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Heat Shock
The heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. In a normal cell, proteostasis (protein homeostasis) must be maintained because proteins are the main functional units of the cell. Many proteins take on a defined configuration in a process known as protein folding in order to perform their biological functions. If these structures are altered, critical processes could be affected, leading to cell damage or death. The heat shock response can be employed under stress to induce the expression of heat shock proteins (HSP), many of which are molecular chaperones, that help prevent or reverse protein misfolding and provide an environment for proper folding. Protein folding is already challenging due to the crowded intracellular space where aberrant interactions can arise; it becomes more difficult wh ...
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Heat Shock Protein
Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans. Heat-shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70 and 90 kilodal ...
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Cell Stress Response
Cellular stress response is the wide range of molecular changes that cells undergo in response to environmental stressors, including extremes of temperature, exposure to toxins, and mechanical damage. Cellular stress responses can also be caused by some viral infections. The various processes involved in cellular stress responses serve the adaptive purpose of protecting a cell against unfavorable environmental conditions, both through short term mechanisms that minimize acute damage to the cell's overall integrity, and through longer term mechanisms which provide the cell a measure of resiliency against similar adverse conditions. General characteristics Cellular stress responses are primarily mediated through what are classified as ''stress proteins''. Stress proteins often are further subdivided into two general categories: those that only are activated by stress, or those that are involved both in stress responses and in normal cellular functioning. The essential character of ...
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Heat Shock Response Pathway
In thermodynamics, heat is defined as the form of energy crossing the boundary of a thermodynamic system by virtue of a temperature difference across the boundary. A thermodynamic system does not ''contain'' heat. Nevertheless, the term is also often used to refer to the thermal energy contained in a system as a component of its internal energy and that is reflected in the temperature of the system. For both uses of the term, heat is a form of energy. An example of formal vs. informal usage may be obtained from the right-hand photo, in which the metal bar is "conducting heat" from its hot end to its cold end, but if the metal bar is considered a thermodynamic system, then the energy flowing within the metal bar is called internal energy, not heat. The hot metal bar is also transferring heat to its surroundings, a correct statement for both the strict and loose meanings of ''heat''. Another example of informal usage is the term '' heat content'', used despite the fact that p ...
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Herschel K
Herschel or Herschell may refer to: People * Herschel (name), various people Places * Herschel, Eastern Cape, South Africa * Herschel, Saskatchewan * Herschel, Yukon * Herschel Bay, Canada * Herschel Heights, Alexander Island, Antarctica * Herschel Island, Canada * Mount Herschel, Antarctica * Cape Sterneck, Antarctica Astronomy * Herschel (crater), various craters in the solar system * 2000 Herschel, an asteroid * 35P/Herschel–Rigollet, a comet * Herschel Catalogue (other), various astronomical catalogues of nebulae * Herschel Medal, awarded by the UK Royal Astronomical Society * Herschel Museum of Astronomy, in Bath, United Kingdom * Herschel Space Observatory, operated by the European Space Agency * Herschel wedge, an optical prism used in solar observation * Herschel's Garnet Star, a red supergiant star * William Herschel Telescope, in the Canary Islands * Telescopium Herschelii, a constellation * Uranus, for a time known as Herschel Other us ...
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Serendipitous
Serendipity is an unplanned fortunate discovery. Serendipity is a common occurrence throughout the history of product invention and scientific discovery. Etymology The first noted use of "serendipity" was by Horace Walpole on 28 January 1754. In a letter he wrote to his friend Horace Mann, Walpole explained an unexpected discovery he had made about a lost painting of Bianca Cappello by Giorgio Vasari by reference to a Persian fairy tale, ''The Three Princes of Serendip''. The princes, he told his correspondent, were "always making discoveries, by accidents and sagacity, of things which they were not in quest of." The name comes from '' Serendip'', an old Persian name for Sri Lanka (Ceylon), hence ''Sarandib'' by Arab traders. It is derived from the Sanskrit ''Siṃhaladvīpaḥ'' (Siṃhalaḥ, Sri Lanka + dvīpaḥ, island). The word has been exported into many other languages, with the general meaning of "unexpected discovery" or "fortunate chance". Applications Inven ...
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Drosophila
''Drosophila'' () is a genus of flies, belonging to the family Drosophilidae, whose members are often called "small fruit flies" or (less frequently) pomace flies, vinegar flies, or wine flies, a reference to the characteristic of many species to linger around overripe or rotting fruit. They should not be confused with the Tephritidae, a related family, which are also called fruit flies (sometimes referred to as "true fruit flies"); tephritids feed primarily on unripe or ripe fruit, with many species being regarded as destructive agricultural pests, especially the Mediterranean fruit fly. One species of ''Drosophila'' in particular, '' D. melanogaster'', has been heavily used in research in genetics and is a common model organism in developmental biology. The terms "fruit fly" and "''Drosophila''" are often used synonymously with ''D. melanogaster'' in modern biological literature. The entire genus, however, contains more than 1,500 species and is very diverse in appearan ...
