Chaperonin 60. Medical search

A group II chaperonin found in eukaryotic CYTOSOL. It is comprised of eight subunits with each subunit encoded by a separate gene. This chaperonin is named after one of its subunits which is a T-COMPLEX REGION-encoded polypeptide.

A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was originally studied in BACTERIA where it is commonly referred to as GroES protein.

A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.

A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.

A subcategory of chaperonins found in ARCHAEA and the CYTOSOL of eukaryotic cells. Group II chaperonins form a barrel-shaped macromolecular structure that is distinct from GROUP I CHAPERONINS in that it does not utilize a separate lid like structure to enclose proteins.

A 20 cM region of mouse chromosome 17 that is represented by a least two HAPLOTYPES. One of the haplotypes is referred to as the t-haplotype and contains an unusual array of mutations that affect embryonic development and male fertility. The t-haplotype is maintained in the gene pool by the presence of unusual features that prevent its recombination.

An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC 2.8.1.1.

Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.

Group II chaperonins found in species of ARCHAEA.

A subcategory of chaperonins found in MITOCHONDRIA; CHLOROPLASTS; and BACTERIA. Group I chaperonins form into a barrel-shaped macromolecular structure that is enclosed by a separate lid-like protein component.

An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

A group of irregular rod-shaped bacteria that stain gram-positive and do not produce endospores.

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.

Proteins found in any species of archaeon.

Conformational transitions of a protein from unfolded states to a more folded state.

Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.

A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.

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.

A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.

A genus of extremely thermophilic heterotrophic archaea, in the family THERMOCOCCACEAE, occurring in heated sea flows. They are anaerobic chemoorganotropic sulfidogens.

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.

Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.

A genus of aerobic, chemolithotrophic, coccoid ARCHAEA whose organisms are thermoacidophilic. Its cells are highly irregular in shape, often lobed, but occasionally spherical. It has worldwide distribution with organisms isolated from hot acidic soils and water. Sulfur is used as an energy source.

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.

A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains.

Proteins found in any species of bacterium.

The process of cleaving a chemical compound by the addition of a molecule of water.

Cells of the higher organisms, containing a true nucleus bounded by a nuclear membrane.

5'-Adenylic acid, monoanhydride with imidodiphosphoric acid. An analog of ATP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It is a potent competitive inhibitor of soluble and membrane-bound mitochondrial ATPase and also inhibits ATP-dependent reactions of oxidative phosphorylation.

Presence of warmth or heat or a temperature notably higher than an accustomed norm.

Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.

Proteins prepared by recombinant DNA technology.

A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.

An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.

A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.

A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.

The rate dynamics in chemical or physical systems.

The reconstitution of a protein's activity following denaturation.

A genus of anaerobic, chemolithotropic coccoid ARCHAEA, in the family DESULFUROCOCCACEAE. They live in marine environments.

Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.

Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

A set of opposing, nonequilibrium reactions catalyzed by different enzymes which act simultaneously, with at least one of the reactions driven by ATP hydrolysis. The results of the cycle are that ATP energy is depleted, heat is produced and no net substrate-to-product conversion is achieved. Examples of substrate cycling are cycling of gluconeogenesis and glycolysis pathways and cycling of the triglycerides and fatty acid pathways. Rates of substrate cycling may be increased many-fold in association with hypermetabolic states resulting from severe burns, cold exposure, hyperthyroidism, or acute exercise.

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Proteins obtained from ESCHERICHIA COLI.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.

Macromolecular complexes formed from the association of defined protein subunits.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A class of organic compounds which contain an anilino (phenylamino) group linked to a salt or ester of naphthalenesulfonic acid. They are frequently used as fluorescent dyes and sulfhydryl reagents.

A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.

A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules.

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.

Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

A genus of facultatively anaerobic heterotrophic archaea, in the order THERMOPLASMALES, isolated from self-heating coal refuse piles and acid hot springs. They are thermophilic and can grow both with and without sulfur.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)

A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.

Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.

An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

Measurement of the intensity and quality of fluorescence.

An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.

The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.

