Chaperonin Containing TCP-1
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.
Group II Chaperonins
t-Complex Genome Region
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.
Group I Chaperonins
Gram-Positive Asporogenous Rods, Irregular
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).
Molecular Sequence Data
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.
Amino Acid Sequence
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.
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.
Sequence Homology, Amino Acid
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 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.
Electrophoresis, Polyacrylamide Gel
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.
Protein Structure, Tertiary
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.
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.
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)
HSP70 Heat-Shock Proteins
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 184.108.40.206.) EC 220.127.116.11.
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 18.104.22.168.
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)
Protein Structure, Secondary
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 human heat-shock protein family: expression of a novel heat-inducible HSP70 (HSP70B) and isolation of its cDNA and genomic...
The human heat-shock protein multigene family comprises several highly conserved proteins with structural and functional properties in common, but which vary in the extent of their inducibility in response to metabolic stress. We have isolated and characterized a novel human HSP70 cDNA, HSP70B cDNA, and its corresponding gene sequence. HSP70B cDNA hybrid-selected an mRNA encoding a more basic 70 kDa heat-shock protein than both the major stress-inducible HSP70 and constitutively expressed HSC70 heat-shock proteins, which in common with other heat-shock 70 kDa proteins bound ATP. The complete HSP70B gene was sequenced and, like the major inducible HSP70 gene, is devoid of introns. The HSP70B gene has 77% sequence similarity to the HSP70 gene and 70% similarity to HSC70 cDNA, with greatest sequence divergence towards the 3-terminus. The HSP70B gene represents a functional gene, as indicated by Northern-blot analysis with specific oligonucleotides, hybrid-selected translation with a specific ...
Bacterial heat shock protein GroEL (Hsp64) exerts immunoregulatory effects on T cells by utilizing apoptosis
Aggregatibacter actinomycetemcomitans (Aa) expresses a 64-kDa GroEL protein belonging to the heat shock family of proteins. This protein has been shown to influence human host cells, but the apoptotic capacity of the GroEL protein regarding T cells is not yet known. The purpose of this study was to investigate the ability of A. actinomycetemcomitans GroEL (AaGroEL) protein to induce human peripheral blood T-cell apoptosis. Endogenous, purified AaGroEL protein was used as an antigen. In AaGroEL-treated T cells, the data indicated that phosphatidylserine exposure, an early apoptotic event, was dose- and time-dependent. The AaGroEL-treated T cells were also positive for active caspase-3 in a dose-dependent manner. The rate of AaGroEL-induced apoptosis was suppressed by the addition of the general caspase inhibitor Z-VAD-FMK. Furthermore, cleaved caspase-8 bands (40/36 kDa and 23 kDa) were identified in cells responding to AaGroEL. DNA fragmentation was also detected in the AaGroEL-treated T cells. ...
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Antibody Response to Chlamydial Heat Shock Protein 60 Is Strongly Associated With Acute Coronary Syndromes | Circulation
Seropositivity to Cp-HSP60 was detected in 217 (99%) of 219 patients with ACS but in only 8 (20%) of 40 patients with SA and in none of the control subjects (P=0.0001, ACS patients versus control subjects; P=0.003, ACS patients versus SA patients; and P=0.05, SA patients versus control subjects). Seropositivity to Cp was detected in 67%, 60%, and 30% of ACS patients, SA patients, and control subjects, respectively (P=0.001, ACS and SA patients versus control subjects). Elevated hs-CRP was found in 60% of ACS patients versus 25% of SA patients and 8% of control subjects (P,0.001, ACS patients versus SA patients and control subjects). Considering the cutoff level of 0.40, Cp-HSP60 IgG antibody levels had 99% specificity and 94% sensitivity for ACS. No differences in anti-Cp-HSP60 or in anti-Cp IgG antibody titers and prevalence of seropositivity were observed between AMI and UA patients (Table) or, in patients with UA, between those with (n=65) and those without (n=114) raised TnT levels. ...
Recombinant Human Heat Shock Protein β-7/HSPB7 (C-6His) | Bon Opus Biosciences
Recombinant Human Heat shock protein beta-7 is produced by our E.coli expression system and the target gene encoding Met1-Ile170 is expressed with a 6His tag at the C-terminus. Bon Opus Cat. #CG80
Recombinant Human Hsp90 alpha protein (ab191952) | Abcam
Buy our Recombinant Human Hsp90 alpha protein. Ab191952 is a protein fragment produced in Escherichia coli and has been validated in SDS-PAGE. Abcam provides…
Recombinant Human Hsp90 beta protein (ab80353) | Abcam
Buy our Recombinant Human Hsp90 beta protein. Ab80353 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE. Abcam provides…
Sequence Similarity - 1SS8: GroEL Sequence Similarity Report Page
1SS8: Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Using chemical genetics to explore GroEL function - University of Arizona
The chaperonin GroEL in the bacterial cytoplasm has been shown to assist polypeptide chain folding but to date, a strain severely conditionally deficient in GroEL has not been available. Such a strain would allow one to address such questions as: do GroEL-deficient cells continue to translate polypeptides? How many and which polypeptides become misfolded/aggregated under such conditions? Are inclusion bodies formed? Are other chaperones induced? Here we propose to attack this problem by producing a chemical inhibitor that will cross E. coli membranes and immediately shut off the ATPase of a mutationally sensitized GroEL, blocking chaperonin action. Based on molecular modeling studies, we have selected two residues in the ATP pocket, Asn479 and Ile493, to mutate to smaller residues, alanine and glycine, to create a hydrophobic pocket potentially capable of binding one or more of a chemically synthesized series of adenine analogues with large, hydrophobic groups attached at various positions. The ...
