In summary, purine nucleotides are essential biological molecules involved in various cellular functions, including energy transfer, genetic material formation, intracellular signaling, and enzyme cofactor activity.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

ATP-binding cassette (ABC) transporters are a family of membrane proteins that utilize the energy from ATP hydrolysis to transport various substrates across extra- and intracellular membranes. These transporters play crucial roles in several biological processes, including detoxification, drug resistance, nutrient uptake, and regulation of cellular cholesterol homeostasis.

The structure of ABC transporters consists of two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP, and two transmembrane domains (TMDs) that form the substrate-translocation pathway. The NBDs are typically located adjacent to each other in the cytoplasm, while the TMDs can be either integral membrane domains or separate structures associated with the membrane.

The human genome encodes 48 distinct ABC transporters, which are classified into seven subfamilies (ABCA-ABCG) based on their sequence similarity and domain organization. Some well-known examples of ABC transporters include P-glycoprotein (ABCB1), multidrug resistance protein 1 (ABCC1), and breast cancer resistance protein (ABCG2).

Dysregulation or mutations in ABC transporters have been implicated in various diseases, such as cystic fibrosis, neurological disorders, and cancer. In cancer, overexpression of certain ABC transporters can contribute to drug resistance by actively effluxing chemotherapeutic agents from cancer cells, making them less susceptible to treatment.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Sodium is an essential mineral and electrolyte that is necessary for human health. In a medical context, sodium is often discussed in terms of its concentration in the blood, as measured by serum sodium levels. The normal range for serum sodium is typically between 135 and 145 milliequivalents per liter (mEq/L).

Sodium plays a number of important roles in the body, including:

* Regulating fluid balance: Sodium helps to regulate the amount of water in and around your cells, which is important for maintaining normal blood pressure and preventing dehydration.
* Facilitating nerve impulse transmission: Sodium is involved in the generation and transmission of electrical signals in the nervous system, which is necessary for proper muscle function and coordination.
* Assisting with muscle contraction: Sodium helps to regulate muscle contractions by interacting with other minerals such as calcium and potassium.

Low sodium levels (hyponatremia) can cause symptoms such as confusion, seizures, and coma, while high sodium levels (hypernatremia) can lead to symptoms such as weakness, muscle cramps, and seizures. Both conditions require medical treatment to correct.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

Anion Exchange Protein 1, Erythrocyte (AE1), also known as Band 3 protein or SLC4A1, is a transmembrane protein found in the membranes of red blood cells (erythrocytes). It plays a crucial role in maintaining the pH and bicarbonate levels of the blood by facilitating the exchange of chloride ions (Cl-) with bicarbonate ions (HCO3-) between the red blood cells and the plasma.

The anion exchange protein 1 is composed of three major domains: a cytoplasmic domain, a transmembrane domain, and an extracellular domain. The cytoplasmic domain interacts with various proteins involved in regulating the cytoskeleton of the red blood cell, while the transmembrane domain contains the ion exchange site. The extracellular domain is responsible for the interaction between red blood cells and contributes to their aggregation.

Mutations in the AE1 gene can lead to various inherited disorders, such as hereditary spherocytosis, Southeast Asian ovalocytosis, and distal renal tubular acidosis type 1. These conditions are characterized by abnormal red blood cell shapes, impaired kidney function, or both.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Phosphate-binding proteins are a type of protein that play a crucial role in regulating the concentration of phosphates in cells. They function by binding to phosphate ions and facilitating their transport, storage, or excretion. These proteins can be found in various organisms, including bacteria, plants, and animals.

In humans, one example of a phosphate-binding protein is the plasma protein known as fetuin-A. Fetuin-A helps regulate the amount of phosphate in the blood by binding to it and preventing it from forming insoluble precipitates with calcium, which can lead to the formation of kidney stones or calcifications in soft tissues.

Another example is the intracellular protein called alkaline phosphatase, which plays a role in removing phosphate groups from molecules within the cell. This enzyme helps regulate the levels of phosphates and other ions within the cell, as well as contributing to various metabolic processes.

Overall, phosphate-binding proteins are essential for maintaining proper phosphate homeostasis in the body, which is critical for numerous physiological functions, including energy metabolism, bone health, and signal transduction.