A family of archaea, in the order DESULFUROCOCCALES, consisting of anaerobic cocci which utilize peptides, proteins or carbohydrates facultatively by sulfur respiration or fermentation. There are eight genera: AEROPYRUM, Desulfurococcus, Ignicoccus, Staphylothermus, Stetteria, Sulfophoboccus, Thermodiscus, and Thermosphaera. (From Bergey's Manual of Systematic Bacteriology, 2d ed)

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. (1/1959)

Both chlamydial and human heat shock protein 60s (HSP 60), which colocalize in human atheroma, may contribute to inflammation during atherogenesis. We tested the hypothesis that chlamydial or human HSP 60 activates human endothelial cells (ECs), smooth muscle cells (SMCs), and monocyte-derived macrophages. We examined the expression of adhesion molecules such as endothelial-leukocyte adhesion molecule-1 (E-selectin), intercellular adhesion molecule-1 (ICAM-1), and vascular cell adhesion molecule-1 (VCAM-1), and the production of the proinflammatory cytokine interleukin-6 (IL-6). We also tested whether either HSP 60 induces nuclear factor-kappaB (NF-kappaB), which contributes to the gene expression of these molecules. Either chlamydial or human HSP 60 induced E-selectin, ICAM-1, and VCAM-1 expression on ECs similar to levels induced by Escherichia coli lipopolysaccharide (LPS). Each HSP 60 also significantly induced IL-6 production by ECs, SMCs, and macrophages to an extent similar to that induced by E. coli LPS, as assessed by enzyme-linked immunosorbent assay (ELISA). In ECs, either HSP 60 triggered activation of NF-kappaB complexes containing p65 and p50 Rel proteins. Heat treatment abolished all these effects, but did not alter the ability of E. coli LPS to induce these functions. Chlamydial and human HSP 60s therefore activate human vascular cell functions relevant to atherogenesis and lesional complications. These findings help to elucidate the mechanisms by which a chronic asymptomatic chlamydial infection might contribute to the pathophysiology of atheroma. (+info)

Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica. (2/1959)

Entamoeba histolytica is a microaerophilic protozoan parasite in which neither mitochondria nor mitochondrion-derived organelles have been previously observed. Recently, a segment of an E. histolytica gene was identified that encoded a protein similar to the mitochondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins after passage through organellar membranes. The possible function and localization of the amebic Hsp60 were explored here. Like Hsp60 of mitochondria, amebic Hsp60 RNA and protein were both strongly induced by incubating parasites at 42 degreesC. 5' and 3' rapid amplifications of cDNA ends were used to obtain the entire E. histolytica hsp60 coding region, which predicted a 536-amino-acid Hsp60. The E. histolytica hsp60 gene protected from heat shock Escherichia coli groEL mutants, demonstrating the chaperonin function of the amebic Hsp60. The E. histolytica Hsp60, which lacked characteristic carboxy-terminal Gly-Met repeats, had a 21-amino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo. This presequence was necessary to target Hsp60 to one (and occasionally two or three) short, cylindrical organelle(s). In contrast, amebic alcohol dehydrogenase 1 and ferredoxin, which are bacteria-like enzymes, were diffusely distributed throughout the cytosol. We suggest that the Hsp60-associated, mitochondrion-derived organelle identified here be named "crypton," as its structure was previously hidden and its function is still cryptic. (+info)

Effect of transforming growth factor beta on experimental Salmonella typhimurium infection in mice. (3/1959)

We have investigated the effect of the in vivo administration of recombinant transforming growth factor beta (rTGF-beta) on the pathogenic mechanisms involved in Salmonella typhimurium experimental infection in mice. The protective response elicited by macrophages was induced by rTGF-beta1 by 2 days after experimental infection, as demonstrated by an increased NO production, while the humoral protective effect began with cytokine mRNA expression 2 days after the challenge and continued after 5 days with cytokine release and lymphocyte activation. We demonstrated that all mice who received rTGF-beta1 survived 7 days after infection. The number of bacteria recovered in the spleens and in the livers of rTGF-beta1-treated mice 2 and 5 days after infection was significantly smaller than that found in the same organs after phosphate-buffered saline (PBS) inoculation. Furthermore, 2 and 5 days after infection, splenic macrophages from rTGF-beta1-treated mice showed a greater NO production than did those from PBS-treated mice. The effect of rTGF-beta1 on S. typhimurium infection in mice was correlated with the expression of cell costimulatory CD28 molecules. Five days after S. typhimurium infection, the percentage of CD28(+)-expressing T cells in splenic lymphocytes from rTGF-beta1-treated mice increased with respect to that from control mice. Gamma interferon (IFN-gamma) mRNA was present in a greater amount in spleen cells from rTGF-beta1-treated mice after 2 days, although the intensity of the band decreased 5 days after the challenge. A similar pattern was obtained with the mRNAs for interleukin-1alpha (IL-1alpha), IL-6, TGF-beta, and inducible nitric oxide synthase, which showed greater expression in cells obtained from rTGF-beta1-treated and S. typhimurium-infected mice 2 days after challenge. The treatment with rTGF-beta1 induced an increase in IL-1alpha and IFN-gamma release in the supernatant of splenocyte cultures 5 days after the experimental infection with S. typhimurium. Moreover, we demonstrated that 5 days after infection, the IFN-gamma titer was significantly greater in the sera of rTGF-beta-treated mice than in those of PBS-treated mice. Also, hsp60 showed greater expression 2 days after the challenge in splenocytes from rTGF-beta1-treated mice. The role played by proinflammatory and immunoregulatory cytokines and by CD28 is discussed. (+info)