Chaperonin overproduction and metabolic erosion caused by mutation accumulation in Escherichia coli - Zurich Open Repository...
Bacterial cells adapting to a constant environment tend to accumulate mutations in portions of their genome that are not maintained by selection. This process has been observed in bacteria evolving under strong genetic drift, and especially in bacterial endosymbionts of insects. Here, we study this process in hypermutable Escherichia coli populations evolved through 250 single-cell bottlenecks on solid rich medium in a mutation accumulation experiment that emulates the evolution of bacterial endosymbionts. Using phenotype microarrays monitoring metabolic activity in 95 environments distinguished by their carbon sources, we observe how mutation accumulation has decreased the ability of cells to metabolize most carbon sources. We study if the chaperonin GroEL, which is naturally overproduced in bacterial endosymbionts, can ameliorate the process of metabolic erosion, because of its known ability to buffer destabilizing mutations in metabolic enzymes. Our results indicate that GroEL can slow down ...
JCI - Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages
Reagents. The recombinant Chlamydia trachomatis HSP 60 fusion protein expression plasmid was the gift of R. Stephens (University of California-San Francisco, San Francisco, California, USA) (24). Production of chlamydial HSP 60, purification, and site-specific proteolysis with thrombin were performed as described elsewhere (25) using a RediPack GST Purification Module (Pharmacia Biotech, Piscataway, New Jersey, USA). Recombinant human HSP 60 was purchased from StressGen Biotechnologies Corp. (Victoria, British Columbia, Canada). E. coli lipopolysaccharide (LPS) was purchased from Sigma Chemical Co. (St. Louis, Missouri, USA). Formalin-inactivated C. pneumoniae elementary bodies were obtained from Washington Research Foundation (Seattle, Washington, USA).. Cell isolation and culture. Human vascular ECs from human umbilical cord and SMCs from saphenous veins were isolated and cultured as described (26, 27). Vascular SMCs and ECs were cultured in DMEM and M199 medium (BioWhittaker, Walkersville, ...
RCSB PDB - 1SS8: GroEL Macromolecules Report Page
1SS8: Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Hspe1 (untagged) - Mouse heat shock protein 1 (chaperonin 10) (Hspe1), nuclear gene encoding mitochondrial protein, (10ug) -...
Hspe1 (untagged) - Mouse heat shock protein 1 (chaperonin 10) (Hspe1), nuclear gene encoding mitochondrial protein, (10ug), 10 µg.
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Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) ELISA Kits
Reaktivität: Huhn, Rind (Kuh), Hund and more. 79 verschiedene HSPD1 ELISA Kits vergleichen. Alle direkt auf antikoerper-online.de bestellbar!
GroEL Protein Human Recombinant | HSPD1 Antigen | ProSpec
GROEL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 572 aa (27-573 a.a.) and having a molecular mass of 60kDa.
Hspd1 - 60 kDa heat shock protein, mitochondrial - Mus musculus (Mouse) - Hspd1 gene & protein
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Page:Climatic Cycles and Tree-Growth - 1919.djvu/25 - Wikisource, the free online library
doubles mentioned above are plotted, together with a selected list of 6 small singles particularly deficient in red tissues. They are, 1904 double once in 10, 1902 double once in 10, 1899 single, 1895 single, 1894 single, and 1880 double once in 10. In these it is evident that drought in the spring stops the growth of the tree. The double ring, therefore, seems to be an intermediate form between the large normal single ring, growing through the warm parts of the year, and the small, deficient ring, ending its growth by midsummer. This occasional failure to benefit by the summer rains probably explains why the Prescott trees do not show an agreement of more than about 70 per cent between growth and rainfall. It suggests also that the Flagstaff trees, which grow under conditions of more rainfall and have very few double rings, give a more accurate record than those of Prescott.. Consistent with this view of the doubling is the condition of the outer ring in the Prescott sections collected by Mr. ...
Recombinant Human Heat Shock 27kDa Protein 1, His-tagged HSPB1-2651H - Creative BioMart
Recombinant Human Hsp27 (amino acids 1-205) was fused to a His·Tag sequence at the N-terminus and expressed inS. frugiperdainsect cells.MW = 27 kDa.
CPn0134 is orthologously related to CT110: residues 1-544 of CPn0134 are 91% similar to residues 1-544 of CT110, a predicted 60 kD chaperonin (protein cpn60, GroEL protein) & (57 kD chlamydial hypersensitivity antigen; HSP60) from C. trachomatis ...
Gribun A, Kimber MS, Ching R, Sprangers R, Fiebig KM & Houry WA (2005) The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J Biol Chem 280, 16185-96. PubMed ...
HSP60 Antibody (GROEL/730) [HRP] (NBP2-34625H): Novus Biologicals
Mouse Monoclonal Anti-HSP60 Antibody (GROEL/730) [HRP]. Mitochondrial Marker. Validated: WB, ELISA, Flow, ICC/IF, IHC-Fr, IHC-P, IP. Tested Reactivity: Human. 100% Guaranteed.