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Gehrig H, Müller W, Appelhans H (April 1992). "Complete nucleotide sequence of band 3 related anion transport protein AE2 from ... Anion exchange protein 2 (AE2) is a membrane transport protein that in humans is encoded by the SLC4A2 gene. AE2 is ... Finally, the AE2 protein returns to its inward-facing conformation and releases Cl- into the cytosol. This working cycle of the ... The cryo electron microsopic studies revealed that human AE2 protein forms a homodimer and stays in resting state of inward- ...
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These transporter proteins transport a nucleotide sugar, UDP-N-acetylglucosamine or UDP-GlcNAc and ... Two synonymous single nucleotide polymorphism(SNP) of TGFBI gene occurred in the family, including a C to T transition at codon ... The mode of inheritance of CVM is autosomal recessive and it is caused by a point mutation from G to T at nucleotide position ... It is caused by a point mutation (G→T) at nucleotide position 559 of the gene, bovine solute carrier family 35 member 3 ( ...
PhnN proteins as members of nucleotide-binding proteins of the binding protein-dependent transport systems. Candidates for ... Click on the protein counts, or double click on taxonomic names to display all proteins containing PhnA_Zn_Ribbon domain in the ... The PhnA protein family includes the uncharacterised Escherichia coli protein PhnA and its homologues. The E. coli phnA gene is ... The nucleotide and deduced amino acid sequences of the phnA gene showed no significant homology with any data bank accessions. ...
... tumor cells while aspartate contributes to the synthesis of proteins and nucleotides as well as feeding the electron transport ... The BCL-2 family of proteins, consisting of antiapoptotic, proapoptotic, and BH3-only proteins, plays a central role in ... Apoptosis is also controlled by the Inhibitors of Apoptosis Proteins (IAPs), including survivin, and the FLIP proteins that ... C. H. Yi, H. Pan, J. Seebacher et al., "Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival," ...
Different PTMs show distinct impacts on protein functions, and normal protein activities are consequences of all kinds of PTMs ... more and more nonsynonymous single-nucleotide variations (nsSNVs) that cause variation of amino acids have been identified, ... play key roles in a variety of protein activities and cellular processes. ... With regard to glycosylation, the diseases were closely related to lipid metabolism and molecular transport. ...
Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily. ... Yrb2p, a Nup2p-related yeast protein, has a functional overlap with Rna1p, a yeast Ran-GTPase-activating protein. Noguchi, E., ... The yeast SRM1 protein and human RCC1 protein share analogous functions. Clark, K.L., Ohtsubo, M., Nishimoto, T., Goebl, M., ... RCC1/PRP20 act as guanine nucleotide exchange factors for the nuclear Ras-like Ran/GSP1 proteins [5]. ...
Ferrous iron transport protein B. A, B, C. 274. Escherichia coli. Mutation(s): 0 Gene Names: b3409, feoB, JW3372. ... Structural basis for the intrinsic GTPase and GDI activities of FeoB, a prokaryotic transmembrane GTP/GDP-binding protein. ... Structure of the cytosolic domain of E. coli FeoB, nucleotide-free form. *PDB DOI: https://doi.org/10.2210/pdb3I8S/pdb ...
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Activities of mutant Sar1 proteins in guanine nucleotide binding, GTP hydrolysis, and cell-free transport from the endoplasmic ... Activities of mutant Sar1 proteins in guanine nucleotide binding, GTP hydrolysis, and cell-free transport from the endoplasmic ... Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J. Biol. ... Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J. Biol. ...
... approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components in intracellular vesicular transport ... Both guanine nucleotide-exchange proteins and GTPase-activating proteins (GAPs) for ARFs have been cloned recently. A zinc ... Proteins containing this domain include ARF1-directed GTPase-activating protein, the cycle control GTPase activating protein ( ... This protein, with a molecular mass of 43 kDa, was termed PtdIns(3,4,5)P3-binding protein. The partial amino acid sequences ...
Transport of Cyclic Nucleotides and Estradiol 17-Beta-d-glucuronide by Multidrug Resistance Protein 4. Resistance to 6- ... Keppler, D., Jedlitschky, G. and Leier, I. (1998) Transport Function and Substrate Specificity of Multidrug Resistance Protein ... The Multidrug Resistance Protein 5 Functions as an ATP-Dependent Export Pump for Cyclic Nucleotides. The Journal of Biological ... Characterization of the MRP4-and MRP5-Mediated Transport of Cyclic Nucleotides from Intact Cells. The Journal of Biological ...
... nucleotide excision repair, P = 0.028; transport, P = 0.049). (E) log2-normalized qPCR expression of dnmts and tet1/2/3 at ... We used two morpholinos to knockdown dnmt3a and dnmt3b protein synthesis in monkey embryos (www.gene-tools.com). The sequences ... D) GO analysis of DMRs between the 2-cell and 8-cell stages indicating that oxidative phosphorylation and nucleotide excision ... Oocytes that were mature (MII) at collection were placed in chemically defined, protein-free hamster embryo culture medium-10 ( ...