Conformational changes generated in GroEL during ATP hydrolysis as seen by time-resolved infrared spectroscopy. (4/1959)

Changes in the vibrational spectrum of the chaperonin GroEL in the presence of ADP and ATP have been followed as a function of time using rapid scan Fourier transform infrared spectroscopy. The interaction of nucleotides with GroEL was triggered by the photochemical release of the ligands from their corresponding biologically inactive precursors (caged nucleotides; P3-1-(2-nitro)phenylethyl nucleotide). Binding of either ADP or ATP induced the appearance of small differential signals in the amide I band of the protein, sensitive to protein secondary structure, suggesting a subtle and localized change in protein conformation. Moreover, conformational changes associated with ATP hydrolysis were detected that differed markedly from those observed upon nucleotide binding. Both, high-amplitude absorbance changes and difference bands attributable to modifications in the interaction between oppositely charged residues were observed during ATP hydrolysis. Once this process had occurred, the protein relaxed to an ADP-like conformation. Our results suggest that the secondary structure as well as salt bridges of GroEL are modified during ATP hydrolysis, as compared with the ATP and ADP bound protein states. (+info)

Enhanced fatty streak formation in C57BL/6J mice by immunization with heat shock protein-65. (5/1959)

Recent data suggest that the immune system is involved in atherogenesis. Thus, interest has been raised as to the possible antigens that could serve as the initiators of the immune reaction. In the current work, we studied the effects of immunization with recombinant heat shock protein-65 (HSP-65) and HSP-65-rich Mycobacterium tuberculosis (MT) on early atherogenesis in C57BL/6J mice fed either a normal chow diet or a high-cholesterol diet (HCD). A rapid, cellular immune response to HSP-65 was evident in mice immunized with HSP-65 or with MT but not in the animals immunized with phosphate-buffered saline (PBS) alone. Early atherosclerosis was significantly enhanced in HCD-fed mice immunized with HSP-65 (n=10; mean aortic lesion size, 45 417+/-9258 microm2) or MT (n=15; 66 350+/-6850 microm2) compared with PBS-injected (n=10; 10 028+/-3599 microm2) or nonimmunized (n=10; 9500+/-2120 microm2) mice. No fatty streak lesions were observed in mice fed a chow diet regardless of the immunization protocol applied. Immunohistochemical analysis of atherosclerotic lesions from the HSP-65- and MT-immunized mice revealed infiltration of CD4 lymphocytes compared with the relatively lymphocyte-poor lesions in the PBS-treated or nonimmunized mice. Direct immunofluorescence analysis of lesions from HSP-65- and MT-immunized mice fed an HCD exhibited extensive deposits of immunoglobulins compared with the fatty streaks in the other study groups, consistent with the larger and more advanced lesions found in the former 2 groups. This model, which supports the involvement of HSP-65 in atherogenesis, furnishes a valuable tool to study the role of the immune system in atherogenesis. (+info)

Physiological states of individual Salmonella typhimurium cells monitored by in situ reverse transcription-PCR. (6/1959)

The possibility of using levels of specific mRNAs in individual bacteria as indicators of single-cell physiology was investigated. Estimates of the numbers of groEL and tsf mRNAs per cell in Salmonella typhimurium cells in different physiological states were obtained by Northern analysis. The average number of groEL mRNAs per cell was estimated to be 22 in fast-growing cultures and 197 in heat-shocked cultures. The average number of tsf mRNAs per cell was estimated to be 37 in fast-growing cultures, 4 in slow-growing cultures, and 0 in nongrowing cultures. The potential of mRNA-targeted in situ reverse transcription (RT)-PCR to monitor quantitatively different levels of groEL and tsf mRNA in individual cells and thus monitor both specific gene induction and general growth activity was assessed. Neither groEL nor tsf mRNA was present in stationary-phase cells, but it was shown that stationary-phase cells contain other RNA species at high levels, which may provide a possibility for monitoring directly stationary-phase individual cells by the use of in situ RT-PCR. The outcome of the in situ RT-PCR analyses indicated that a population of fast-growing cells is heterogeneous with respect to groEL mRNA single-cell contents, suggesting a cell-cycle-controlled expression of groEL in S. typhimurium, whereas a fast-growing culture is homogeneous with respect to tsf mRNA single-cell contents, suggesting that the level of tsf mRNA is relatively constant during the cell cycle. (+info)

