Cold Shock Proteins and Peptides
Molecular Sequence Data
Gene Expression Regulation, Bacterial
Amino Acid Sequence
HSP70 Heat-Shock Proteins
HSP90 Heat-Shock Proteins
Sequence Homology, Amino Acid
HSP27 Heat-Shock Proteins
Protein Structure, Secondary
HSP72 Heat-Shock Proteins
Antimicrobial Cationic Peptides
Heat-Shock Proteins, Small
Electrophoresis, Gel, Two-Dimensional
HSC70 Heat-Shock Proteins
A segment of cold shock protein directs the folding of a combinatorial protein. (1/35)It has been suggested that protein domains evolved by the non-homologous recombination of building blocks of subdomain size. In earlier work we attempted to recapitulate domain evolution in vitro. We took a polypeptide segment comprising three beta-strands in the monomeric, five-stranded beta-barrel cold shock protein (CspA) of Escherichia coli as a building block. This segment corresponds to a complete exon in homologous eukaryotic proteins and includes residues that nucleate folding in CspA. We recombined this segment at random with fragments of natural proteins and succeeded in generating a range of folded chimaeric proteins. We now present the crystal structure of one such combinatorial protein, 1b11, a 103-residue polypeptide that includes segments from CspA and the S1 domain of the 30S ribosomal subunit of E. coli. The structure reveals a segment-swapped, six-stranded beta-barrel of unique architecture that assembles to a tetramer. Surprisingly, the CspA segment retains its structural identity in 1b11, recapitulating its original fold and deforming the structure of the S1 segment as necessary to complete a barrel. Our work provides structural evidence that (i) random shuffling of nonhomologous polypeptide segments can lead to folded proteins and unique architectures, (ii) many structural features of the segments are retained, and (iii) some segments can act as templates around which the rest of the protein folds. (+info)
Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion. (2/35)Curli fibers, encoded by the csgBAC genes, promote biofilm formation in Escherichia coli and other enterobacteria. Curli production is dependent on the CsgD transcription activator, which also promotes cellulose biosynthesis. In this study, we investigated the effects of CsgD expression from a weak constitutive promoter in the biofilm formation-deficient PHL565 strain of E. coli. We found that despite its function as a transcription activator, the CsgD protein is localized in the cytoplasmic membrane. Constitutive CsgD expression promotes biofilm formation by PHL565 and activates transcription from the csgBAC promoter; however, csgBAC expression remains dependent on temperature and the growth medium. Constitutive expression of the CsgD protein results in altered transcription patterns for at least 24 novel genes, in addition to the previously identified CsgD-dependent genes. The cspA and fecR genes, encoding regulatory proteins responding to cold shock and to iron, respectively, and yoaD, encoding a putative negative regulator of cellulose biosynthesis, were found to be some of the novel CsgD-regulated genes. Consistent with the predicted functional role, increased expression of the yoaD gene negatively affects cell aggregation, while yoaD inactivation results in stimulation of cell aggregation and leads to increased cellulose production. Inactivation of fecR results in significant increases in both cell aggregation and biofilm formation, while the effects of cspA are not as strong in the conditions tested. Our results indicate that CsgD can modulate cellulose biosynthesis through activation of the yoaD gene. In addition, the positive effect of CsgD on biofilm formation might be enhanced by repression of the fecR gene. (+info)
Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems. (3/35)Although the cold-shock response has now been studied in a number of different organisms for several decades, it is only in the last few years that we have begun to understand the molecular mechanisms that govern adaptation to cold stress. Notably, all organisms from prokaryotes to plants and higher eukaryotes respond to cold shock in a comparatively similar manner. The general response of cells to cold stress is the elite and rapid overexpression of a small group of proteins, the so-called CSPs (cold-shock proteins). The most well characterized CSP is CspA, the major CSP expressed in Escherichia coli upon temperature downshift. More recently, a number of reports have shown that exposing yeast or mammalian cells to sub-physiological temperatures (<30 or <37 degrees C respectively) invokes a co-ordinated cellular response involving modulation of transcription, translation, metabolism, the cell cycle and the cell cytoskeleton. In the present review, we summarize the regulation and role of cold-shock genes and proteins in the adaptive response upon decreased temperature with particular reference to yeast and in vitro cultured mammalian cells. Finally, we present an integrated model for the co-ordinated responses required to maintain the viability and integrity of mammalian cells upon mild hypothermic cold shock. (+info)
Global effects of homocysteine on transcription in Escherichia coli: induction of the gene for the major cold-shock protein, CspA. (4/35)Homocysteine (Hcy) is a thiol-containing amino acid that is considered to be medically important because it is linked to the development of several life-threatening diseases in humans, including cardiovascular disease and stroke. It inhibits the growth of Escherichia coli when supplied in the growth medium. Growth inhibition is believed to arise as a result of partial starvation for isoleucine, which occurs because Hcy perturbs the biosynthesis of this amino acid. This study attempted to further elucidate the inhibitory mode of action of Hcy by examining the impact of exogenously supplied Hcy on the transcriptome. Using gene macroarrays the transcript levels corresponding to 68 genes were found to be reproducibly altered in the presence of 0.5 mM Hcy. Of these genes, the biggest functional groups affected were those involved in translation (25 genes) and in amino acid metabolism (19 genes). Genes involved in protection against oxidative stress were repressed in Hcy-treated cells and this correlated with a decrease in catalase activity. The gene showing the strongest induction by Hcy was cspA, which encodes the major cold-shock protein CspA. RT-PCR and reporter fusion experiments confirmed that cspA was induced by Hcy. Induction of cspA by Hcy was not caused by nutritional upshift, a stimulus known to induce CspA expression, nor was it dependent on the presence of a functional CspA protein. The induction of cspA by Hcy was suppressed when isoleucine was included in the growth medium. These data suggest that the induction of CspA expression in the presence of Hcy occurs because of a limitation for isoleucine. The possibility that Hcy-induced cspA expression is triggered by translational stalling that occurs when the cells are limited for isoleucine is discussed. (+info)