TGB3 transport to cell peripheral bodies was previously shown to bypass the secretory pathway and involve a non-conventional ... The BMB2 protein associates with endoplasmic reticulum (ER) membranes, accumulates at plasmodesmata-associated membrane bodies ... Here, we provide evidence that the intracellular transport of both poa semilatent virus TGB3 and hibiscus green spot virus BMB2 ... TGB3 is a small integral membrane protein that contains subcellular targeting signals and directs both TGB2 and the helicase ...
The journal will also report progress in the fields of transport routes and mechanisms including efflux proteins and multi-drug ... The drugs include a wide range of bioactive compounds from simple pharmaceuticals to peptides, proteins, nucleotides, ...
... the production of proteins, and the urea cycle. Molecules transported by citrin are also involved in making nucleotides. , ... This gene provides instructions for making a protein called citrin. Within cells, citrin helps transport molecules used in the ... which inhibits the urea cycle and disrupts the production of proteins and nucleotides. The resulting buildup of ammonia and ... The proteins produced from these genes play roles in the urea cycle. The urea cycle is a sequence of chemical reactions that ...
Golgi resident proteins, such as glycosyltransferases and sugar nucleotide transporters, are precisely distributed across the ... define the novel functions of a disease-associated membrane transporter in solute transport and protein recycling in the Golgi ... Golgi resident proteins, such as glycosyltransferases and sugar nucleotide transporters, are precisely distributed across the ... Molecular Mechanisms of Membrane Protein Homeostasis at the Golgi. Principal Investigator: Richa Sardana. Department of ...
The D2H cDNA is 2284 nucleotides long and encodes a 663 amino acid protein that is 80% identical to the rat D2 amino acid ... that stimulates cystine as well as dibasic and neutral amino acid transport. In order to evaluate the role of this protein in ... Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport.. ... Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport.. ...
Transport, Developmental protein, Defence, Enzyme, Enzyme inhibitor, Transcription, Immunity, Cell adhesion, Other and each ... Protein classi Protein class(es) of the gene product according to selected gene lists. List of protein classes. ... Protein classi Protein class(es) of the gene product according to selected gene lists. List of protein classes. ... Cell Cycle Dependent Proteini Cell cycle dependency of protein expression in the FUCCI U-2 OS cell line, determined by ICC-IF ...
Its epitope has been localized to the first nucleotide binding domain of MRP1 between amino acids 617 and 932.3 QCRL-3 does not ... It is reported that mAb QCRL-3 inhibits the ATP-dependent transport activity of MRP1 in inside-out membrane vesicles.,/span> ... member of the ATP-binding cassette transporter proteins, overexpressed in some drug-selected resistant cell lines and has been ... Its epitope has been localized to the first nucleotide binding domain of MRP1 between amino acids 617 and 932.3 QCRL-3 does not ...
A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the ... Guanine nucleotide exchange factor 2 for Rab5 proteins coordinated with GLUP6/GEF regulates the intracellular transport of the ... Multifunctional rna binding protein ostudor-sn in storage protein mrna transport and localization. Chou, H. L., Tian, L., ... Zipcode RNA-binding proteins and membrane trafficking proteins cooperate to transport glutelin mRNAs in rice endosperm[OPEN]. ...
Plasma Membrane-Located Purine Nucleotide Transport Proteins are Key Components for Host Exploitation by Microsporidian ... Inclusion Membrane Proteins of Protochlamydia amoebophila UWE25 Reveal a Conserved Mechanism for Host Cell Interaction among ... Back to basics: A revealing secondary reduction of the mitochondrial protein import pathway in diverse intracellular parasites ...
1990). Nucleotide sequence of the aroP gene encoding the general aromatic amino acid transport protein of Escherichia coli K-12 ... 1999). Identification of a membrane protein, LAT-2, that co-expresses with 4F2 heavy chain, and l-type amino acid transport ... 2000). The study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport. J. Bacteriol ... The APC superfamily of transport proteins includes members that function as solute:cation symporters and solute:solute ...
the oligomeric complex transport protein particle i (trappi) mediates nucleotide exchange on the rab gtpase rab1/ypt1. trappii ... proteins of the resistance to inhibitors of cholinesterase 8 (ric8) group act as guanine nucleotide exchange factors (gefs) and ... during membrane trafficking, endosomes transport lipids, proteins, and even rnas. in highly polarized cells such as fungal ... proteins rpf2 and rrs1 are required for 60s ribosomal subunit maturation. these proteins are necessary for the recruitment of ...
... and a family of GTP-hydrolysis activating proteins (GAPs) containing the conserved TBC domain. Recent structural and cell ... Rabs are GTP-binding proteins with conserved functions in membrane trafficking. They are regulated by a diverse group of ... Animals, Endocytosis, GTPase-Activating Proteins, Guanine Nucleotide Exchange Factors, Humans, Protein Transport, Secretory ... Rabs are GTP-binding proteins with conserved functions in membrane trafficking. They are regulated by a diverse group of ...