Molecular chaperones: pathways and networks. (7/1959)

Some proteins synthesized by growing eukaryotic cells are transferred along unidirectional pathways of molecular chaperones until the risk of aggregation has decreased and they can be released safely. Mature proteins denatured by stress may instead be handled by chaperones acting in branched, reversible networks. (+info)

Identification of Mycobacterium kansasii by using a DNA probe (AccuProbe) and molecular techniques. (8/1959)

The newly formulated Mycobacterium kansasii AccuProbe was evaluated, and the results obtained with the new version were compared to the results obtained with the old version of this test by using 116 M. kansasii strains, 1 Mycobacterium gastri strain, and 19 strains of several mycobacterial species. The sensitivity of this new formulation was 97.4% and the specificity was 100%. Still, three M. kansasii strains were missed by this probe. To evaluate the variability within the species, genetic analyses of the hsp65 gene, the spacer sequence between the 16S and 23S rRNA genes, and the 16S rRNA gene of several M. kansasii AccuProbe-positive strains as well as all AccuProbe-negative strains were performed. Genetic analyses of the one M. gastri strain from the comparative assay and of two further M. gastri strains were included because of the identity of the 16S rRNA gene in M. gastri to that in M. kansasii. The data confirmed the genetic heterogeneity of M. kansasii. Furthermore, a subspecies with an unpublished hsp65 restriction pattern and spacer sequence was described. The genetic data indicate that all M. kansasii strains missed by the AccuProbe test belong to one subspecies, the newly described subspecies VI, as determined by the hsp65 restriction pattern and the spacer sequence. Since the M. kansasii strains that are missed are rare and all M. gastri strains are correctly negative, the new formulated AccuProbe provides a useful tool for the identification of M. kansasii. (+info)

The impaired chaperonin 60 activity leads to impaired mitochondrial quality control. Two genes DDHD1 and CYP2U1 have shown ... Two mitochondrial resident proteins are mutated in HSP: paraplegin and chaperonin 60. Paraplegin is a m-AAA metalloprotease of ... Symptoms of HSP may begin at any age, from infancy to older than 60 years. If symptoms begin during the teenage years or later ... 60 (8): 1045-1049. doi:10.1001/archneur.60.8.1045. PMID 12925358. Harding AE (1981). "Hereditary "pure" spastic paraplegia: a ...

https://en.wikipedia.org/wiki/Hereditary_spastic_paraplegia

In view of the fact that chaperonin Ssocpn (920 kDa), which includes ATP, K+ and Mg2 + but has not produced any additional ... An active aminopeptidase associated with the chaperonin of Solfobulus solfataricus MT4 was described. Sommaruga et al.(2014) ... Cerchia, Laura (7 August 1999). "An archaeal chaperonin-based reactor for renaturation of denatured proteins. Extremophile". ... 299 (2): 255-60. doi:10.1111/j.1574-6968.2009.01759.x. PMID 19735462. Zillig W, Stetter KO, Wunderl S, Schulz W, Priess H, ...

https://en.wikipedia.org/wiki/Sulfolobus_solfataricus

1998). "Streptococcus iniae, a human and animal pathogen: specific identification by the chaperonin 60 gene identification ...

https://en.wikipedia.org/wiki/Streptococcus_iniae

Using the chaperonin 60 gene (Cpn60), specific species of DNA sequencing can be distinguished in the ~600-bp region. It is ... Species and Phenotypically Similar Lactococcus and Vagococcus Species by Reverse Checkerboard Hybridization to Chaperonin 60 ... species and phenotypically similar Lactococcus and Vagococcus species by reverse checkerboard hybridization to chaperonin 60 ... nor does it survive heating at 60 degrees Celsius for 30 minutes. It is nonpigmented. E. malodoratus does not produce ...

https://en.wikipedia.org/wiki/Enterococcus_malodoratus

Species and Phenotypically Similar Lactococcus and Vagococcus Species by Reverse Checkerboard Hybridization to Chaperonin 60 ...

https://en.wikipedia.org/wiki/Enterococcus_pseudoavium

Binding of GroES to the open cavity of the chaperonin induces the individual subunits of the chaperonin to rotate such that the ... this is not the case with chaperonins". It has been found that many anti-chaperonin antibodies exist and are associated with ... Chaperonin 10 aids HSP60 in folding by acting as a dome-like cover on the ATP active form of HSP60. This causes the central ... In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains ...