Anti-Hsp70 抗体 [EP1007Y] (ab45133) | アブカム
高い抗原親和性、特異性と安定した品質を兼ね備えたアブカムのウサギ・モノクローナル抗体 RabMAb® ab45133 交差種: Rat,Hu 適用: WB,IHC-P,Flow Cyt,ICC/IF
Anti-Hsp27 抗体 [EP1724Y] (ab62339) | アブカム
高い抗原親和性、特異性と安定した品質を兼ね備えたアブカムのウサギ・モノクローナル抗体 RabMAb® ab62339 交差種: Hu 適用: WB,IHC-P,ICC
The Human Mitochondrial Chaperonin: It Takes Two Single-Rings to Tango by Adrian Sergio Enriquez
The human mitochondrial chaperonin is a macromolecular machine that catalyzes the proper folding and assembly of newly imported mitochondrial proteins into their biologically active state. It is composed of two proteins from the highly conserved heat shock protein family, hsp10 and hsp60, that assemble into large oligomeric complexes responsible for mediating the folding of non-native polypeptides in an ATP dependent manner. In addition to its innate role in protein folding, human mitochondrial hsp60 has been implicated in numerous moonlighting cellular activities that have been linked to diseases conditions such as cancer and neurodegeneracy. In light of its cellular importance, the conditions that propel the human mitochondrial chaperonin through its protein folding mechanism are not well understood. Here I propose a protein folding scheme for the mitochondrial chaperonin based on negative stain electron microscopy 3-D reconstructions. I found that the human mitochondrial chaperonin complex
Identification of Important Amino Acid Residues That Modulate Binding of Escherichia coli GroEL to Its Various Cochaperones |...
GroEL/GroES is the only chaperone machine of E. coli that is absolutely essential for bacterial survival under all laboratory conditions tested (Fayetet al. 1989). GroEL/GroES homologs are found in all organisms except in some Archaea species (Macarioet al. 1999) and the recently sequenced Ureaplasmum urealyticum mycobacterium (Glasset al. 2000). The E. coli GroEL chaperone can function not only with its own GroES cochaperone, but also with bacteriophage-encoded cochaperones, such as the bacteriophage T4-encoded Gp31 cochaperone (van der Vieset al. 1994) or the bacteriophage RB49-encoded CocO cochaperone (Ang et al. 2000, 2001). Apparently, the bacteriophage-encoded cochaperones are uniquely qualified to help in the folding of the major bacteriophage-encoded capsid protein, Gp23 (Laemmliet al. 1970; Georgopouloset al. 1972; van der Vieset al. 1994; Andreadis and Black 1998; Anget al. 2000). Yet, Gp31 and CocO can also help GroEL in its generalized chaperone function, since either can substitute ...
New GroEL-like chaperonin of bacteriophage OBP P. fluorescens suppresses thermal protein aggregation in an ATP-dependent manner...
Recently, we discovered and studied the first virus-encoded chaperonin of bacteriophage EL Pseudomonas aeruginosa, gene product (gp) 146. In the present work, we performed bioinformatics analysis of currently predicted GroEL-like proteins encoded by phage genomes in comparison with cellular and mitochondrial chaperonins. Putative phage chaperonins share a low similarity and do not form a monophyletic group; nevertheless, they are closer to bacterial chaperonins in the phylogenetic tree. Experimental investigation of putative GroEL-like chaperonin proteins has been continued by physicochemical and functional characterization of gp246 encoded by the genome of Pseudomonas fluorescens bacteriophage OBP. Unlike the more usual double-ring architecture of chaperonins, including the EL gp146, the recombinant gp246 produced by E. coli cells has been purified as a single heptameric ring. It possesses an ATPase activity and does not require a co-chaperonin for its functioning. In vitro experiments ...
Interactions of GroEL/GroES with a heterodimeric intermediate during α<sub>2</sub>β<sub>2</sub> assembly of mitochondrial...
TY - JOUR. T1 - Interactions of GroEL/GroES with a heterodimeric intermediate during α2β2 assembly of mitochondrial branched-chain α-ketoacid dehydrogenase. T2 - cis capping of the native-like 86-kDa intermediate by GroES. AU - Song, Jiu Li. AU - Wynn, R. Max. AU - Chuang, David T.. PY - 2000/7/21. Y1 - 2000/7/21. N2 - We showed previously that the interaction of an αβ heterodimeric intermediate with GroEL/GroES is essential for efficient α2β2 assembly of human mitochondrial branched-chain α-ketoacid dehydrogenase. In the present study, we further characterized the mode of interaction between the chaperonins and the native-like αβ heterodimer. The αβ heterodimer, as an intact entity, was found to bind to GroEL at a 1:1 stoichiometry with a K(D) of 1.1 x 10-7 M. The 1:1 molar ratio of the GroEL-αβ complex was confirmed by the ability of the complex to bind a stoichiometric amount of denatured lysozyme in the trans cavity. Surprisingly, in the presence of MgADP, GroES was able to cap ...
Autoimmunity to Human Heat Shock Protein 60, Chlamydia pneumoniae Infection, and Inflammation in Predicting Coronary Risk |...
In the present study, we showed that the presence of an elevated level of IgA antibodies against human Hsp60 protein predicts a coronary event several years before the coronary event actually occurs. Researchers at Wicks laboratory have studied the role of microbial Hsp60 in the development of atherosclerosis. Their studies indicate that immunization with mycobacterial Hsp65 induces atherosclerosis in laboratory animals.3,4⇓ In humans, they have found that immunity to mycobacterial Hsp65 is associated with the pathogenesis of carotid5 and coronary6 atherosclerosis. Hsp65 antibodies were found more often in patients with atherosclerotic lesions than in persons without such lesions,5 and the presence of these antibodies also predicted carotid atherosclerosis.7,8⇓ It has been shown that these antibodies cross-react with E coli Hsp60, chlamydial Hsp60, and human Hsp60 antibodies and are cytotoxic to endothelial cells.9 In the present study, we confirmed these findings and extended them to apply ...