Cold shock domain proteins and glycine-rich RNA-binding proteins from Arabidopsis thaliana can promote the cold adaptation process in Escherichia coli. (5/35)Despite the fact that cold shock domain proteins (CSDPs) and glycine-rich RNA-binding proteins (GRPs) have been implicated to play a role during the cold adaptation process, their importance and function in eukaryotes, including plants, are largely unknown. To understand the functional role of plant CSDPs and GRPs in the cold response, two CSDPs (CSDP1 and CSDP2) and three GRPs (GRP2, GRP4 and GRP7) from Arabidopsis thaliana were investigated. Heterologous expression of CSDP1 or GRP7 complemented the cold sensitivity of BX04 mutant Escherichia coli that lack four cold shock proteins (CSPs) and is highly sensitive to cold stress, and resulted in better survival rate than control cells during incubation at low temperature. In contrast, CSDP2 and GRP4 had very little ability. Selective evolution of ligand by exponential enrichment (SELEX) revealed that GRP7 does not recognize specific RNAs but binds preferentially to G-rich RNA sequences. CSDP1 and GRP7 had DNA melting activity, and enhanced RNase activity. In contrast, CSDP2 and GRP4 had no DNA melting activity and did not enhance RNAase activity. Together, these results indicate that CSDPs and GRPs help E.coli grow and survive better during cold shock, and strongly imply that CSDP1 and GRP7 exhibit RNA chaperone activity during the cold adaptation process. (+info)
Bacterial toxicity of potassium tellurite: unveiling an ancient enigma. (6/35)Biochemical, genetic, enzymatic and molecular approaches were used to demonstrate, for the first time, that tellurite (TeO(3) (2-)) toxicity in E. coli involves superoxide formation. This radical is derived, at least in part, from enzymatic TeO(3) (2-) reduction. This conclusion is supported by the following observations made in K(2)TeO(3)-treated E. coli BW25113: i) induction of the ibpA gene encoding for the small heat shock protein IbpA, which has been associated with resistance to superoxide, ii) increase of cytoplasmic reactive oxygen species (ROS) as determined with ROS-specific probe 2'7'-dichlorodihydrofluorescein diacetate (H(2)DCFDA), iii) increase of carbonyl content in cellular proteins, iv) increase in the generation of thiobarbituric acid-reactive substances (TBARs), v) inactivation of oxidative stress-sensitive [Fe-S] enzymes such as aconitase, vi) increase of superoxide dismutase (SOD) activity, vii) increase of sodA, sodB and soxS mRNA transcription, and viii) generation of superoxide radical during in vitro enzymatic reduction of potassium tellurite. (+info)
Role of RNA structure and susceptibility to RNase E in regulation of a cold shock mRNA, cspA mRNA. (7/35)Degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30 degrees C and is moderately dependent on RNase E. Investigations in vitro show that degradosomes prepared from normal or cold-shocked cultures cleave the cspA mRNA preferentially at a single site in vitro between two stem-loops approximately 24 residues 3' to the termination codon and approximately 31 residues from the 3' end. The site of cleavage is independent of the temperature and largely independent of the phosphorylation status of the 5' end of cspA mRNA. A 5' stem-loop, potential occlusion of the initiation and termination codons, temperature-dependent translational efficiency, and the position of the RNase E cleavage site can explain the differential stability of the cspA mRNA. (+info)
Dimorphic aggregation behavior of a fusion polypeptide incorporating a stable protein domain (EGFP) with an amyloidogenic sequence (retroCspA). (8/35)(+info)
Cold shock proteins and peptides are a group of proteins and peptides that are produced in response to exposure to cold temperatures. These proteins and peptides are thought to play a role in protecting cells from the damaging effects of cold stress. They are found in a variety of organisms, including bacteria, plants, and animals, and are induced by exposure to temperatures below the optimal growth temperature for the organism. Cold shock proteins and peptides are believed to function by stabilizing cellular structures, preventing the formation of ice crystals, and protecting cellular enzymes from cold-induced denaturation. They have been the subject of extensive research in the medical field due to their potential therapeutic applications, including their use in the treatment of cold-related injuries and diseases.
In the medical field, "cold temperature" refers to a body temperature that is below the normal range of 98.6°F (37°C). This can be caused by a variety of factors, including exposure to cold temperatures, certain medical conditions, or the use of certain medications. A person with a cold temperature may experience symptoms such as shivering, feeling weak or fatigued, and having difficulty concentrating. In severe cases, a cold temperature can lead to hypothermia, which is a life-threatening condition characterized by a dangerously low body temperature. Medical professionals may use various methods to measure body temperature, including oral thermometers, rectal thermometers, and ear thermometers. If a person's body temperature is found to be below the normal range, they may be treated with measures to raise their body temperature, such as warm blankets or heating pads, and in severe cases, may require hospitalization for further treatment.
Heat-shock proteins (HSPs) are a group of proteins that are produced in response to cellular stress, such as heat, oxidative stress, or exposure to toxins. They are also known as stress proteins or chaperones because they help to protect and stabilize other proteins in the cell. HSPs play a crucial role in maintaining cellular homeostasis and preventing the aggregation of misfolded proteins, which can lead to cell damage and death. They also play a role in the immune response, helping to present antigens to immune cells and modulating the activity of immune cells. In the medical field, HSPs are being studied for their potential as diagnostic and therapeutic targets in a variety of diseases, including cancer, neurodegenerative disorders, and infectious diseases. They are also being investigated as potential biomarkers for disease progression and as targets for drug development.
Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.
In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. They are typically composed of 2-50 amino acids and can be found in a variety of biological molecules, including hormones, neurotransmitters, and enzymes. Peptides play important roles in many physiological processes, including growth and development, immune function, and metabolism. They can also be used as therapeutic agents to treat a variety of medical conditions, such as diabetes, cancer, and cardiovascular disease. In the pharmaceutical industry, peptides are often synthesized using chemical methods and are used as drugs or as components of drugs. They can be administered orally, intravenously, or topically, depending on the specific peptide and the condition being treated.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
HSP70 heat shock proteins are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or infection. They are also known as heat shock proteins because they are upregulated in cells exposed to high temperatures. HSP70 proteins play a crucial role in the folding and refolding of other proteins in the cell. They act as molecular chaperones, helping to stabilize and fold newly synthesized proteins, as well as assisting in the refolding of misfolded proteins. This is important because misfolded proteins can aggregate and form toxic structures that can damage cells and contribute to the development of diseases such as Alzheimer's, Parkinson's, and Huntington's. In addition to their role in protein folding, HSP70 proteins also play a role in the immune response. They can be recognized by the immune system as foreign antigens and can stimulate an immune response, leading to the production of antibodies and the activation of immune cells. Overall, HSP70 heat shock proteins are important for maintaining cellular homeostasis and protecting cells from damage. They are also of interest in the development of new therapies for a variety of diseases.