https://en.wikipedia.org/wiki/GroEL

The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL. GroES exists as a ring- ... Heat shock 10 kDa protein 1 (Hsp10), also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF), is a protein that in ... "Entrez Gene: HSPE1 heat shock 10kDa protein 1 (chaperonin 10)". Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT ... Lee KH, Kim HS, Jeong HS, Lee YS (October 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial ...

https://en.wikipedia.org/wiki/GroES

The original chaperonin is proposed to have evolved from a peroxiredoxin. Group I chaperonins (Cpn60) are found in bacteria as ... In archaea, the chaperonin is called the thermosome. In eukarya, the cytoplasmic chaperonin is called CCT (also called TRiC). ... The active chaperonin role is in turn involved with specific chaperonin-substrate interactions that may be coupled to ... The GroEL/GroES complex in E. coli is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex. GroEL ...

https://en.wikipedia.org/wiki/Chaperonin

July 2013). "The H/D-exchange kinetics of the Escherichia coli co-chaperonin GroES studied by 2D NMR and DMSO-quenched exchange ... 425 (14): 2541-60. doi:10.1016/j.jmb.2013.04.008. PMID 23583779. Stewart JH, Shapiro RH, DePuy CH, Bierbaum VH (1977). " ...

https://en.wikipedia.org/wiki/Hydrogen–deuterium_exchange

CCT is a group II chaperonin, a large protein complex that assists in the folding of other proteins. CCT is formed of a double ... After AMP-PNP is bound to CCT the substrates move within the chaperonin's cavity. It also seems that in the case of actin, the ... The actin is recognized, loaded, and delivered to the cytosolic chaperonin (CCT) in an open conformation by the inner end of ... Brackley KI, Grantham J (Jan 2009). "Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle ...

https://en.wikipedia.org/wiki/Actin

"Entrez Gene: CCT6A chaperonin containing TCP1, subunit 6A (zeta 1)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, ... Segel GB, Boal TR, Cardillo TS, Murant FG, Lichtman MA, Sherman F (August 1992). "Isolation of a gene encoding a chaperonin- ... Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a ... a subunit of the eukaryotic TRiC chaperonin from humans and yeast". J Biol Chem. 269 (28): 18616-22. doi:10.1016/S0021-9258(17) ...

https://en.wikipedia.org/wiki/CCT6A

This gene encodes chaperonin cofactor A. GRCh38: Ensembl release 89: ENSG00000171530 - Ensembl, May 2017 GRCm38: Ensembl ... "Entrez Gene: TBCA tubulin folding cofactor A". Lewis SA, Tian G, Vainberg IE, Cowan NJ (1996). "Chaperonin-mediated folding of ... 10 (10): 1546-60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. Guasch A, Aloria K, Pérez R, et al. (2002). "Three- ...

https://en.wikipedia.org/wiki/TBCA

Trent JD, Kagawa HK, Yaoi T, Olle E, Zaluzec NJ (May 1997). "Chaperonin filaments: the archaeal cytoskeleton?". Proceedings of ... 148 (1): 352-60. doi:10.1128/JB.148.1.352-360.1981. PMC 216199. PMID 7287626. "Archaea Basic Biology". March 2018. Chow C, ... Bibcode:2005JMolE..60..174M. doi:10.1007/s00239-004-0046-3. PMID 15791728. S2CID 27481111. Makarova KS, Grishin NV, Shabalina ... 29 (2-3): 151-60. doi:10.1016/0303-2647(93)90091-P. PMID 8374067. Golyshina OV, Pivovarova TA, Karavaiko GI, Kondratéva TF, ...

https://en.wikipedia.org/wiki/Archaea

Despite only 11% of sequence similarity, MSP and the N-terminus of the bacterial P-pilus associated chaperonin PapD share a ... They all have more than 60% sequence identity. Proteins with limited sequence similarity were identified in species from plants ...

https://en.wikipedia.org/wiki/Major_sperm_protein

They and others found early on that a chaperonin-mediated folding reaction can be reconstituted in a test tube, and that has ... His research into protein folding uncovered the action of chaperonins, protein complexes that assist the folding of other ... Art Horwich Lab at Yale Interview with Arthur Horwich Chaperonin-Mediated Protein Folding Arthur Horwich Seminars: "Chaperone- ... Such assemblies, known as chaperonins, also exist in other cellular compartments and are essential components, mediating ...