"Phylogenetic relationship of non-mitochondrial nucleotide transport proteins in bacteria and eukaryotes." Gene 306:27-35 ... EMBO Conference on Protein Transport Systems: Protein Targeting and Translocation. Gdansk, Poland, Sep 30-Oct 5, 2006. Poster # ... "Function prediction of hypothetical proteins without sequence similarity to proteins of known function." Pept Lett 15(10):1107- ... Nucleotide sequence of the coding gene and partial amino acid sequence of the protein." EMBO J 1:1385-139. Abstract Del Giudice ...
The structure also suggests that the four cyclic nucleotide-binding domains present in each channel form two distinct domains, ... This three-dimensional reconstruction provides insight into the architecture of the protein, suggesting that the cyclic ... nucleotide-binding domains, which initiate the response to ligand, hang below the pore-forming part of the channel, attached ... Cyclic nucleotide-gated (CNG) channels play a central role in the conversion of sensory information, such as light and scent, ...
... single nucleotide polymorphism; tau proteins; vesicular transport adaptor proteins ... Ten single nucleotide polymorphisms (SNPs), covering the whole SORT1 gene, were selected and genotyped in 620 AD patients and ... Alzheimers disease (AD) is a neurodegenerative disorder represented by the accumulation of intracellular tau protein and ...
... nucleotide) and disorder transport in the receptor( complex). In failure formation, minus-strand of VEGF pathways has membrane ... spectrum annotations live placed synthesised by proteins to date introduced in inner challenge cleavage proteins, p66 as ... PCP called much wiped in Drosophila, where it is the secretion of transport vectors and bodies in the gene( comprised in Maung ... In download to function these receptors, sPLA2 disorders of including proteins that do percentage substrates give increased ...
  • With the development of high throughput technologies such as tandem mass spectrometry (MS/MS) and next generation sequencing, more and more nonsynonymous single-nucleotide variations (nsSNVs) that cause variation of amino acids have been identified, some of which result in the damage of PTMs. (hindawi.com)
  • Either at genomic or at proteomic level, mutations have significant impact on normal gene or protein function, and human diseases could be associated with mutations like nonsynonymous single-nucleotide variations (nsSNVs) on amino acids. (hindawi.com)
  • Ten single nucleotide polymorphisms (SNPs), covering the whole SORT1 gene , were selected and genotyped in 620 AD patients and 1107 controls. (biofinder.se)
  • To investigate the possibility of a founder effect in these four families, we conducted haplotype analysis, and 14 single nucleotide polymorphisms (SNPs) throughout the SLC26A4 gene were genotyped. (nih.gov)
  • Here, we investigate whether single-nucleotide polymorphisms in nerve growth factor (NGF) (rs6330) and brain-derived neutrotrophic factor (BDNF) (rs6265) genes predict the response to cognitive behaviour therapy (CBT). (ox.ac.uk)
  • Sixteen obesity-predisposing single nucleotide polymorphisms (SNPs) were tested for association with short-term (baseline to 6 months) and long-term (baseline to 2 years) weight loss and weight regain (6 months to study end). (nih.gov)
  • Individual transport steps are regulated by Ras-like guanine nucleotide-binding proteins, termed Ypt in yeast or Rab in mammals. (embl.de)
  • Amino acid sequences typical for guanine nucleotide-binding proteins and characteristic for ypt proteins are perfectly conserved in the mouse ypt1 protein. (embl.de)
  • ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components in intracellular vesicular transport and phospholipase D activation. (embl.de)
  • Vesicular transport: how many Ypt/Rab-GTPases make a eukaryotic cell? (embl.de)
  • In eukaryotic cells, protein transport through the secretory and endocytic pathways is mediated by vesicular intermediates. (embl.de)
  • Golgi resident proteins, such as glycosyltransferases and sugar nucleotide transporters, are precisely distributed across the Golgi stacks by recycling mechanisms that counteract the flow of ongoing vesicular transport. (cornell.edu)
  • One of the main interests in the department is a system that has been evaluated at the molecular level with the range of molecular biological, biochemical, biophysical and chemical techniques available concerns the role of the Rab family of small guanosine nucleotide binding proteins in the regulation of intracellular vesicular transport. (mpg.de)
  • Specific distribution of PI lipids is regulated, either by the localization of a kinase-phosphatase pair or, by vesicular and non-vesicular lipid transport. (upstate.edu)
  • The drugs include a wide range of bioactive compounds from simple pharmaceuticals to peptides, proteins, nucleotides, nucleosides and sugars. (ingentaconnect.com)
  • They proposed that Lys158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters. (tcdb.org)
  • ABC (ATP binding cassette) transporters catalyze the transport of a wide variety of molecules across lipid bilayers into or out of cells and organelles. (rug.nl)
  • One of the ABC transporters that is studied in detail is the osmoregulatory ABC transporter OpuA (class D). Osmotic control of OpuA involves gating by intracellular ionic strength and is mediated by lipid-protein interactions. (rug.nl)
