Abstract: Small heat shock proteins form large cytosolic assemblies from an α-crystallin domain (ACD) flanked by sequence extensions. Mutation of a conserved arginine in the ACD of several human small heat shock protein family members causes many common inherited diseases of the lens and neuromuscular system. The mutation R120G in αB-crystallin causes myopathy, cardiomyopathy and cataract. We have solved the X-ray structure of the excised ACD dimer of human αB R120G close to physiological pH and compared it with several recently determined wild-type vertebrate ACD dimer structures. Wild-type excised ACD dimers have a deep groove at the interface floored by a flat extended bottom sheet. Solid-state NMR studies of large assemblies of full-length αB-crystallin have shown that the groove is blocked in the ACD dimer by curvature of the bottom sheet. The crystal structure of R120G ACD dimer also reveals a closed groove, but here the bottom sheet is flat. Loss of Arg120 results in rearrangement of ...

In Leuconostoc oenos, different stresses such as heat, ethanol, and acid shocks dramatically induce the expression of an 18-kDa small heat shock protein called Lo 18. The corresponding gene (hsp18) was cloned from a genomic library of L. oenos constructed in Escherichia coli. A 2.3-kb DNA fragment carrying the hsp18 gene was sequenced. The hsp18 gene encodes a polypeptide of 148 amino acids with a calculated molecular mass of 16,938 Da. The Lo18 protein has a significant identity with small heat shock proteins of the alpha-crystallin family. The transcriptional start site was determined by primer extension. This experiment allowed us to identify the promoter region exhibiting high similarity to consensus promoter sequences of gram-positive bacteria, as well as E. coli. Northern blot analysis showed that hsp18 consists of a unique transcription unit of 0.6 kb. Moreover, hsp18 expression seemed to be controlled at the transcriptional level. This small heat shock protein was found to be ...

αB-Crystallin (αB) and HSP27 belong to the class of small Heat Shock Proteins (sHSPs) whose levels of expression increase under conditions of cellular stress, viz., heat, pH, and ischemia. sHSPs form an integral part of the cellular chaperone network by maintaining aggregation-prone proteins in a soluble state. Due to their tendency to form large oligomeric structures, human small heat shock factors have been refractory to structural studies. We are using a combination of solution-state and solid-state NMR approaches to define the structures of dimeric constructs and of large oligomers. Although the full extent of the functions of αB-Crystallin (αB) and HSP27 remain to be determined, the proteins are each implicated in certain inherited forms of dystrophies and αB is also implicated in breast and other forms of cancer.. The PhoQ/PhoP two-component regulatory system plays a critical role in bacterial virulence. PhoQ is a sensor kinase that is capable of sensing the environment in which the ...

article{c39ed0c6-71b3-44bd-ae7d-1c63648fa85e, abstract = {,p,The small heat shock protein (sHsp) chaperones are crucial for cell survival and can prevent aggregation of client proteins that partially unfold under destabilizing conditions. Most investigations on the chaperone activity of sHsps are based on a limited set of thermosensitive model substrate client proteins since the endogenous targets are often not known. There is a high diversity among sHsps with a single conserved β-sandwich fold domain defining the family, the α-crystallin domain, whereas the N-terminal and C-terminal regions are highly variable in length and sequence among various sHsps and conserved only within orthologues. The endogenous targets are probably also varying among various sHsps, cellular compartments, cell type and organism. Here we have investigated Hsp21, a non-metazoan sHsp expressed in the chloroplasts in green plants which experience huge environmental fluctuations not least in temperature. We describe how ...

Effect of long term heat stress and dietary restriction on the expression of small heat shock protein sHSP genes in rat liver tissue ...

The eleven students involved learned basic experimental design (with positive and negative controls), troubleshooting, a wide variety of laboratory techniques, and data collection, analysis and presentations skills. In addition, students learned to read and analyze scientific work from other labs since they are given scientific articles to read beginning on their first day in the lab. This project is in collaboration with Ivor Benjamin M.D., Ph.D. at the University of Utah, which allowed these students the unique opportunity of discussing their research with a larger audience once a month. In addition to intellectual enrichment, students learned to function as a team, with those more experienced (graduate students Kelsey Langston and Whitney Hayes) mentoring those who are new in the lab. As students progressed in their understanding of the project and mastery of basic laboratory skills, they become involved in planning our weekly group meeting, preparing figures for presentations/publications, ...

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.