Bacillus subtilis is a gram-positive, rod-shaped bacterium that is commonly found in soil and the gastrointestinal tracts of animals. It is a member of the Bacillus genus and is known for its ability to form endospores, which are highly resistant to environmental stressors such as heat, radiation, and chemicals. In the medical field, B. subtilis is used in a variety of applications, including as a probiotic to promote gut health, as a source of enzymes for industrial processes, and as a model organism for studying bacterial genetics and metabolism. It has also been studied for its potential use in the treatment of certain infections, such as those caused by antibiotic-resistant bacteria. However, it is important to note that B. subtilis can also cause infections in humans, particularly in individuals with weakened immune systems. These infections can range from mild skin infections to more serious bloodstream infections. As such, it is important to use caution when working with this bacterium and to follow proper safety protocols to prevent the spread of infection.
In the medical field, a base sequence refers to the specific order of nucleotides (adenine, thymine, cytosine, and guanine) that make up the genetic material (DNA or RNA) of an organism. The base sequence determines the genetic information encoded within the DNA molecule and ultimately determines the traits and characteristics of an individual. The base sequence can be analyzed using various techniques, such as DNA sequencing, to identify genetic variations or mutations that may be associated with certain diseases or conditions.
Escherichia coli (E. coli) is a type of bacteria that is commonly found in the human gut. E. coli proteins are proteins that are produced by E. coli bacteria. These proteins can have a variety of functions, including helping the bacteria to survive and thrive in the gut, as well as potentially causing illness in humans. In the medical field, E. coli proteins are often studied as potential targets for the development of new treatments for bacterial infections. For example, some E. coli proteins are involved in the bacteria's ability to produce toxins that can cause illness in humans, and researchers are working to develop drugs that can block the activity of these proteins in order to prevent or treat E. coli infections. E. coli proteins are also used in research to study the biology of the bacteria and to understand how it interacts with the human body. For example, researchers may use E. coli proteins as markers to track the growth and spread of the bacteria in the gut, or they may use them to study the mechanisms by which the bacteria causes illness. Overall, E. coli proteins are an important area of study in the medical field, as they can provide valuable insights into the biology of this important bacterium and may have potential applications in the treatment of bacterial infections.
The Cold-Shock Response (CSR) is a cellular response that occurs in organisms exposed to sudden and severe cold temperatures. It is a protective mechanism that helps cells survive and adapt to the cold stress. In the medical field, the CSR is of particular interest in the study of cold-related injuries and diseases, such as hypothermia, frostbite, and cold-induced illnesses. The CSR involves a complex series of molecular and cellular events that lead to the production of heat shock proteins (HSPs), which help protect cells from damage caused by cold stress. The CSR is triggered by the exposure of cells to cold temperatures, which leads to the formation of ice crystals within the cells. This ice crystal formation causes damage to cellular structures and triggers the activation of stress response pathways. In response, cells produce HSPs, which help protect cellular structures from damage and promote their repair. Overall, the CSR is an important mechanism that helps organisms survive and adapt to cold temperatures, and it has important implications for the prevention and treatment of cold-related injuries and diseases.
In the medical field, "Shock, Septic" refers to a severe and life-threatening condition that occurs when the body's immune system overreacts to an infection, leading to widespread inflammation and damage to organs and tissues. Septic shock is a type of sepsis, which is a condition that occurs when the body's response to an infection causes inflammation throughout the body. In septic shock, the immune system releases large amounts of chemicals that cause blood vessels to narrow and blood pressure to drop, leading to reduced blood flow to vital organs such as the heart, brain, and kidneys. Symptoms of septic shock may include fever, chills, rapid heartbeat, rapid breathing, confusion, and decreased urine output. Treatment for septic shock typically involves antibiotics to treat the underlying infection, fluids and medications to maintain blood pressure and oxygen levels, and supportive care to manage symptoms and prevent complications.，。
In the medical field, "Adaptation, Physiological" refers to the ability of an organism to adjust to changes in its environment or to changes in its internal state in order to maintain homeostasis. This can involve a wide range of physiological processes, such as changes in heart rate, blood pressure, breathing rate, and hormone levels. For example, when a person is exposed to high temperatures, their body may undergo physiological adaptations to help them stay cool. This might include sweating to release heat from the skin, or dilating blood vessels to increase blood flow to the skin and help dissipate heat. Physiological adaptations can also occur in response to changes in an individual's internal state, such as during exercise or when the body is under stress. For example, during exercise, the body may increase its production of oxygen and glucose to meet the increased energy demands of the muscles. Overall, physiological adaptations are a fundamental aspect of how organisms are able to survive and thrive in a changing environment.
In the medical field, a shock is a life-threatening medical condition characterized by a sudden and severe drop in blood pressure, which results in inadequate blood flow to vital organs and tissues. This can lead to a range of symptoms, including rapid or weak pulse, rapid or shallow breathing, confusion, dizziness, and loss of consciousness. There are several types of shock, including: 1. Hypovolemic shock: This type of shock occurs when the body loses a significant amount of blood or fluid, leading to a drop in blood volume and blood pressure. 2. Cardiogenic shock: This type of shock occurs when the heart is unable to pump enough blood to meet the body's needs, often due to a heart attack or severe heart failure. 3. Distributive shock: This type of shock occurs when the body's blood vessels dilate, leading to a drop in blood pressure and inadequate blood flow to vital organs and tissues. 4. Septic shock: This type of shock occurs when the body's immune system overreacts to an infection, leading to widespread inflammation and damage to organs and tissues. Prompt recognition and treatment of shock are critical to prevent further complications and improve outcomes. Treatment typically involves addressing the underlying cause of the shock, such as administering fluids or medications to increase blood pressure, and providing supportive care to maintain vital organ function.