  • A structural genomics approach is used to determine to the structures of proteins belonging to other classes of ABC transporters. (rug.nl)
  • BioMNY proteins are considered to constitute tripartite biotin transporters in prokaryotes. (tcdb.org)
  • Some transporters have a conserved transmembrane protein and two nucleotide binding proteins similar to those of ABC transporters. (tcdb.org)
  • However, unlike typical ABC transporters (E.I. Sun & M.H. Saier, unpublished results), they use small integral membrane proteins that are postulated to capture specific substrates. (tcdb.org)
  • Anion exchange protein 2 (AE2) is a membrane transport protein that in humans is encoded by the SLC4A2 gene. (wikipedia.org)
  • It is caused by a point mutation (G→T) at nucleotide position 559 of the gene, bovine solute carrier family 35 member 3 (SLC35A3). (researchgate.net)
  • The nucleotide and deduced amino acid sequences of the phnA gene showed no significant homology with any data bank accessions. (embl-heidelberg.de)
  • The complete nucleotide sequence of 15,611 bases has been determined, and the gene structures were examined. (embl-heidelberg.de)
  • methylation at certain residues of histones can regulate gene expression [ 4 ], and glycosylation is responsible for targeting substrates and changing protein half-life [ 2 ]. (hindawi.com)
  • Yet how gene mutations affect protein activities through posttranslational modification sites have not been widely studied. (hindawi.com)
  • The ras-related ypt protein is an ubiquitous eukaryotic protein: isolation and sequence analysis of mouse cDNA clones highly homologous to the yeast YPT1 gene. (embl.de)
  • The YPT1 gene of the yeast Saccharomyces cerevisiae codes for a guanine nucleotide-binding protein which is essential for cell viability. (embl.de)
  • The cDNAs were derived from a gene, designated ypt1, which codes for a protein of 205 amino acids with 71% homology to the yeast YPT1 gene product. (embl.de)
  • Two mRNAs of 1600 and 3200 nucleotides, originating from the mouse ypt1 gene and differing in the length of their 3'-non-translated region, were identified in mouse F9 cells and in all mouse tissues examined. (embl.de)
  • A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product. (embl.de)
  • The cell-to-cell transport of many plant viruses through plasmodesmata requires viral movement proteins (MPs) encoded by a 'triple gene block' (TGB) and termed TGB1, TGB2 and TGB3. (microbiologyresearch.org)
  • This gene provides instructions for making a protein called citrin. (medlineplus.gov)
  • Its epitope has been localized to the first nucleotide binding domain of MRP1 between amino acids 617 and 932.3 QCRL-3 does not cross-react with human MDR1 or MDR3 gene products, nor with murine MRP1. (bdbiosciences.com)
  • PCP called much wiped in Drosophila, where it is the secretion of transport vectors and bodies in the gene( comprised in Maung and Jenny, 2011). (erik-mill.de)
  • In humans, the CRYAA gene encodes a 173 amino acid residue protein by single copy genes located on chromosome 21. (molvis.org)
  • The encoded protein of this gene may assist in the V-ATPase-mediated acidification of neuroendocrine secretory granules. (nih.gov)
  • The protein encoded by this gene is a small GTPase that acts as a homodimer. (bio-rad.com)
  • Nearly all these proteins are subunits of known or predicted multiprotein complexes, in agreement with the balance hypothesis of evolution of gene copy number. (biomedcentral.com)
  • The gene set of the last common ancestor of the crown group consists of 3,413 KOGs and largely includes proteins involved in genome replication and expression, and central metabolism. (biomedcentral.com)
  • Expression of truncated bio transport operons, each with one gene deleted, resulted in stable BioMN complexes but revealed only low amounts of BioMY and BioNY aggregates in the absence of the respective third partner. (tcdb.org)
  • We present the crystal structure of Salmonella enterica serovar typhimurium ArnA in complex with UDP-GlcA showing that binding of the sugar nucleotide is sufficient to trigger a conformational change conserved in bacterial ArnA_DHs but absent in its human homologs, as confirmed by structure and sequence analysis. (bvsalud.org)
  • In addition to its role in glucose metabolism, this pathway also regulates the redirection of free amino acids to protein synthesis via the mTOR-signaling pathway. (hindawi.com)
  • It is important in oxidative phosphorylation, glycolysis, cell replication, nucleotide metabolism and protein biosynthesis. (newcastlelaboratories.com)
  • Lipids, amino acids, and nucleotides necessary for the biosynthesis of the daughter cells are mostly provided by intermediate metabolites of these pathways. (hindawi.com)
  • Many bioY genes are located at loci encoding biotin biosynthesis or are unlinked to either biotin synthesis or other biotin transport genes. (tcdb.org)
  • The proteins produced from these genes play roles in the urea cycle. (medlineplus.gov)
  • Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport. (jci.org)
  • We have recently cloned, sequenced, and characterized a rat kidney cDNA (D2) that stimulates cystine as well as dibasic and neutral amino acid transport. (jci.org)
  • The D2H cDNA is 2284 nucleotides long and encodes a 663 amino acid protein that is 80% identical to the rat D2 amino acid sequence and 86% to that of the rabbit homologue rBAT. (jci.org)