Thomas Ziegelhoffer | Craig Lab | Biochemistry | UW-Madison
Email: [email protected] Tom received his BS degree in Bacteriology from the University of Wisconsin-Madison in 1983. He worked as a research technician at UW-Madison in the lab of Norman Drinkwater (McArdle Laboratory for Cancer Research) until entering graduate school in 1985. He did graduate work in the laboratory of Costa Georgopoulos at the University of Utah in Salt Lake City and was awarded a PhD. degree in 1991. His thesis work focused on the role of E. coli heat shock proteins GroEL and GroES in bacteriophage morphogenesis. He returned to UW-Madison for post-doctoral work in the Craig lab, (supported by a fellowship from the National Institutes of Health), where he primarily studied the biochemistry of the SSA and SSB cytosolic Hsp70 chaperones of S. cerevisiae. In 1995, he became an associate researcher in the Plant Biotechnology Lab at the UW Biotechnology Center. The primary focus of his work at the UWBC was the expression and characterization of microbial enzymes in transgenic ...
GroES - Wikipedia
Heat shock 10 kDa protein 1 (Hsp10) also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF) is a protein that in humans is encoded by the HSPE1 gene. The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL. GroES exists as a ring-shaped oligomer of between six and eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides an isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60. Escherichia coli GroES has also been shown to bind ATP cooperatively, and with an affinity comparable to that of GroEL. Each GroEL subunit ...
Protection against tuberculosis by passive transfer with T-cell clones recognizing mycobacterial heat-shock protein 65. -...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Vaccine Therapy in Treating Patients With Advanced Stage III-IV Melanoma - Full Text View - ClinicalTrials.gov
PRIMARY OBJECTIVES:. I. To estimate the maximum tolerated dose (MTD) and clinically appropriate dose of human heat shock protein (hsp)110-gp100 chaperone complex melanoma vaccine (recombinant hsp110-gp100 chaperone complex vaccine) to recommend a phase II dose in stage IIIB/C and stage IV metastatic melanoma patients.. SECONDARY OBJECTIVES:. I. To examine the effect of the recombinant human hsp110-gp100 chaperone complex vaccine on measurable clinical tumor.. II. To determine gp100 and hsp110 specific cell mediated and humoral immune responses elicited by the chaperone complex vaccine.. III. To determine the effect of dose and serial administration of the chaperone complex vaccine on cell mediated and humoral immune responses.. IV. To quantify patient characteristics (human leukocyte antigen [HLA] subtype, immune cell function, etc.) that may correlate with immune response to the chaperone complex vaccine.. OUTLINE: This is a dose-escalation study.. Patients receive recombinant hsp110-gp100 ...
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Fancy large double ring link sterling silver toggle bracelet.. Marked 925. Weighs 56.6 grams.. Bracelet is about 39.5mm wide, & 8″ flat length.. Excellent estate condition. Gently pre-owned.. ...
Expanding proteins - David Bradley
A new study reveals that the static snapshots recorded in protein crystallography may be missing the bigger picture. Investigations of a bacterial protein using cryomicroscopy shows the protein in a balloon-like mode previously hidden from sold state studies. The discovery suggests that techniques complementary to X-ray crystallography are essential if molecular biology is to gain a complete understanding of protein structure.. Steven Ludtke, assistant professor of biochemistry and molecular biology and co-director of the National Center for Macromolecular Imaging at Baylor College of Medicine and colleagues Dong-Hua Chen and Wah Chiu there and Jiu-Li Song and David Chuang at The University of Texas Southwestern Medical Center in Dallas, studied a mutant protein and came to this perhaps not so startling conclusion. The protein GroEL chaperones misfolded proteins and nudges them into their active folded state in the cell. Protein misfolding is implicated in a number of neurodegenerative diseases, ...
Tumor cells transfected with a bacterial heat-shock gene lose tumorigenicity and induce protection against tumors. | JEM
The gene encoding a highly immunogenic mycobacterial heat-shock protein (hsp65) was transfected into the murine macrophage tumor cell line J774. The resulting hsp65-expressing cells (J774-hsp65) were no longer able to produce tumors in syngeneic mice. This loss of tumorigenicity was not mediated through T cells since the transfected cells did not produce tumors in athymic mice. If mice are first immunized with the J774-hsp65 cells and then challenged with the parent J774 cells, the mice do not develop tumors, indicating that the presence of the mycobacterial hsp65 protein greatly enhances immunological recognition of unique structures expressed by the parent tumor cells. This is further confirmed by the demonstration in vitro of T cells derived from J774-hsp65-immunized mice that are cytotoxic for the parent J774 cells. The results provide the basis for a novel strategy for enhancing the immunological recognition and decreasing the tumorigenicity of transformed cells. ...
Immune Response Regulation | Science Signaling
Mycobacterial heat shock proteins have been implicated in the way the host response to mycobacterial infection is finely balanced to control pathogen dissemination while preventing immunopathology. Constitutive overexpression of mycobacterial Hsp70 (myHsp70) enhances mycobacterial clearance in mouse models, and Hsps can promote antitumor and antiviral immune responses. Human dendritic cells pulsed with myHsp70 generate potent antigen-specific cytotoxic T cell responses, which are dependent on a calcium-signaling cascade. Floto et al. now show that this critical function of myHsp70 is dependent on signaling through the HIV coreceptor, CCR5.. R. A. Floto, P. A. MacAry, J. M. Boname, T. S. Mien, B. Kampmann, J. R. Hair, O. S. Huey, E. N. G. Houben, J. Pieters, C. Day, W. Oehlmann, M. Singh, K. G. C. Smith, P. J. Lehner, Dendritic cell stimulation by mycobacterial Hsp70 is mediated through CCR5. Science 314, 454-458 (2006). [Abstract] [Full Text]. ...