HSP90 Heat-Shock Proteins are a family of proteins that play a crucial role in the folding and stability of other proteins in the cell. They are also involved in a variety of cellular processes, including cell growth, differentiation, and apoptosis. HSP90 proteins are highly conserved across different species and are found in all kingdoms of life. In the medical field, HSP90 Heat-Shock Proteins have been implicated in a number of diseases, including cancer, neurodegenerative disorders, and infectious diseases. In cancer, HSP90 is often overexpressed and is thought to play a role in the development and progression of the disease by stabilizing and promoting the activity of key oncogenic proteins. As a result, HSP90 has become a target for cancer therapy, and several drugs that target HSP90 have been developed and are currently being tested in clinical trials.
RNA, Bacterial refers to the ribonucleic acid molecules that are produced by bacteria. These molecules play a crucial role in the functioning of bacterial cells, including the synthesis of proteins, the regulation of gene expression, and the metabolism of nutrients. Bacterial RNA can be classified into several types, including messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA), which all have specific functions within the bacterial cell. Understanding the structure and function of bacterial RNA is important for the development of new antibiotics and other treatments for bacterial infections.
HSP27 Heat-Shock Proteins are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or injury. They are also known as heat shock proteins 27 or HSPB1. HSP27 proteins are found in all cells and tissues of the body and play a crucial role in maintaining cellular homeostasis and protecting cells from damage. HSP27 proteins are involved in a variety of cellular processes, including cell proliferation, differentiation, and apoptosis (programmed cell death). They also play a role in regulating the immune response and have been implicated in the development of various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. In the medical field, HSP27 proteins are being studied as potential therapeutic targets for the treatment of various diseases. For example, some researchers are investigating the use of HSP27 inhibitors to treat cancer, while others are studying the potential of HSP27 as a biomarker for disease diagnosis and prognosis.
RNA-binding proteins (RBPs) are a class of proteins that interact with RNA molecules, either in the cytoplasm or in the nucleus of cells. These proteins play important roles in various cellular processes, including gene expression, RNA stability, and RNA transport. In the medical field, RBPs are of particular interest because they have been implicated in a number of diseases, including cancer, neurological disorders, and viral infections. For example, some RBPs have been shown to regulate the expression of genes that are involved in cell proliferation and survival, and mutations in these proteins can contribute to the development of cancer. Other RBPs have been implicated in the regulation of RNA stability and turnover, and changes in the levels of these proteins can affect the stability of specific mRNAs and contribute to the development of neurological disorders. In addition, RBPs play important roles in the regulation of viral infections. Many viruses encode proteins that interact with host RBPs, and these interactions can affect the stability and translation of viral mRNAs, as well as the overall pathogenesis of the infection. Overall, RBPs are an important class of proteins that play critical roles in many cellular processes, and their dysfunction has been implicated in a number of diseases. As such, they are an active area of research in the medical field, with the potential to lead to the development of new therapeutic strategies for a variety of diseases.
Chaperonin 60, also known as GroEL or Hsp60, is a protein complex that plays a crucial role in the folding and assembly of proteins in the cell. It is found in all organisms, from bacteria to humans, and is particularly important in the folding of newly synthesized proteins and the refolding of misfolded proteins. The chaperonin 60 complex consists of two identical subunits, each with a molecular weight of approximately 60 kDa, hence the name. The subunits form a barrel-like structure with a central cavity that can accommodate unfolded or partially folded proteins. The complex uses energy from ATP hydrolysis to facilitate the folding process by stabilizing the intermediate states of the protein as it folds into its final structure. In the medical field, chaperonin 60 has been implicated in a number of diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease, as well as certain types of cancer. Abnormal folding of chaperonin 60 has also been linked to the development of certain types of bacterial infections. As such, understanding the role of chaperonin 60 in protein folding and its involvement in disease may lead to the development of new therapeutic strategies for these conditions.
In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.
In the medical field, a peptide fragment refers to a short chain of amino acids that are derived from a larger peptide or protein molecule. Peptide fragments can be generated through various techniques, such as enzymatic digestion or chemical cleavage, and are often used in diagnostic and therapeutic applications. Peptide fragments can be used as biomarkers for various diseases, as they may be present in the body at elevated levels in response to specific conditions. For example, certain peptide fragments have been identified as potential biomarkers for cancer, neurodegenerative diseases, and cardiovascular disease. In addition, peptide fragments can be used as therapeutic agents themselves. For example, some peptide fragments have been shown to have anti-inflammatory or anti-cancer properties, and are being investigated as potential treatments for various diseases. Overall, peptide fragments play an important role in the medical field, both as diagnostic tools and as potential therapeutic agents.
HSP72 heat shock proteins are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or infection. They are also known as heat shock proteins 70 (HSP70) and are found in all living organisms, from bacteria to humans. HSP72 proteins play a crucial role in protecting cells from damage and promoting their survival. They act as molecular chaperones, helping to fold and stabilize other proteins in the cell, and preventing them from aggregating or becoming damaged. They also play a role in the degradation of damaged proteins and in the activation of immune responses. In the medical field, HSP72 proteins are being studied for their potential therapeutic applications. For example, they have been shown to have anti-inflammatory and anti-cancer effects, and they may be useful in treating a variety of diseases, including neurodegenerative disorders, cardiovascular disease, and cancer. They are also being investigated as potential biomarkers for disease diagnosis and prognosis.
Hemorrhagic shock is a medical emergency that occurs when a person loses a significant amount of blood, leading to a drop in blood pressure and inadequate blood flow to vital organs. This can result in damage to organs, tissue, and cells, and if not treated promptly, can be life-threatening. Hemorrhagic shock can be caused by a variety of factors, including trauma (such as a severe injury or surgery), childbirth, severe bleeding from a medical condition (such as a bleeding ulcer or a bleeding tumor), or a severe allergic reaction. Symptoms of hemorrhagic shock may include pale skin, rapid heartbeat, rapid breathing, dizziness or lightheadedness, cold, clammy skin, and a weak or rapid pulse. Treatment typically involves stabilizing the patient's blood pressure and stopping the bleeding, which may involve surgery, medications, or other interventions.
The common cold is a viral infection that affects the upper respiratory tract, including the nose, throat, and sinuses. It is caused by a variety of viruses, including rhinoviruses, coronaviruses, and adenoviruses. The common cold is highly contagious and can be spread through contact with infected individuals or surfaces contaminated with the virus. Symptoms of the common cold typically include a runny or stuffy nose, sore throat, cough, and sometimes fever, body aches, and headaches. The common cold is a self-limiting illness, meaning that it will usually resolve on its own within a week or two without the need for medical treatment. However, over-the-counter medications such as pain relievers, decongestants, and cough suppressants can help alleviate symptoms.