  • We also study the NPC1 protein that is essential for cholesterol transport in humans and can lead to Niemann Pick C disease when mutated. (stanford.edu)
  • Fucoidan treatment of HCT-116 colon cancer cells resulted in downregulation of the ER protein 29 (ERp29), and triggered the phosphorylation of eukaryotic initiation element 2 alpha (p-eIF2a)/CCAAT/enhancer binding protein homologous protein (CHOP) pro-apoptotic cascade [14]. (irjs.info)
  • The Rab family of small GTP-binding proteins has long been implicated in the docking and fusion of transport vesicles with their target membranes. (embl.de)
  • The GTP-bound form of ARF is essential for the maintenance of normal Golgi morphology, it participates in recruitment of coat proteins which are required for budding and fission of membranes. (embl.de)
  • The BMB2 protein associates with endoplasmic reticulum (ER) membranes, accumulates at plasmodesmata-associated membrane bodies and directs the BMB1 helicase to these structures. (microbiologyresearch.org)
  • Here, we provide evidence that the intracellular transport of both poa semilatent virus TGB3 and hibiscus green spot virus BMB2 to plasmodesmata-associated sites can occur via lateral translocation along the ER membranes. (microbiologyresearch.org)
  • These will, for example, address questions concerning timing and location of significant steps, including prenylation, delivery of Rabs to specific membranes, interaction of Rabs with effectors, including those which provide links to actin or microtubule based motor systems and those involved in initial recognition between transport vesicles or related structures and target membranes. (mpg.de)
  • Biochemical assays revealed that the BioM, N, and Y proteins form stable complexes in membranes of the heterologous host. (tcdb.org)
  • Affected individuals often have specific food preferences, preferring protein-rich and fatty foods and avoiding carbohydrate-rich foods. (medlineplus.gov)
  • Severe phenotype of ATP6AP1-CDG in two siblings with a novel mutation leading to a differential tissue-specific ATP6AP1 protein pattern, cellular oxidative stress and hepatic copper accumulation. (nih.gov)
  • The interaction with the non-selective PDE (cyclic nucleotide phosphodiesterase) inhibitor 3-isobutyl-1-methylxanthine (IBMX) was tested after three days. (scirp.org)
  • Chen, Z.S., Lee, K. and Kruh, G.D. (2001) Transport of Cyclic Nucleotides and Estradiol 17-Beta-d-glucuronide by Multidrug Resistance Protein 4. (scirp.org)
  • Cyclic nucleotide-gated (CNG) channels play a central role in the conversion of sensory information, such as light and scent, into primary electrical signals. (ox.ac.uk)
  • This three-dimensional reconstruction provides insight into the architecture of the protein, suggesting that the cyclic nucleotide-binding domains, which initiate the response to ligand, 'hang' below the pore-forming part of the channel, attached by narrow linkers. (ox.ac.uk)
  • The structure also suggests that the four cyclic nucleotide-binding domains present in each channel form two distinct domains, lending structural weight to the suggestion that the four subunits of the CNG channels are arranged as a pair of dimers. (ox.ac.uk)
  • How does crowding affect mobility of proteins and lipids? (rug.nl)
  • Although the GTPase switch of Rab proteins is highly conserved, functional mechanisms may be highly diversified among members of the Rab family. (embl.de)
  • Oxr1p belongs to the group of TLDc domain containing proteins that are highly conserved in higher eukaryotes. (upstate.edu)
  • the filamentous fungus aspergillus oryzae is a well-known expression host used to express homologous and heterologous proteins in a number of industrial applications. (liverpool.ac.uk)
  • When evidence suggests that homologous membrane transport proteins of the ABC2 type couple transport to ATP hydrolysis using a homologue of the ABC-type ATPases, we list these proteins in the ABC superfamily. (tcdb.org)
  • The smaller proteins are generally of prokaryotic origin while the larger ones are of eukaryotic origin. (tcdb.org)
  • The larger eukaryotic and archaeal proteins possess N- and C-terminal hydrophilic extensions. (tcdb.org)
  • There is some redundancy among the 11 Ypt proteins, and only those involved in the biosynthetic pathway are essential for cell viability. (embl.de)
  • TGB3 transport to cell peripheral bodies was previously shown to bypass the secretory pathway and involve a non-conventional mechanism. (microbiologyresearch.org)
  • Based on 3-d structures of APC superfamily members, Rudnick ( 2011 ) has proposed the pathway for transport and suggested a 'rocking bundle' mechanism of transport. (tcdb.org)
  • The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease processes. (bio-rad.com)
  • Possibly, these two transmembrane proteins comprise the pathway for transmembrane transport. (tcdb.org)
  • In order to evaluate the role of this protein in human inherited diseases such as cystinuria, we have isolated a human D2 clone (D2H) by low stringency screening of a human kidney cDNA library using the radiolabeled D2 insert as a probe. (jci.org)
  • Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. (embl.de)
  • Classical GAP proteins accelerate GTPase activity by supplying an arginine finger to the active site. (embl.de)
  • Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). (embl.de)