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Polytene Chromosome
Polytene chromosomes are large chromosomes which have thousands of DNA strands. They provide a high level of function in certain tissues such as salivary glands of insects. Polytene chromosomes were first reported by E.G.Balbiani in 1881. Polytene chromosomes are found in dipteran flies: the best understood are those of '' Drosophila'', ''Chironomus'' and '' Rhynchosciara''. They are present in another group of arthropods of the class Collembola, a protozoan group Ciliophora, mammalian trophoblasts and antipodal, and suspensor cells in plants. In insects, they are commonly found in the salivary glands when the cells are not dividing. They are produced when repeated rounds of DNA replication without cell division forms a giant chromosome. Thus polytene chromosomes form when multiple rounds of replication produce many sister chromatids ''which stay fused together''. Polytene chromosomes, at interphase, are seen to have distinct thick and thin banding patterns. These p ...
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Ferruccio Ritossa
Ferruccio Ritossa (February 26, 1936 – January 9, 2014) was an Italian geneticist best known for his discovery of the heat shock response in the model organism ''Drosophila'' (fruit flies). Early life and education Ritossa was born in the town of Pinguente in Istria in 1936, one of three sons. His father, a butcher, was killed in the foibe killings when Ritossa was a young child. His mother moved the family to Italy and taught school in an orphanage, where her three children were also educated. Ritossa attended the University of Bologna to study agricultural sciences and graduated in 1958. He became interested in genetics, particularly in then-emerging molecular studies of the field, and joined a newly established course in biophysics taught by Adriano Buzzati-Traverso at the University of Pavia, where Buzzati-Traverso had begun to establish ''Drosophila'' research and collections. Buzzati-Traverso founded a laboratory, now the Istituto di Genetica e Biofisica, in Naples a ...
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Immune System
The immune system is a network of biological processes that protects an organism from diseases. It detects and responds to a wide variety of pathogens, from viruses to parasitic worms, as well as cancer cells and objects such as wood splinters, distinguishing them from the organism's own healthy tissue. Many species have two major subsystems of the immune system. The innate immune system provides a preconfigured response to broad groups of situations and stimuli. The adaptive immune system provides a tailored response to each stimulus by learning to recognize molecules it has previously encountered. Both use molecules and cells to perform their functions. Nearly all organisms have some kind of immune system. Bacteria have a rudimentary immune system in the form of enzymes that protect against virus infections. Other basic immune mechanisms evolved in ancient plants and animals and remain in their modern descendants. These mechanisms include phagocytosis, antimicrobial ...
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Peptide
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyc ...
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Promoter Region
In genetics, a promoter is a sequence of DNA to which proteins bind to initiate transcription of a single RNA transcript from the DNA downstream of the promoter. The RNA transcript may encode a protein (mRNA), or can have a function in and of itself, such as tRNA or rRNA. Promoters are located near the transcription start sites of genes, upstream on the DNA (towards the 5' region of the sense strand). Promoters can be about 100–1000 base pairs long, the sequence of which is highly dependent on the gene and product of transcription, type or class of RNA polymerase recruited to the site, and species of organism. Promoters control gene expression in bacteria and eukaryotes. RNA polymerase must attach to DNA near a gene for transcription to occur. Promoter DNA sequences provide an enzyme binding site. The -10 sequence is TATAAT. -35 sequences are conserved on average, but not in most promoters. Artificial promoters with conserved -10 and -35 elements transcribe more slowly. ...
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HSF1
Heat shock factor 1 (HSF1) is a protein that in humans is encoded by the ''HSF1'' gene. HSF1 is highly conserved in eukaryotes and is the primary mediator of transcriptional responses to proteotoxic stress with important roles in non-stress regulation such as development and metabolism. Structure Human HSF1 consists of several domains which regulate its binding and activity. DNA-Binding Domain (DBD) This N-terminal domain of approximately 100 amino acids is the most highly conserved region in the HSF protein family and consists of a helix-turn-helix loop. The DBD of each HSF1 monomer recognizes the sequence nGAAn on target DNA. Repeated sequences of the nGAAn pentamer constitute heat shock elements (HSEs) for active HSF1 trimers to bind. Oligomerization Domain (Leucine Zipper Domains) The two regions responsible for oligomerization between HSF1 monomers are leucine zipper (LZ) domains 1-3 and 4 (these regions are also commonly referred to as HR-A/B and HR-C). LZ1-3 is s ...
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