A peptide library is a collection of synthetic peptides that are designed to represent a diverse range of possible peptide sequences. These libraries are used in various fields of medicine, including drug discovery, vaccine development, and diagnostics. In drug discovery, peptide libraries are used to identify potential drug candidates by screening for peptides that bind to specific targets, such as receptors or enzymes. These libraries can be designed to contain a large number of different peptide sequences, allowing researchers to identify a wide range of potential drug candidates. In vaccine development, peptide libraries are used to identify peptides that can stimulate an immune response. These peptides can be used to create vaccines that are designed to elicit a specific immune response against a particular pathogen. In diagnostics, peptide libraries are used to identify peptides that can be used as biomarkers for specific diseases. These peptides can be detected in biological samples, such as blood or urine, and can be used to diagnose or monitor the progression of a particular disease. Overall, peptide libraries are a valuable tool in the medical field, allowing researchers to identify potential drug candidates, develop vaccines, and diagnose diseases.
Lactams, macrocyclic are a class of organic compounds that contain a ring of atoms with a nitrogen atom at the center. They are also known as lactones or macrolactams. Macrocyclic lactams are often used in the medical field as antibiotics, such as the antibiotic vancomycin, which is used to treat severe bacterial infections. They are also used in other therapeutic applications, such as in the treatment of cancer and as imaging agents in diagnostic procedures.
Benzoquinones are a class of organic compounds that contain a benzene ring with two ketone groups (-C=O) attached to adjacent carbon atoms. They are commonly found in nature and are also synthesized in the laboratory for various industrial and medicinal applications. In the medical field, benzoquinones have been studied for their potential therapeutic effects. Some benzoquinones have been found to have anti-inflammatory, anti-cancer, and anti-bacterial properties. For example, some benzoquinones have been shown to inhibit the growth of certain types of cancer cells, while others have been found to have anti-inflammatory effects in animal models of inflammatory diseases. However, it is important to note that not all benzoquinones are safe or effective for medical use, and some may even be toxic or harmful. Therefore, the use of benzoquinones in medicine should be carefully evaluated and monitored by medical professionals.
Molecular chaperones are a class of proteins that assist in the folding, assembly, and transport of other proteins within cells. They play a crucial role in maintaining cellular homeostasis and preventing the accumulation of misfolded or aggregated proteins, which can lead to various diseases such as neurodegenerative disorders, cancer, and certain types of infections. Molecular chaperones function by binding to nascent or partially folded proteins, preventing them from aggregating and promoting their proper folding. They also assist in the assembly of multi-subunit proteins, such as enzymes and ion channels, by ensuring that the individual subunits are correctly folded and assembled into a functional complex. There are several types of molecular chaperones, including heat shock proteins (HSPs), chaperonins, and small heat shock proteins (sHSPs). HSPs are induced in response to cellular stress, such as heat shock or oxidative stress, and are involved in the refolding of misfolded proteins. Chaperonins, on the other hand, are found in the cytosol and the endoplasmic reticulum and are involved in the folding of large, complex proteins. sHSPs are found in the cytosol and are involved in the stabilization of unfolded proteins and preventing their aggregation. Overall, molecular chaperones play a critical role in maintaining protein homeostasis within cells and are an important target for the development of new therapeutic strategies for various diseases.
Antimicrobial cationic peptides (ACPs) are a class of naturally occurring peptides that have the ability to kill or inhibit the growth of microorganisms, such as bacteria, fungi, and viruses. They are characterized by their positive charge, which allows them to interact with the negatively charged cell membranes of microorganisms and disrupt their integrity, leading to cell death. ACPs are found in a variety of organisms, including plants, insects, and animals, and are often part of the innate immune system. They are also being studied for their potential use in the development of new antibiotics and antifungal agents, as well as for their potential therapeutic applications in the treatment of a range of infections and inflammatory diseases. Some examples of ACPs include defensins, cathelicidins, and histatins. These peptides are typically small, ranging in size from 10 to 50 amino acids, and are highly conserved across different species, suggesting that they have an important biological function.
Heat-Shock Proteins, Small (HSPs) are a group of proteins that are produced in response to cellular stress, such as heat, oxidative stress, or exposure to toxins. They are also known as stress proteins or chaperones because they help to protect and stabilize other proteins in the cell. Small Heat-Shock Proteins (sHSPs) are a subclass of HSPs that are typically between 10 and 40 kDa in size. They are found in all organisms and are involved in a variety of cellular processes, including protein folding, stabilization, and degradation. In the medical field, sHSPs have been studied for their potential role in a variety of diseases, including cancer, neurodegenerative disorders, and infectious diseases. Some research suggests that sHSPs may have anti-inflammatory and anti-apoptotic effects, and may be involved in the regulation of immune responses. However, more research is needed to fully understand the role of sHSPs in health and disease.
In the medical field, acclimatization refers to the process by which an individual's body adapts to changes in environmental conditions, particularly changes in altitude. When a person moves to a higher altitude, the air pressure and oxygen levels decrease, which can cause altitude sickness if the body is not able to adjust quickly enough. Acclimatization helps the body to gradually adjust to these changes by increasing the production of red blood cells, which carry oxygen, and by allowing the body to adjust its breathing and heart rate. This process can take several days to several weeks, depending on the altitude and the individual's fitness level.
In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. Cyclic peptides are a type of peptide in which the amino acids are linked in a ring-like structure, rather than in a linear chain. These cyclic peptides can have a variety of biological activities, including antimicrobial, antiviral, and anti-inflammatory effects. They are being studied for their potential use in the development of new drugs and therapies.
In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.
In the medical field, oligopeptides are short chains of amino acids that typically contain between two and 50 amino acids. They are often used in various medical applications due to their unique properties and potential therapeutic effects. One of the main benefits of oligopeptides is their ability to penetrate the skin and reach underlying tissues, making them useful in the development of topical treatments for a variety of conditions. For example, oligopeptides have been shown to improve skin elasticity, reduce the appearance of wrinkles, and promote the growth of new skin cells. Oligopeptides are also used in the development of medications for a variety of conditions, including osteoporosis, diabetes, and hypertension. They work by interacting with specific receptors in the body, which can help to regulate various physiological processes and improve overall health. Overall, oligopeptides are a promising area of research in the medical field, with potential applications in a wide range of therapeutic areas.