The potential use of heat-shock proteins to vaccinate against mycobacterial infections. | Base documentaire | BDSP
Over the last few years, some of our experiments in which mycobacterial heat-shock protein HSP antigens were presented to the immune system as if they were viral antigens have had a significant impact on our understanding of protective immunity against tuberculosis. They have also markedly enhanced the prospects for new vaccines. We now know...
Immunofluorescent analysis of Heat Shock Protein 84 using Anti-Heat Shock Protein 84 Polyclonal Antibody (Product# PA3-012) shows staining in U251 Cells. Heat Shock Protein 84 staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with or an antibody recognizing Heat Shock Protein 84 (Product# PA3-012) at a dilution of 1:100 over night at 4 °C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product# 35552, Goat Anti-Rabbit). Images were taken at 60X magnification. ...
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Super Bowl 2014! Woo! (I really think it should be Superbowl, one word, but I guess thats incorrect.) Here are 5 relatively easy Football-Shaped Super Bowl
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مهندسی ژنتیک ژنوم هستهای گیاه برای اختصاصی کردن بیان ژن در کلروپلاست با طراحی و تراریزش سیگما فاکتور هیبرید
سیستمی با قرار دادن پیشبر شوک حرارتی E. coli (groE) در ناقل پلاستیدی و ساخت سیگما فاکتور هیبرید گیاه- باکتری تحت یک پیشبر مختص بافت طراحی گردید تا بتوان بر مشکل کاهش رشد و یا باروری گیاه در انتقال ژن به پلاستید که اغلب به دلیل اثرات تولید دائمی محصول تراژن ایجاد میگردد غلبه نمود. بهطوریکه با ترکیب موتیفهای قسمت پایانة N شبه سیگما فاکتور توتون که دارای توالی نشانه برای ورود به کلروپلاست و موتیف برهمکنش با پلیمراز کلروپلاستی میباشد با موتیفهای قسمت C-ترمینال فاکتور سیگما 32ی E. coli که قدرت تشخیص و اتصال به پروموتر groE را دارد، یک فاکتور سیگمای هیبرید گیاه E. coli
Chemistry for Biologists: Nucleic acids
DNA is formed from two polynucleotide chains. Each chain has a helical structure (a helix), in other words the molecule is coiled like a spring.. The two helices are then intertwined to give a double helix. The bases are on the inside of the helix and the phosphate groups are on the outside.. The two helices are held together by pairing of the nucleotides bases through hydrogen bonding. Because the double ring purines are bigger than the single ring pyrimidines the structure can only form with purine bases opposite pyrimidine bases. A big one complements a little one to take up about the same space.. ...
HSPB8 Protein Human Recombinant | HSP22 Antigen | ProSpec
HSPB8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 23.7kDa.
blogorrhea: More Science on the Desktop
So to create my own family tree of two dozen or so microbes, I said to hell with 16S ribosomes and decided to use, as my yardstick, genetic variation in the GroEL gene, which codes for the 60-kiloDalton heat-shock protein. I chose this protein (or rather, the gene for it) as my phylo-yardstick for a number of reasons. First, the DNA sequence is sizable, at about 1643 nucleotides (making it somewhat bigger than the 16S rDNA). Its important to have a large yardstick gene when looking for faint genetic signals. Secondly, this protein is essentially universal in prokaryotes. Its ubiquitous but not necessarily highly conserved, in the same sense that rRNA is highly conserved. (Highly conserved is not what you want. Think about it. Taken to the extreme, a highly conserved sequence is invariant. It never changes. And is therefore useless for phylogenetics.) Thirdly, the GroEL heat-shock protein has multiple intracellular touchpoints: Its known to interact with GroES, ALDH2, and dihydrofolate ...
PPT - NUCLEOTIDE MONOMER PowerPoint Presentation - ID:2227992
NUCLEOTIDE MONOMER. H. 5. Pyrimidines (single ring bases) thymine cytosine uracil Purines (double-ring bases) adenine guanine. 1. 5C ribose/ deoxyribose sugar @ 1 C , N-base covalently bonds @ 5 C, phosphate bonds. DEHYDRATION. l inks them. Slideshow 2227992 by...
Asian Journal of Research in Chemistry
In Present study our aim is to purify and characterize GroES and GroEL from genetically modified strain E.coli U1/pUS01/pUSS1?CAT L .GroES was eluted at 0.2M NaCl and GroEL was at 0.3M NaCl. From1.4 litres culture 7.5mg GroEL and 50mg GroES was purified.
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ABIN599719 - antibodies-online HSPD1 antibody | Antibodypedia
Lyophilized powder may be stored at -20°C. Stable for 1 year at -20°C. Aliquot to avoid freeze-thaw cycles. Store at -20°C. Reconstituted product is stable for 1 year at -20°C ...
Recombinant Human Heat Shock 27kDa Protein 1 HSPB1-4923H - Creative BioMart
Recombinant Human HSPB1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids and have a molecular weight of 22.7 kDa. The protein was purified by proprietary chromatographic techniques.
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Hsp60兔多克隆抗体(ab82513)可与小鼠, 大鼠, 羊, 兔, 鸡, 豚鼠, 仓鼠, 牛, 狗, 人, 猪, 果蝇, 鱼, 猴, 大肠杆菌, 蟹样本反应并经WB实验严格验证，被1篇文献引用。
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Hereditary spastic paraplegia
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 ...
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, ...
1998). "Streptococcus iniae, a human and animal pathogen: specific identification by the chaperonin 60 gene identification ...
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 ...
Species and Phenotypically Similar Lactococcus and Vagococcus Species by Reverse Checkerboard Hybridization to Chaperonin 60 ...