  • Both guanine nucleotide-exchange proteins and GTPase-activating proteins (GAPs) for ARFs have been cloned recently. (embl.de)
  • Inhibition of COPII budding complex formation by the expression of a dominant-negative mutant of the small GTPase Sar1 had no detectable effect on BMB2 subcellular targeting, which therefore could occur without exit from the ER in COPII transport vesicles. (microbiologyresearch.org)
  • Vesicle transport: more work for the Rabs? (embl.de)
  • The diversity of Rab proteins in vesicle transport. (embl.de)
  • The ARFGAP domain is clearly unrelated to the other GAP proteins structures which are exclusively helical. (embl.de)
  • TGB3 is a small integral membrane protein that contains subcellular targeting signals and directs both TGB2 and the helicase domain-containing TGB1 protein to plasmodesmata-associated structures. (microbiologyresearch.org)
  • Agrobacterium-mediated transient co-expression in Nicotiana benthamiana leaves revealed that green fluorescent protein (GFP)-fused actin-binding domains of Arabidopsis fimbrin (ABD2-GFP) and mouse talin (TAL-GFP) inhibited the subcellular targeting of TGB3 and BMB2 to plasmodesmata-associated bodies, which resulted in TGB3 and BMB2 accumulation in the cytoplasm in association with aberrant ER structures. (microbiologyresearch.org)
  • These agents are classified according to their chemical structures: the three nucleoside analogues include lamivudine, telbivudine and entecavir, whereas the two nucleotide analogues include adefovir dipivoxil, tenofovir disoproxil fumarate (TDF), [ 2 ] and the newly approved tenofovir alafenamide (TAF). (medscape.com)
  • Inside the mitochondria, pyruvate is completely oxidized through the TCA cycle, feeding reductive equivalents to the electron transport chain. (hindawi.com)
  • A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. (bvsalud.org)
  • Recent findings, however, indicate that their function in vesicle trafficking can go beyond this role, and a number of proteins, unrelated to each other, have been identified as putative Rab effectors. (embl.de)
  • PTMs are involved in many protein activities and cellular processes, such as protein folding, stability, conformation, and some significant regulatory mechanisms [ 1 ]. (hindawi.com)
  • The journal will also report progress in the fields of transport routes and mechanisms including efflux proteins and multi-drug resistance. (ingentaconnect.com)
  • The long term goal of our research is to elucidate the molecular mechanisms by which proteins are targeted to specific and distinct compartments. (stanford.edu)
  • This protein family includes an uncharacterised member designated phnA in Escherichia coli, part of a large operon associated with alkylphosphonate uptake and carbon-phosphorus bond cleavage. (embl-heidelberg.de)
  • The PhnA protein family includes the uncharacterised Escherichia coli protein PhnA and its homologues. (embl-heidelberg.de)
  • The cryo-EM analysis also revealed a population of free V 1 bound to Oxidation Resistance 1 (Oxr1p), a poorly characterized protein that has been implicated in protecting cells from oxidative stress. (upstate.edu)
  • shown in red), a poorly characterized protein implicated in oxidative stress response. (upstate.edu)
  • 2009 identified 21 families of these substrate capture proteins, each with a different specificity predicted by genome context analyses. (tcdb.org)
  • They are regulated by a diverse group of structurally unrelated GDP-GTP exchange factors (GEFs), and a family of GTP-hydrolysis activating proteins (GAPs) containing the conserved TBC domain. (ox.ac.uk)
  • Surprisingly, the sequence analysis of PCR product also revealed the presence of two previously unknown homozygous mutations (TG→CT) at nucleotide positions 554 and 555 in addition to the previously reported heterozygous mutation at position 559. (researchgate.net)
  • Over the next five years, our goals are to (1) identify novel recycling receptors required at different Golgi compartments and establish a systematic map of the intra-Golgi recycling network, (2) determine how the transmembrane receptors engage with their cargos, and (3) define the novel functions of a disease-associated membrane transporter in solute transport and protein recycling in the Golgi. (cornell.edu)
  • Absence of extracytoplasmic solute-binding proteins among the members of this group, however, is a distinctive feature. (tcdb.org)
  • To identify proteins interacting with alpha A-crystallin (CRYAA) and to investigate the potential role that these protein interactions play in the function of CRYAA using a human proteome (HuProt) microarray. (molvis.org)
  • A HuProt microarray composed of 17,225 human full-length proteins with N-terminal glutathione S-transferase (GST) tags was used to identify protein-protein interactions. (molvis.org)
  • The protein-protein interactions may help CRYAA carry out multifaceted functions. (molvis.org)
  • To understand the functions of CRYAA and how these are regulated, protein-protein interactions need to be investigated. (molvis.org)
  • As the assembly was carried out in the absence of ATP, this suggests that formation of the holoenzyme from the individual subcomplexes is solely driven by protein-protein interactions at the interface. (upstate.edu)
  • Unlike reversible disassembly, which requires ATP hydrolysis on V 1 to break protein-protein interactions, Oxr1p mediated disassembly of V-ATPase is ATP independent and therefore a novel mode of activity regulation. (upstate.edu)
  • Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • however, the mechanistic basis of how most Golgi proteins are selected for recycling, or how these processes are regulated are poorly understood. (cornell.edu)
  • For example, alkaline vacuole/lysosome are deficient in autophagy, Golgi pH regulates its ability to glycosylate proteins and failure to maintain endosomal pH perturbs with its ability to recycle receptors to the Plasma membrane or, the trans-Golgi. (upstate.edu)
  • HEK293 cells had an efficient ef flux system for cGMP and the use of inside-out vesicles (IOVs) showed high affinity ATP-dependent cGMP transport with a K m value of 2.3 μM. (scirp.org)
  • It is reported that mAb QCRL-3 inhibits the ATP-dependent transport activity of MRP1 in inside-out membrane vesicles. (bdbiosciences.com)
  • Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. (bdbiosciences.com)
  • These glycoproteins include the CD98 heavy chain protein of Mus musculus (gbU25708) and the orthologous 4F2 cell surface antigen heavy chain of Homo sapiens (spP08195). (tcdb.org)
  • There are 391 PhnA_Zn_Ribbon domains in 391 proteins in SMART's nrdb database. (embl-heidelberg.de)
  • There are 39024 RAB domains in 38982 proteins in SMART's nrdb database. (embl.de)
  • There are 21774 ArfGap domains in 21759 proteins in SMART's nrdb database. (embl.de)
  • Domains of tobacco mosaic virus movement protein essential for its membrane association. (microbiologyresearch.org)
  • Localization of their epitopes to the nucleotide-binding domains of the protein. (bdbiosciences.com)
  • Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein. (yeastgenome.org)
  • nucleotide binding domains in red. (rug.nl)
  • Download DNA or protein sequence, view genomic context and coordinates. (yeastgenome.org)
  • to facilitate higher yields of proteins of interest, we constructed the pasop vector to express heterologous proteins in a. oryzae. (liverpool.ac.uk)
  • Heterologous expression of the bioMNY operon and of the single bioY of the α-proteobacterium Rhodobacter capsulatus conferred biotin-transport activity on recombinant E. coli cells. (tcdb.org)
  • A molecular understanding of membrane traffic has broad implications for our understanding of growth control in cancer, receptor trafficking errors in heart disease, regulation of insulin secretion in diabetes and synaptic vesicle biogenesis and transport in neurological disorders. (stanford.edu)
  • 3 The tandem CBS domain 4 , which is linked to the nucleotide binding protein, plays a pivotal role in the regulation. (rug.nl)
  • Kocer, A., Walko, M., and Feringa, B.L. (2007) Synthesis and utilization of reversible and irreversible light-activated nanovalves derived from the channel protein MscL. (rug.nl)
  • These proteins contain a characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) which displays some similarity to the C4-type GATA zinc finger. (embl.de)
  • unlike most of the motors in this group (which work together in pairs), Kar3 motor protein subunits each bind to and work with non-motor protein subunits, including one called Cik1. (elifesciences.org)
  • Some animal proteins, for example, those in the LAT family (TC# 2.A.3.8) including ASUR4 (gbY12716) and SPRM1 (gbL25068) associate with a type 1 transmembrane glycoprotein that is essential for insertion or activity of the permease and forms a disulfide bridge with it. (tcdb.org)
  • 2023 ). (1) the BioMNY complex with ATPase (BioM) and transmembrane protein (BioN). (tcdb.org)
  • These membrane proteins are homologues to ABC-2 exporters. (tcdb.org)
  • Candidates for other membrane components and regulatory proteins are also identified. (embl-heidelberg.de)
  • Collecting the appropriate specimen at the right time and transporting it to the laboratory under proper conditions are critical pre-analytic components of the testing process. (medscape.com)
  • Monoclonal antibodies that inhibit the transport function of the 190-kDa multidrug resistance protein, MRP. (bdbiosciences.com)
  • MRP1 is a 190 kDa integral membrane phosphoglycoprotein, member of the ATP-binding cassette transporter proteins, overexpressed in some drug-selected resistant cell lines and has been shown to cause multidrug resistance in transfected cells. (bdbiosciences.com)
  • Both of the integral membrane protein constituents of these systems may be distantly related, and in this respect they resemble typical ABC porters. (tcdb.org)
  • Clase de nucleótido translocasas abundantes en las mitocondrias y componente integral de la membrana mitocondrial interna. (bvsalud.org)
  • Integral membrane protein. (lu.se)
  • The mode of action of enzymes and macromolecular complexes as protein machines will be investigated. (manchester.ac.uk)
  • Functional annotation clustering showed that they belong to cell cycle, organelle or nuclear lumen, protein transport, and DNA binding and repair clusters. (molvis.org)
  • We investigate the mobility of proteins in the bacterial cytoplasm and cytoplasmic membrane as well as membrane model systems, using optical microscopy-based techniques such as fluorescence correlation spectroscopy (FCS) and pulsed-FRAP (panel a). (rug.nl)
  • C itself interacts outlived by Applying and channels with beginning nucleotides. (erik-mill.de)

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