Cloning, molecular, in the medical field refers to the process of creating identical copies of a specific DNA sequence or gene. This is achieved through a technique called polymerase chain reaction (PCR), which amplifies a specific DNA sequence to produce multiple copies of it. Molecular cloning is commonly used in medical research to study the function of specific genes, to create genetically modified organisms for therapeutic purposes, and to develop new drugs and treatments. It is also used in forensic science to identify individuals based on their DNA. In the context of human cloning, molecular cloning is used to create identical copies of a specific gene or DNA sequence from one individual and insert it into the genome of another individual. This technique has been used to create transgenic animals, but human cloning is currently illegal in many countries due to ethical concerns.
Chaperonins are a class of molecular chaperones that assist in the folding of proteins. They are found in all forms of life and play a crucial role in maintaining cellular homeostasis by preventing protein aggregation and misfolding. There are two main types of chaperonins: Group I chaperonins, which are found in the cytoplasm, and Group II chaperonins, which are found in the mitochondria and chloroplasts. The most well-known chaperonin is the GroEL/GroES complex, which is found in Group I chaperonins. This complex consists of two subunits, GroEL and GroES, which work together to fold proteins. GroEL acts as a cage-like structure that surrounds the unfolded protein, while GroES acts as a lid that covers the opening of the cage. The two subunits work together to facilitate the folding of the protein by providing a protected environment and using ATP to drive conformational changes in the protein. Chaperonins are important for the proper functioning of many cellular processes, including protein synthesis, cell division, and stress response. Mutations in chaperonin genes can lead to a variety of diseases, including neurodegenerative disorders, such as Alzheimer's and Parkinson's disease, and certain types of cancer.
HSC70 Heat-Shock Proteins (HSPs) are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or infection. They are also known as heat shock proteins 70 (HSP70) and are found in all living organisms, from bacteria to humans. HSC70 HSPs play a crucial role in maintaining cellular homeostasis by helping to refold misfolded or damaged proteins, preventing protein aggregation, and assisting in the degradation of damaged proteins. They also play a role in the immune response by helping to transport antigens to the cell surface for presentation to the immune system. In the medical field, HSC70 HSPs have been studied for their potential therapeutic applications. For example, they have been shown to have anti-inflammatory and anti-cancer effects, and they are being investigated as potential treatments for a variety of diseases, including neurodegenerative disorders, cancer, and autoimmune diseases.
Cardiogenic shock is a medical condition in which the heart is unable to pump enough blood to meet the body's needs. This can occur as a result of a heart attack, heart failure, or other conditions that affect the heart's ability to function properly. Symptoms of cardiogenic shock may include rapid or weak pulse, low blood pressure, confusion, and shortness of breath. Treatment typically involves medications to improve heart function and support organ function, as well as mechanical support such as a heart pump. In severe cases, surgery may be necessary to repair or replace the damaged heart tissue.
In the medical field, a cell line refers to a group of cells that have been derived from a single parent cell and have the ability to divide and grow indefinitely in culture. These cells are typically grown in a laboratory setting and are used for research purposes, such as studying the effects of drugs or investigating the underlying mechanisms of diseases. Cell lines are often derived from cancerous cells, as these cells tend to divide and grow more rapidly than normal cells. However, they can also be derived from normal cells, such as fibroblasts or epithelial cells. Cell lines are characterized by their unique genetic makeup, which can be used to identify them and compare them to other cell lines. Because cell lines can be grown in large quantities and are relatively easy to maintain, they are a valuable tool in medical research. They allow researchers to study the effects of drugs and other treatments on specific cell types, and to investigate the underlying mechanisms of diseases at the cellular level.
Testis-enhanced gene transfer family
Heat shock protein
Alfred L. Goldberg
List of examples of convergent evolution
Gamma delta T cell
Feline arterial thromboembolism
Mitogen-activated protein kinase
Euthyroid sick syndrome
Natural killer cell
Heat shock response
Testis-enhanced gene transfer family - Wikipedia
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Regulate the activity2
- Included here are peptides and proteins that regulate the activity of transcription factors and cellular processes in response to signals from cell surface receptors. (usda.gov)
- A group of cell cycle proteins that negatively regulate the activity of CYCLIN / CYCLIN-DEPENDENT KINASE complexes. (nih.gov)
- The trimeric Sec61/SecY complex is a protein-conducting channel (PCC) for secretory and membrane proteins. (cipsm.de)
- The testis-enhanced gene transcript (TEGT) family includes the testis-enhanced gene transcript proteins of mammals, which are expressed at high levels in the testis, the putative glutamate/aspartate binding proteins of plants and animals, the YccA protein of Escherichia coli and the YetJ protein of Bacillus subtilis. (wikipedia.org)
- Homologues include a putative cold shock inducible protein and a SecY stabilizing protein. (wikipedia.org)
- The proteins contain putative N‐terminal signal peptides as well as hydro‐phobic C‐terminal sequences, indicating that the proteins may be membrane bound. (researchwithrutgers.com)
- A large family of regulatory proteins that function as accessory subunits to a variety of CYCLIN-DEPENDENT KINASES. (umassmed.edu)
- AMP-Activated Protein Kinases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (rush.edu)
- Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. (rush.edu)
- AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP. (rush.edu)
- This graph shows the total number of publications written about "AMP-Activated Protein Kinases" by people in this website by year, and whether "AMP-Activated Protein Kinases" was a major or minor topic of these publications. (rush.edu)
- Below are the most recent publications written about "AMP-Activated Protein Kinases" by people in Profiles. (rush.edu)
- A family of cell cycle proteins containing ANKYRIN REPEATS that are specific inhibitors of cyclin D-dependent kinases. (nih.gov)