https://en.wikipedia.org/wiki/Arthur_L._Horwich

Kelson TL, Ohura T, Kraus JP (March 1996). "Chaperonin-mediated assembly of wild-type and mutant subunits of human propionyl- ... a. Carbamazepine (antiepileptic drug): significantly lowers enzyme levels in the liver b. E. coli chaperonin proteins groES and ... 255 (1): 60-65. doi:10.1016/S0021-9258(19)86263-4. PMID 6765947. Diacovich L, Mitchell DL, Pham H, Gago G, Melgar MM, Khosla C ...

https://en.wikipedia.org/wiki/Propionyl-CoA_carboxylase

Bakthavatsalam D, Soung RH, Tweardy DJ, Chiu W, Dixon RA, Woodside DG (Jun 2014). "Chaperonin-containing TCP-1 complex directly ... Roobol A, Holmes FE, Hayes NV, Baines AJ, Carden MJ (1995). "Cytoplasmic chaperonin complexes enter neurites developing in ... "Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta ... "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Curr. Biol. 4 (2): ...

https://en.wikipedia.org/wiki/T-complex_1

Group 2 chaperonins are found in both the cytosol of eukaryotic cells as well as in archaea. Group 2 chaperonins also contain ... Chaperonins are divided into two groups. Group 1 chaperonins are commonly found in bacteria, chloroplasts, and mitochondria. ... All chaperonins exhibit two states (open and closed), between which they can cycle. This cycling process is important during ... Chaperonins are a special class of chaperones that promote native state folding by cyclically encapsulating the peptide chain. ...

https://en.wikipedia.org/wiki/Proteostasis

4 Chaperone Chaperonin Heat shock protein The term "TCP-1" is variously expanded as "T-complex protein 1" and "tailless complex ... T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), is a multiprotein complex and the ... Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that ... "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM". Nature ...

https://en.wikipedia.org/wiki/TRiC_(complex)

Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a ... Suppl 1: 355-60. PMID 8098743. Lopez-Fanarraga M, Avila J, Guasch A, et al. (2002). "Review: postchaperonin tubulin folding ... 150 (2): 349-60. doi:10.1083/jcb.150.2.349. PMC 2180222. PMID 10908577. Takeoka A, Shimizu M, Horio T (2001). "Identification ...

https://en.wikipedia.org/wiki/TUBA1B

1998). "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin". Cell. 93 (5): 863-73. doi:10.1016/ ... 10 (10): 1546-60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. Strausberg RL, Feingold EA, Grouse LH, et al. (2003). " ...

https://en.wikipedia.org/wiki/PFDN2

... chaperonins Chaperonins are characterized by their barrel-shaped structure with binding sites for client proteins inside the ... Human HPS90AB1 shares 60% overall homology to its closest relative HSP90AA1. Murine HSP90AB1 was cloned in 1987 based on ...

https://en.wikipedia.org/wiki/HSP90AB1

Biological machines Chaperome Chaperonin Chemical chaperones Heat shock protein Heat shock factor 1 Molecular chaperone therapy ... The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are ... Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Quarterly Reviews of ... Martin J, Hartl FU (February 1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proceedings ...

https://en.wikipedia.org/wiki/Chaperone_(protein)

Other examples of protein cages are clathrin cages, viral envelopes, chaperonins, and the iron storage protein ferritin. There ... Buckminsterfullerene (C60) and the 60 atoms of this molecule are arranged in a cage-like structure and the framework resembles ...

https://en.wikipedia.org/wiki/Macromolecular_cages

Methanococcus maripaludis chaperonin, reconstructed to 0.43 nanometer resolution. This bacterial protein complex is a machine ... January 2010). "Mechanism of folding chamber closure in a group II chaperonin". Nature. 463 (7279): 379-83. Bibcode:2010Natur. ... An area of the specimen is imaged at both zero and at high angle (~60-70 degrees) tilts, or in the case of the related method ...

https://en.wikipedia.org/wiki/Single_particle_analysis

Like GroES, gp31 forms a stable complex with GroEL chaperonin that is absolutely necessary for the folding and assembly in vivo ... The icosahedron consists of 20 triangular faces delimited by 12 fivefold vertexes and consists of 60 asymmetric units. Thus, an ... turning 60 degrees counterclockwise, then taking k steps to get to the next pentamer. The triangulation number T for the capsid ...

https://en.wikipedia.org/wiki/Capsid

"Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles". Nature. 423 (6940): 628-632. ... ATP-responsive nanotubular carriers composed of chaperonin proteins, a biomolecular machine (4) non-crosslinked photoactuators ... 60 (1-2): 33-47. doi:10.1002/ijch.201900165. ISSN 1869-5868. Hashim, P. K.; Bergueiro, Julian; Meijer, E. W.; Aida, Takuzo ( ...