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 ...
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 ...
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 ...
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). " ...
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 ...
"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) ...
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- ...
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, ...
Major sperm protein
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 ...
Arthur L. Horwich
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 ...
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 ...
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): ...
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. ...
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 ...
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 ...
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). " ...
... 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 ...
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 ...
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 ...
Single particle analysis
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 ...
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 ...
"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 ( ...
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 ...
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 ( ...
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 ...
... 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). " ...
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 ...
Heat shock protein
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- ...
The chaperonin-60 universal target is a barcode for bacteria that enables de novo assembly of metagenomic sequence data
1gr5.1 | SWISS-MODEL Template Library
The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms<...
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 ...
Genes | Free Full-Text | Impacts of the Type I Toxin-Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene Expression
Atypical Streptococcus suis in Man, Argentina, 2013 - Volume 20, Number 3-March 2014 - Emerging Infectious Diseases journal -...
The link between transcript regulation and de novo protein synthesis in the retrograde high light acclimation response of...
To my British readers
HOMD :: SEQF1643
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. ...
HOMD :: SEQF3527
The roles of molecular chaperones in vivo<...
MH DELETED MN ADDED MN
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. ...
薬学部 - 研究成果 - Keio University
Graduate School of Health Sciences - Research output - Okayama University
Microbial carriage state of peripheral blood dendritic cells (DCs) in chronic periodontitis influences DC differentiation,...
CoP: Co-expressed Biological Processes
","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 ...
Kaninchen HSPD1 ELISA Kit | Produkt Nr. ABIN628283
... 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 ...
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
DeCS 2010 - Deleted terms
Application of proteomics to identify the target molecules involved in Lonicera japonica-induced photokilling in human lung...
We found six 73-kDa heat shock protein 70 with pI values of 5.23-5.60 (Figure 1; arrow S1), four 61-kDa chaperonin with pI ... To further elucidate whether the protein expression of HSP60 (chaperonin) and HSP70 is involved in photoactivated Lonicera ... chaperonin and actin cytoplasmic 1. These protein spot families are identical in molecular weight but different in pI values. ... heat shock protein 70 and chaperonin, also known as heat shock protein 60), cytoskeleton-related proteins (heat shock protein ...
Cpn60SUBUNITProteinGenesAmino AcidsFamilyFunctionHsp60GroESGroup I chaperoninSubunit with uniqueProteinsApproximately 60Highly conservedMoleculeHeatAlpha subunitRRNATRiCPutativeHydrolysisProtein FoldingBacterialSequencesBacteriaMolecularCPN10PolypeptideGeneReceptorsComplexesOrganismCrystal structureStructureCellsDataProperties
- Microbial profiling using the chaperonin60 (cpn60) universal target (UT) improves resolution of vaginal species associated with negative health outcomes compared to the more commonly used 16S ribosomal DNA target. (bvsalud.org)
- CRD_01646 groEL Chaperonin Cpn60/TCP-1 Length = 545 Score = 30.0 bits (66), Expect = 0.15, Method: Compositional matrix adjust. (microbedb.jp)
- The underlying data provided by the journal are published in the S1B File of the article, given that original files were not available for assessment in a number of instances and the integrity issues surrounding the preparation of Fig 2B, the PLOS Biology Editors issue this Expression of concern: A chaperonin subunit with unique structures is essential for folding of a Specific Substrate. (kellersign.com)
- Peng L, Fukao Y, Myouga F, Motohashi R, Shinozaki K, Shikanai T (2011) A Chaperonin Subunit with Unique Structures Is Essential for vasotec discount Folding of a Specific Substrate. (kellersign.com)
- The underlying data to support the other results reported in the lower regions of lanes 1 and 5 in Fig 2B, the PLOS Biology Editors (2020) Expression of concern: A chaperonin subunit with unique structures is essential for folding of a Specific Substrate. (kellersign.com)
- Citation: The PLOS Biology Editors issue this Expression of concern: A chaperonin subunit with unique structures is essential for folding of a specific substrate. (kellersign.com)
- Coomassie Brilliant Blue staining in the supporting data and updated figures provided by the authors support the overall results presented in Fig 2B, although the PLOS Biology Editors (2020) Expression of concern: A chaperonin subunit with unique structures is essential for folding of a Specific Substrate. (kellersign.com)
- The nucleotide-free chaperonin GroEL is capable of capturing transient unfolded or partially unfolded states that flicker in and out of existence due to large-scale protein dynamic vibrational modes. (elsevier.com)
- This ELISA kit is a solid phase ELISA designed for quantitative determination of Heat Shock Protein 60. (antikoerper-online.de)