- This enzyme also activates the transcription factor NF-KAPPA B and is composed of alpha and beta catalytic subunits, which are protein kinases and gamma, a regulatory subunit. (uchicago.edu)
- Here we demonstrate that PSRP1 is not a bona fide ribosomal protein, but rather a functional homologue of the Escherichia coli cold-shock protein pY. (cipsm.de)
- Expression of the Escherichia coli tryptophanase operon depends on ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical. (cipsm.de)
- High-level expression and function assay of antimicrobiol peptide TmAMP3 of Tenebrio molitor (Tenebrionidae, Coleoptera) in Escherichia coli [J]. , 2011, 54(10): 1111-1117. (insect.org.cn)
- Price TJ, Das V, Dussor G. Adenosine Monophosphate-activated Protein Kinase (AMPK) Activators For the Prevention, Treatment and Potential Reversal of Pathological Pain. (rush.edu)
- A protein serine-threonine kinase that catalyzes the PHOSPHORYLATION of I KAPPA B PROTEINS. (uchicago.edu)
- d ) Validation of the yeast mRNA interactome using western blotting of input samples and eluate after interactome capture with specific antibodies (ADH1, alcohol dehydrogenase 1, PUB1) or against TAP-tagged proteins (PGK1, phosphoglycerate kinase 1, TDH1, triose phosphate dehydrogenase, TRX2, thioredoxine 2, SHE2, Swi5p-dependent HO Expression 2). (nature.com)
- Image analysis of the matched maps identified 7 proteins that were either over- or down-expressed: activated protein kinase c receptor (LACK), alpha tubulin (×2), prostaglandin f2-alpha synthase, protein disulfide isomerase, vesicular transport protein and a hypothetical protein. (who.int)
- Recombinant proteins containing tetratricopeptide repeat (TPR) domains were constructed and confirmation of the binding capacity to Hsc70 was assessed by ELISA. (biomedcentral.com)
- The recombinant TPR proteins were used for investigation of the effect of TPR proteins on bacterial uptake by TG cells and on pregnancy in mice. (biomedcentral.com)
- In this review, we report the emerging usefulness of the assessment of circulating tumour cells, cell-free DNA, extracellular RNA, cell-free proteins, extracellular vesicles, and tumour-educated platelets to evaluate the changing mutational profile of multiple myeloma, as early markers of disease, reliable predictors of prognosis, and as useful tools to perform less invasive monitoring in multiple myeloma. (bvsalud.org)
- Here it is demonstrated that a TIP1 homologue, TIR1, which had been previously cloned as SRP1 (serine‐rich protein), is strongly induced by a downshift in growth temperature from 30 to 10°C. We further cloned TIR2, which is transcribed at a low basal level but is increased strongly by cold shock and, to a lesser extent, by heat shock. (researchwithrutgers.com)
- These biological oligomers and polymers can be Solid-phase peptide synthesis (SPPS), or in continue produced for custom peptide synthesis projects. (conzort.com)
- The High-efficiency solid phase peptide synthesis (HE-SPPS) is give very low production costs. (conzort.com)
- HS causes poor meat quality by impairing protein synthesis and augmenting undesirable fat in meat. (frontiersin.org)
- Cloning, sequence analysis and expression profiling of a heat shock protein 70 gene in Tenebrio molitor (Coleoptera: Tenebrionidae) ( In English ) [J]. , 2013, 56(5): 475-485. (insect.org.cn)
- Protein conformation is critically linked to function and often controlled by interactions with regulatory factors. (cipsm.de)
- Studies previously conducted show that HS negatively affects the skeletal muscle growth and development by changing its effects on myogenic regulatory factors, insulin growth factor-1, and heat-shock proteins. (frontiersin.org)
- TIP1 is the first known cold‐shock‐and heat‐shock‐induced gene in Saccharomyces cerevisiae. (researchwithrutgers.com)
- Only 60% of yeast and 73% of the human RBPs have functions assigned to RNA biology or structural motifs known to convey RNA binding, and many intensively studied proteins surprisingly emerge as RBPs (termed 'enigmRBPs'), including almost all glycolytic enzymes, pointing to emerging connections between gene regulation and metabolism. (nature.com)
- RNA-binding proteins (RBPs) mediate pivotal cellular functions such as RNA transport, degradation or translation and represent key effectors of post-transcriptional gene regulation. (nature.com)
- Furthermore, gene overexpression is also frequently associated to antifungal resistance as well as an increase in the activity of proteins that reduce oxidative damage. (intechopen.com)
- and Its Interaction with Kaposi Sarcoma-associated Herpes Virus Flice-interacting Protein and IKK Subunit ß by EPR Spectroscopy. (uchicago.edu)
- Plastid-specific ribosomal proteins (PSRPs) have been proposed to play roles in the light-dependent regulation of chloroplast translation. (cipsm.de)
- We show that this conserved RNA interactome harbours many proteins without previously assigned roles in RNA biology (enigmRBPs), including surprisingly many metabolic enzymes. (nature.com)
- A family of inhibitory proteins which bind to the REL PROTO-ONCOGENE PROTEINS and modulate their activity. (bvsalud.org)
- In the CYTOPLASM, I-kappa B proteins bind to the transcription factor NF-KAPPA B. Cell stimulation causes its dissociation and translocation of active NF-kappa B to the nucleus. (bvsalud.org)
- These proteins are about 200-250 residues in length and exhibit 7 TMSs. (wikipedia.org)
- Two others are the rat neural membrane protein 35 and the Arabidopsis thaliana Bax inhibitor-1 (BI-1) protein capable of suppressing Bax-induced cell death in yeast. (wikipedia.org)
- Cell fractionation analysis as well as studies using a yeast strain that is conditionally deficient in glycosylation demonstrate that TIP1 is a heavily modified membrane‐associated protein. (researchwithrutgers.com)
- c ) Overlap of mRNA interactome proteins in yeast and HuH-7. (nature.com)
- Incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection, and improper immune development. (conzort.com)
- Heart failure always causes circulatory failure, but the converse is not necessarily the case, because various noncardiac conditions (eg, hypovolemic shock, septic shock) can produce circulatory failure in the presence of normal, modestly impaired, or even supranormal cardiac function. (medscape.com)
- ABSTRACT In order to define the protein expressional changes related to the process of meglumine antimoniate resistance in anthroponotic cutaneous leishmaniasis (CL), we performed a comparative proteomics analysis on sensitive and resistant strains of Leishmania tropica isolated from Iranian CL patients. (who.int)
- Several molecular mechanisms with antifungal agents have been reported for C. albicans where insertions, deletions, and point mutations in genes codifying target proteins are frequently related to the antifungal drug resistance. (intechopen.com)