https://en.wikipedia.org/wiki/Takuzo_Aida

Lee KH, Kim HS, Jeong HS, Lee YS (Oct 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial ... typically occur within 30-60 minutes of ingesting alcoholic beverages; and c) occur in other Asian as well as non-Asian ...

https://en.wikipedia.org/wiki/ALDH2

The technologies of introducing genes of mammalian chaperonins into the yeast genome and overexpressing existing chaperonins ... As some proteins require chaperonin for proper folding, Pichia is unable to produce a number of proteins, since P. pastoris ... 45: 52-60. doi:10.1016/j.biologicals.2016.09.015. PMID 27810255. Ali Razaghi; Roger Huerlimann; Leigh Owens; Kirsten Heimann ( ...

https://en.wikipedia.org/wiki/Pichia_pastoris

Like GroES, gp31 forms a stable complex with GroEL chaperonin that is absolutely necessary for the folding and assembly in vivo ... 59: 631-60. doi:10.1146/annurev.bi.59.070190.003215. PMID 2197986. Jackson SE (1998). "How do small single-domain proteins fold ...

https://en.wikipedia.org/wiki/Protein_folding

... metal ion-induced 1D assembly of a molecularly engineered chaperonin". Journal of the American Chemical Society. 131 (22): 7556 ... 60 (1-2): 33-47. doi:10.1002/ijch.201900165. ISSN 0021-2148. Hashim PK, Bergueiro J, Meijer EW, Aida T (2020-06-01). " ...

https://en.wikipedia.org/wiki/Supramolecular_polymer

Xu Z, Horwich AL, Sigler PB (August 1997). "The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex". ... Yeast Hsp90 is 60% identical to human Hsp90α. In mammalian cells, there are two or more genes encoding cytosolic Hsp90 ...

https://en.wikipedia.org/wiki/Hsp90

Biology portal Cellular stress response Chaperone Chaperonin Co-chaperone FourU thermometer Hsp90 cis-regulatory element ROSE ... refer to families of heat shock proteins on the order of 60, 70 and 90 kilodaltons in size, respectively. The small 8- ...

https://en.wikipedia.org/wiki/Heat_shock_protein

... PLoS ...

https://pubmed.ncbi.nlm.nih.gov/23189159/

SWISS-MODEL Template Library (SMTL) entry for 1gr5.1. Solution Structure of apo GroEL by Cryo-Electron microscopy

https://swissmodel.expasy.org/templates/1gr5

The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms. Frontiers in Molecular Biosciences. 2018 May 15;5: ... The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms. Pierce T. ONeil, Alexandra J. Machen, Benjamin C. ... The Chaperonin GroEL : A Versatile Tool for Applied Biotechnology Platforms. In: Frontiers in Molecular Biosciences. 2018 ; Vol ... The nucleotide-free chaperonin GroEL is capable of capturing transient unfolded or partially unfolded states that flicker in ...

https://mayoclinic.pure.elsevier.com/en/publications/the-chaperonin-groel-a-versatile-tool-for-applied-biotechnology-p

... acetonitrile for 60 min. All gradients were performed using the Ultimate 3000 system (Thermo Scientific, Waltham, MA, USA) ...

https://www.mdpi.com/2073-4425/12/5/770/htm

Streptococcus suis serotypes characterized by analysis of chaperonin 60 gene sequences. Appl Environ Microbiol. 2001;67:4828-33 ...

https://wwwnc.cdc.gov/eid/article/20/3/13-1148_article

Chaperonin 60 beta Protein folding FBP aldolase1 Photosynthesis FBP aldolase 2 Photosynthesis ...

https://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-15-320/tables/3

chaperonin60: Further proof? Good grief! Look, heres my point. The Iraq invasion was justified by manufacturing a bogus link ...

https://oracknows.blogspot.com/2005/07/to-my-british-readers.html?showComment=1120813500000

10 kDa chaperonin. 10. SEQF1643,CP001173.1. SEQF1643_00015 jb [NA] [AA] 1680/559. 9684-11363. DNA primase. ... 183/60. 68335-68517. hypothetical protein. 65. SEQF1643,CP001173.1. SEQF1643_00071 jb [NA] [AA] 189/62. 68656-68844. ... 60 kDa chaperonin. 9. SEQF1643,CP001173.1. SEQF1643_00014 jb [NA] [AA] 357/118. 9398-9042. ... 60. SEQF1643,CP001173.1. SEQF1643_00066 jb [NA] [AA] 1863/620. 65056-66918. hypothetical protein. ...