- ab5479 detects Hsp 60 from Human cells, tissues and recombinant protein preparations. (abcam.cn)
- Crude extracts of P. fumarii strain 1AT cells show a strong cross-reaction with antibodies prepared against the thermosome of Pyrodictium occultum , which could suggest highly similar chaperonin protein complexes. (mirnamimics.com)
- Here, we have used a combination of transcriptomics, proteomics and targeted mutagenesis to reveal that the clp gene regulator (ClgR) of Mycobacterium tuberculosis activates the transcription of at least ten genes, including four that encode protease systems (ClpP1/C, ClpP2/C, PtrB and HtrA-like protease Rv1043c) and three that encode chaperones (Acr2, ClpB and the chaperonin Rv3269). (microbiologyresearch.org)
- Epitope mapping studies using human Hsp 60 deletion mutants suggest that this antibody binds between amino acids 211-288. (abcam.cn)
- This gene encodes a member of the chaperonin family. (fishersci.no)
- YbbN acts as a mild inhibitor of GroESL chaperonin function and ATPase activity, suggesting that it is a negative regulator of the GroESL system. (rcsb.org)
- Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)-mediated protein folding, the final step in the accurate expression of genetic information. (nih.gov)
- 4. An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space. (nih.gov)
- 11. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. (nih.gov)
- Heat shock protein 60, Hsp60) and II (e.g. (unipa.it)
- INTRODUCTION: Based upon evidence suggesting that concentrations of anti-heat shock protein-60 (anti-HSP60) and interleukin-2 (IL-2) are associated with atherogenesis, we tested the hypothesis that anti-HSP60 and IL-2 are associated with coronary artery calcium (CAC) score, a marker of subclinical atherosclerosis. (nih.gov)
- ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein.GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques. (assaygenie.com)
- Differential expressed proteins including alpha enolase 1 (ENO1), glutamate dehydrogenase 1 (GLUD1), glutathione S-transferase A1 (GSTA1), ATP synthase subunit 5β (ATP5β), superoxide dismutase [Cu-Zn] (SOD1), cytochrom c oxidase subunit Via (COX6A1) and heat shock protein 60 (HSP60) were further verified by real-time PCR and/or western blot at mRNA or protein expression level. (biomedcentral.com)
- The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. (nih.gov)
- 3NX6: Crystal Structure of co-chaperonin, GroES (Xoo4289) from Xanthomonas oryzae pv. (rcsb.org)
- Belongs to the GroES chaperonin family. (assaygenie.com)
- Large rigid-body domain movements are critical to GroEL-mediated protein folding, especially apical domain elevation and twist associated with the formation of a folding chamber upon binding ATP and co-chaperonin GroES. (rcsb.org)
Group I chaperonin3
- A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. (nih.gov)
- Many of the sequences in cpnDB are partial gene sequences, representing only the universal target portion of the cpn 60 gene (group I chaperonin). (cpndb.ca)
- A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. (nih.gov)
Subunit with unique10
- The PLOS Biology Editors issue this Expression of concern: A chaperonin subunit with unique structures is essential nexium cost per pill for folding of a Specific Substrate. (greenhub.energy)
- Peng L, Fukao Y, Myouga F, Motohashi R, Shinozaki K, Shikanai T (2011) A Chaperonin Subunit with Unique buy plaquenil online canada Structures https://pivnicaorechova.sk/buy-plaquenil-over-the-counter/ Is Essential for Folding of a specific substrate. (waw.pl)
- This is an open access article distributed under the terms of the article, given that original files were not available for assessment in a number of instances and the integrity issues surrounding the preparation of Fig 2B, although the PLOS Biology Editors issue this Expression of concern: A chaperonin subunit with unique structures is essential for folding of a specific substrate. (waw.pl)
- Peng L, Fukao Y, Myouga F, Motohashi R, Shinozaki K, Shikanai T (2011) A Chaperonin Subunit with Unique Structures Is Essential for Folding of a Specific Substrate. (waw.pl)
- Peng L, Fukao Y, Myouga F, Motohashi R, Shinozaki K, Shikanai T (2011) A Chaperonin http://czbo.emaginativeconcepts.com/low-price-maxalt/ Subunit with Unique Structures Is Essential for maxalt versus imitrex Folding of a Specific Substrate. (ovh.net)
- Instead, the authors have not commented on the availability of underlying data to support the overall results presented in Fig 2B, although the PLOS Biology Editors (2020) Expression of concern: A chaperonin subunit with unique structures is essential for folding of a specific substrate. (thebyronsociety.com)
- Peng L, Fukao Y, how to buy cheap lisinopril online https://libraries.rucevzhuru.cz/lisinopril-cost-per-pill/ Myouga F, Motohashi R, Shinozaki K, Shikanai T (2011) A Chaperonin Subunit with Unique Structures Is Essential for Folding of a specific substrate. (urban-intergroup.eu)
- Peng L, Fukao Y, Myouga F, how much does generic vytorin cost Motohashi R, Shinozaki K, Shikanai T (2011) A Chaperonin Subunit with Unique Structures Is Essential for Folding of a specific substrate. (projectretailx.com)
- Specifically, Concerns were raised about discontinuities can farxiga make you tired in the lower regions of lanes 1 and 5 in Fig 2B, although the PLOS Biology Editors (2020) Expression of concern: A chaperonin subunit with unique structures is essential for folding of a specific substrate farxiga price usa . (icedelights.co.uk)
- Citation: The PLOS Biology Editors issue this Expression of concern: A click this chaperonin subunit with unique structures is essential for folding of a Specific Substrate farxiga price usa. (icedelights.co.uk)
- FtsA is a conserved bacterial actin homologue, suggesting that as in eukaryotes, some bacteria exhibit a connection between cytoskeletal actin proteins and chaperonins. (scilifelab.se)
- [ 31 ] In northern Italy, it has been reported that approximately 70% of bovine herds are infected with MAP [ 32 ] and approximately 60% of Sardinian sheep flocks are infected by this pathogen. (medscape.com)