- F-box protein specificity for g1 cyclins is dictated by subcellular localization. (umassmed.edu)
- To facilitate the study of these neurons, transgenic mice were generated that express enhanced green fluorescent protein (EGFP) in subpopulations of GABAergic neurons. (jneurosci.org)
- Our results demonstrate that surface located Hsc70 on TG cells mediates the uptake of pathogenic bacteria and proteins containing the TPR domain inhibit the function of Hsc70 by binding to its EEVD motif. (biomedcentral.com)
- Here we report the selection of camelid-derived single-domain antibodies (nanobodies) that modulate the conformation and spectral properties of the green fluorescent protein (GFP). (cipsm.de)
- The aim of the present study was to identify whether P. gingivalis heat‑shock protein 60 (HSP60) induced the dysfunction of human umbilical vein endothelial cells (HUVECs) in vitro. (spandidos-publications.com)
- Furthermore, atherosclerosis can be triggered and aggravated by the pathogen-driven antigenic peptide from P. gingivalis heat-shock protein 60 (HSP60) ( 15 - 17 ). (spandidos-publications.com)
- Here we show that heat shock cognate protein 70 (Hsc70) contributes to bacterial uptake by TG cells and the EEVD motif of Hsc70 plays an important role in this. (biomedcentral.com)
- Furthermore, the transcriptional responses of B5 at different temperature by using rice straw as sole carbon sources were also analyzed, based on which the mechanism of lignocellulose degradation at high temperature was revealed that B5 could resist the heat by up-regulating the heat shock proteins (HSP) and then secrete various Carbohydrate-Active enzymes (CAZymes) to realize energy balance. (researchsquare.com)
- RNA-binding proteins (RBPs) exert a broad range of biological functions. (nature.com)
- Distant homologues found in Drosophilia melanogaster and the rat are the N-methyl-D-aspartate receptor-associated protein (NMDARAI) and the N-methyl-D-aspartate receptor glutamate binding chain, respectively. (wikipedia.org)
- These proteins are distantly related to the ionotropic glutamate-binding protein of the N-methyl D-aspartate (NMDA) receptor of man. (wikipedia.org)
- This family of proteins includes many ONCOGENE PROTEINS as well as a wide variety of classes of INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS such as CASPASES. (bvsalud.org)
- However, detecting the activity of antifreeze proteins still has some difficulties, especially when only a few of insect samples are available from fields. (insect.org.cn)
- In order to explore if differential scanning calorimetry (DSC) can be used to detect thermal hysteresis activity (THA) of the total protein in insects, the THA of the total protein and hemolymph from Tenebrio molitor larvae was detected by DSC. (insect.org.cn)
- The results showed that each of them had thermal hysteresis activity, and the THA was 0.34-0.43℃ for L. dispar , 0.35-0.42℃ for Y. evonymallus and 0.37-0.40℃ for I. subelongatus , suggesting that the three insect species can improve their cold tolerance through producing antifreeze proteins. (insect.org.cn)
- This study indicates that the differential scanning calorimetry is feasible to identify whether one insect species contains antifreeze proteins through detecting thermal hysteresis activity of the total protein. (insect.org.cn)
- P. gingivalis HSP60 at a concentration of 10 ng/l significantly decreased the expression levels of VE‑cadherin and eNOS protein at 24 h stimulation, whereas no difference in these proteins was identified following a low dose of P. gingivalis HSP60 (1 ng/l). (spandidos-publications.com)
- P. gingivalis HSP60 at 100 ng/l significantly downregulated the expression levels of VE‑cadherin and eNOS protein at 12 h in HUVECs. (spandidos-publications.com)
- Cloning, sequencing and expression analysis of antifreeze protein cDNAs from two color varieties of Tenebrio molitor (Coleoptera: Tenebrionidae) [J]. , 2012, 55(6): 659-667. (insect.org.cn)
- Proteins and peptides that are involved in signal transduction within the cell. (usda.gov)
- Preexisting antivector immunity can severely compromise the ability of Salmonella enterica serovar Typhimurium live vaccines to induce protective CD8 T-cell frequencies after type III secretion system-mediated heterologous protein translocation in orally immunized mice. (cipsm.de)
- After cell lysis, polyadenylated RNAs were captured on oligo d(T) beads followed by stringent washes to remove non-crosslinked proteins. (nature.com)
- NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA, cytokine production and cell survival. (conzort.com)
- Cell proteins were analysed with 2-dimensional electrophoresis and differentially expressed proteins were identified by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry. (who.int)
- protein patterns of subjects with leish- Cell culture maniasis . (who.int)
- Bee venom is a colorless, odorless, clear, and water soluble liquid that is resistant to cold and hot temperatures. (fountainmagazine.com)
- The heterochromatin-enriched HP1 proteins play a critical role in regulation of transcription. (cipsm.de)
- The poultry sector is noted to make a considerable contribution to global nutrition and food security, which helps in the provision of cheap protein, essential micronutrients, and energy to humans ( 1 ). (frontiersin.org)
- Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors. (usda.gov)
- The study shows the usefulness of proteomics in identifying proteins that may express differences between sensitive and resistant L. tropica isolates. (who.int)
- Our preliminary study using 2D isolates were recovered from liq- new cases throughout the world cu- gel electrophoresis in drug sensitive/ uid nitrogen, and sub-cultured in taneous leishmaniasis (CL) remains resistant strains of L. tropica showed RPMI1640 medium (Gibco/BRL) a serious public health problem in that some proteins were differentially supplemented with 10% fetal bovine numerous countries [1,2]. (who.int)
- Sample preparation (protein and drug-resistant L. tropica parasites extraction) niasis, early diagnosis and appropriate . (who.int)
- peptide 14 or 19 from P. gingivalis HSP60 may have either an anti- or pro-atherogenic role, respectively, in the ApoE(−/-) mouse model of infection-triggered atherosclerosis through distinct mechanisms operating in the polarization of T cells. (spandidos-publications.com)
- Bacterial TPR proteins bound to the C-terminal of Hsc70 through its EEVD motif and this binding inhibited bacterial uptake by TG cells. (biomedcentral.com)
- Seasonal changes in cold tolerance of desert beetle Anatolica polita borealis (Coleoptera: Tenebrionidae) and their physiological mechanisms [J]. , 2009, 52(4): 372-379. (insect.org.cn)
- Her admission troponin level was 0.9 ng/mL and the brain natriuretic peptide level was 1650 pg/mL. (jiaecho.org)