https://homd.org/genome/explorer?gid=SEQF1643&anno=prokka

10 kDa chaperonin. 26. SEQF3527,NSLZ01000010.1. SEQF3527_00028 jb [NA] [AA] 1626/541. 27501-29126. 60 kDa chaperonin. ... 60. SEQF3527,NSLZ01000010.1. SEQF3527_00063 jb [NA] [AA] 336/111. 65226-64891. hypothetical protein. ...

https://www.homd.org/genome/explorer?gid=SEQF3527&anno=prokka

keywords = "Chaperonin 60, Chaperonin 10, Molecular Chaperones, HSP70 Heat-Shock Proteins, Protein Binding, Protein ...

https://research.birmingham.ac.uk/en/publications/the-roles-of-molecular-chaperones-in-vivo

D3.383.663.283.266.450.221 Chaperonin 60 D12.644.276.87.185 D12.776.467.87.438 D23.529.87.488 Chaplaincy Service, Hospital ... G2.149.60 Ajuga B1.650.940.800.575.100.575.51 B1.650.940.800.575.100.583.520.51 AKR murine leukemia virus B4.909.574.807. ... B4.970.60 (Replaced for 2015 by Anelloviridae) Anesthesia Department, Hospital N2.278.354.422.70 N2.278.216.500.968.70 Angina ... D12.644.822.750.60 D12.776.645.750.60 Antitoxins D12.776.124.486.485.114.301 D12.776.124.790.651.114.573.601 D12.776.124.790. ...

https://decs.bvs.br/P/mnchg2016.txt

Aizu, E., Yamamoto, S. & Kato, R., 1992 1月, In: The Japanese Journal of Pharmacology. 60, 1, p. 9-17 9 p.. 研究成果: Article › 査読 ... Suzuki, T., Nonaka, H., Fujimoto, K. & Kawashima, K., 1993 6月, In: Journal of Neurochemistry. 60, 6, p. 2285-2289 5 p.. 研究成果: ...

https://keio.pure.elsevier.com/ja/organisations/1b00-faculty-of-pharmacy/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&ordering=publicationYearThenTitle&descending=false&page=5

Sato, Y., Notohara, K., Kojima, M., Takata, K., Masaki, Y. & Yoshino, T., Apr 2010, In: Pathology International. 60, 4, p. 247- ... The Japanese journal of clinical pathology. 60, 2, p. 174-179 6 p.. Research output: Contribution to journal › Review article ...

https://okayama.pure.elsevier.com/en/organisations/graduate-school-of-health-sciences/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Fsystematicreview

Dive into the research topics of Microbial carriage state of peripheral blood dendritic cells (DCs) in chronic periodontitis influences DC differentiation, atherogenic potential. Together they form a unique fingerprint. ...

https://augusta.pure.elsevier.com/en/publications/microbial-carriage-state-of-peripheral-blood-dendritic-cells-dcs-/fingerprints/

60 kDa chaperonin (Protein Cpn60) (groEL protein). 9e-5. At5g18820. EMB3007 (embryo defective 3007). O.I.. C.G.. H.G.. Please ...

http://webs2.kazusa.or.jp/kagiana/cgi-bin/xp2g.cgi?gsm=GSM207564&organism=osa

","10 kDa chaperonin [Ensembl]. Chaperonin 10 Kd subunit [Interproscan].","protein_coding" "AKP15240","groL","Neisseria ... TCP-1/cpn60 chaperonin family [Interproscan].","protein_coding" "AKP15296","glyS","Neisseria gonorrhoeae","Glycine--tRNA ligase ... ","33 kDa chaperonin [Ensembl]. Hsp33 protein [Interproscan].","protein_coding" "AKP14769","WX61_00696","Neisseria gonorrhoeae ...

https://bacteria.sbs.ntu.edu.sg/go/sequences/table/7203

... chaperonin GroEL, mitochondrial chaperonin, heat shock protein family D member 1, HSPD1, hspd1.S, hspd1, LOC100414401, Hspd1, ... HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1)) Reaktivität Alle Reaktivitäten für HSPD1 ELISA Kits * Human 5 ... Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) ELISA Kit HSPD1 Reaktivität: Human Colorimetric Sandwich ELISA 2.5-80 ng/mL ... Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) ELISA Kit HSPD1 Reaktivität: Maus Colorimetric Competition ELISA 0.5-10 ng/mL ...

https://www.antikoerper-online.de/kit/628283/Heat+Shock+60kDa+Protein+1+Chaperonin+HSPD1+ELISA+Kit/