- In this study, an immunochromatographic antigen detection test kit (ICT AgTK) that targets the highly conserved O. tsutsugamushi 60 kDa GroEL chaperonin (heat shock protein 60) was developed. (jsce-ip.com)
- This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state. (nih.gov)
- According to the literature GroEL and its human homologue heat shock protein (HSP)60 may bind to different surface receptors, including toll-like receptor (TLR)4 and scavenger receptors. (omicsonline.org)
- A chaperonin 60 heat-shock protein isolated from bacteria. (nih.gov)
- Association between anti-human heat shock protein-60 and interleukin-2 with coronary artery calcium score. (nih.gov)
- Recent results suggested that a large subset of heat shock protein HSP-60 reactive peripheral lymphoid γδ T cells preexists in normal adult mice, all members of which respond to a single segment of this common HSP. (elsevier.com)
- This gene encodes a major heat shock protein which functions as a chaperonin. (assaygenie.com)
- A chaperonin 10 heat-shock protein isolated from bacterial sources. (nih.gov)
- The amplified region corresponds to nucleotides 142-858 of the Group II chaperonin (alpha subunit) of Methanococcus maripaludis strain S2 . (cpndb.ca)
- The chaperonin 60 gene phylogenetic tree was similar to the previously published tree based on 16S rRNA sequences, and it was also observed that strains with identical chaperonin 60 gene sequences tended to have identical 16S rRNA sequences. (nih.gov)
- Is the cpn 60 better than the 16S rRNA gene for resolving closely related species? (cpndb.ca)
- cpn 60 UT based phylogenies are consistent with those based on 16S rRNA, but cpn 60 UT sequences are generally more variable, providing better resolution of closely related taxa. (cpndb.ca)
- 2012 ) used the Barcode of Life framework and criteria to establish that cpn 60 UT is a preferred barcode for Bacteria compared to the 16S rRNA gene or its variable regions. (cpndb.ca)
- Group II chaperonins (CCT, for c haperonin c ontaining T CP1 or TriC, for T CP1 ri ng c omplex) are archaeal and eukaryote cytoplasmic counterparts of the group I chaperonins. (cpndb.ca)
- Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assembly. (healthsciencessc.org)
- 67 1e-11 At5g16070.1 68418.m01878 chaperonin, putative similar to SWISS-P... 57 8e-09 At3g02530.1 68416.m00241 chaperonin, putative similar to SWISS-P... 56 1e-08 At5g18820.1 68418.m02236 chaperonin, putative similar to SWISS-P... 43 1e-04 At2g28000.1 68415.m03393 RuBisCO subunit binding-protein alpha s... 36 0.020 At5g56500.1 68418.m07051 chaperonin, putative similar to SWISS-P... 34 0.062 At3g13470.1 68416.m01695 chaperonin, putative similar SWISS-PROT. (u-tokyo.ac.jp)
- 33 0.19 At1g26230.1 68414.m03200 chaperonin, putative similar to SWISS-P... 31 0.44 At2g16400.1 68415.m01877 homeodomain-containing protein 29 2.3 At2g33210.1 68415.m04069 chaperonin, putative similar to SWISS-P... 28 5.4 At3g50090.1 68416.m05476 exonuclease family protein contains exo. (u-tokyo.ac.jp)
- The chaperonin GroEL is a megadalton-sized molecular machine that plays an essential role in the bacterial cell assisting protein folding to the native state through actions requiring ATP binding and hydrolysis. (elsevier.com)
- The prototypical chaperonin GroEL assists protein folding through an ATP-dependent encapsulation mechanism. (nih.gov)
- In vivo observation of polypeptide flux through the bacterial chaperonin system. (valteme.com)
- To that effect, partial chaperonin 60 gene sequences were determined for the 35 serotype reference strains of S. suis. (nih.gov)
- The chaperonin 60 gene sequences provided a higher level of discrimination between serotypes than the 16S RNA sequences provided and could form the basis for a diagnostic protocol. (nih.gov)
- Why do only some records have full-length cpn 60 sequences? (cpndb.ca)
- Full-length cpn 60 sequences are available for only a subset of the species represented in cpnDB. (cpndb.ca)
- Many of the sequences were determined through application of the universal, degenerate primers for cpn 60 amplification so that only the universal target sequence is available. (cpndb.ca)
- Is cpn 60 really universal in the Bacteria? (cpndb.ca)
- Chaperonins are a diverse family of molecular chaperones that are present in the plastids, mitochondria, and cytoplasm of eukaryotes, eubacteria and archaea. (cpndb.ca)
- En esas condiciones, una ruta molecular en la que intervienen AMPK y PFKFB3 induce la glucólisis y las células paradas en mitosis muestran unos requerimientos aumentados a la glucosa, una adición que puede tener implicaciones en terapia del cáncer. (sebbm.es)
- Group I chaperonins function with a cochaperonin protein (CPN10 or CPN21). (cpndb.ca)
- Chaperonin Containing T-Complex polypeptide 1, CCT). (unipa.it)
- This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. (assaygenie.com)
- These changes were detected among hybridomas generated with cells restimulated in vitro and included a large increase in hybridizable γδ T cells, a nearly maximal increase in the relative frequency of HSP-60-reactive cells, and structural changes in expressed T-cell receptors of HSP-60-reactive cells. (elsevier.com)
- Archaeal group II chaperonin complexes are composed of variable numbers (often 2 or 3) of subunit types. (cpndb.ca)
- Other options include coexpression with chaperonins or other folding-machinery components, and the use of an alternative host organism. (sigmaaldrich.com)
- Crystal structure of chaperonin-60 from Paracoccus denitrificans. (nih.gov)
- Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. (cathdb.info)
- Interestingly, we failed to elicit a detectable γβ T-cell response to the particular peptide stimulatory for γδ T cells, although at least three other HSP-60 epitopes were recognized. (elsevier.com)
- According to data from the World Health Organization [ 1 ], 6-7 million individuals are infected by the parasite throughout Latin America and around 60-70 million people are at risk of infection. (biomedcentral.com)
- Compositional properties of 60 kDa chaperonin (bottom) versus UniprotKB/SwissProt (top). (ucy.ac.cy)