Chen X, Lin S, Liu Q, Huang J, Zhang W, Lin J, Wang Y, Ke Y, He H. Expression and interaction of small heat shock proteins (sHsps) in rice in response to heat stress. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 2014, 1844 (4): 818-828. ...

Heat-stress induced alterations in localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for ?B-crystallin and hsp ...

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Distal hereditary motor neuronopathies (dHMNs) are a clinically and genetically heterogeneous group of disorders in which motor neurons selectively undergo age-dependant degeneration. Mutations in the small heat-shock protein HSPB1 (HSP27) are responsible for one form of dHMN. In this study, we have analysed the effect of expressing a form of mutant HSPB1 in primary neuronal cells in culture. Mutant (P182L) but not wild-type HSPB1 led to the formation of insoluble intracellular aggregates and to the sequestration in the cytoplasm of selective cellular components, including neurofilament middle chain subunit (NF-M) and p150 dynactin. These findings suggest a possible pathogenic mechanism for HSPB1 whereby the mutation may lead to preferential motor neuron loss by disrupting selective components essential for axonal structure and transport.

Under changes in conditions as diverse as temperature, oxidation or pH, proteins in an organism may undergo harmful denaturation. Small Heat Shock proteins act as paramedics of the cell: during such events they quicky intervene by binding nascently unfolding proteins, leading them to refolding or denaturation pathways. Small heat shock proteins are ubiquitous in all kingdoms of life, but especially effective in plants: after all, plants cannot escape from harsh environmental conditions!. Collaborating with Benesch (University of Oxford) and Vierling (UMass) groups, we have contributed to shedding light into the mode of action of small Heat Shock Proteins in wheat and pea.. We describe a mechanism whereby dimers of these proteins are responsible for capturing their substrate, before assemblying into larger complexes. With our own integrative modelling methods using distance restraints and collision cross-section measurements, we demonstrate that small heat shock protein dimers assemble into ...

Helianthus annuus hsp17.6 G1 protein: a small heat-shock protein from sunflower; amino acid sequence in first source; GenBank Z95153

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

TY - JOUR. T1 - Structural and Mechanical Hierarchies in the α-Crystallin Domain Dimer of the Hyperthermophilic Small Heat Shock Protein Hsp16.5. AU - Bertz, Morten. AU - Chen, Jin. AU - Feige, Matthias J.. AU - Franzmann, Titus M.. AU - Buchner, Johannes. AU - Rief, Matthias. PY - 2010/7. Y1 - 2010/7. N2 - In biological systems, proteins rarely act as isolated monomers. Association to dimers or higher oligomers is a commonly observed phenomenon. As an example, small heat shock proteins form spherical homo-oligomers of mostly 24 subunits, with the dimeric α-crystallin domain as the basic structural unit. The structural hierarchy of this complex is key to its function as a molecular chaperone. In this article, we analyze the folding and association of the basic building block, the α-crystallin domain dimer, from the hyperthermophilic archaeon Methanocaldococcus jannaschii Hsp16.5 in detail. Equilibrium denaturation experiments reveal that the α-crystallin domain dimer is highly stable against ...

Charcot-Marie-Tooth disease (CMT) is the most common inherited neuromuscular disease and is characterized by considerable clinical and genetic heterogeneity. We previously reported a Russian family with autosomal dominant axonal CMT and assigned the locus underlying the disease (CMT2F; OMIM 606595) to chromosome 7q11-q21 (ref. 2). Here we report a missense mutation in the gene encoding 27-kDa small heat-shock protein B1 (HSPB1, also called HSP27) that segregates in the family with CMT2F. Screening for mutations in HSPB1 in 301 individuals with CMT and 115 individuals with distal hereditary motor neuropathies (distal HMNs) confirmed the previously observed mutation and identified four additional missense mutations. We observed the additional HSPB1 mutations in four families with distal HMN and in one individual with CMT neuropathy. Four mutations are located in the Hsp20-alpha-crystallin domain, and one mutation is in the C-terminal part of the HSP27 protein. Neuronal cells transfected with mutated HSPB1

Hsp27, a small heat-shock protein, has important roles in many cellular processes, including cytoskeleton dynamics, cell differentiation, and apoptosis. Its expression in normal epidermis correlates with differentiation; however, little is known about the regulatory mechanisms involved. In this study, we report that Hsp27 undergoes upregulation, phosphorylation, and redistribution to the cytoskeleton during the late phase of epidermal keratinocyte differentiation. Our results also show that the expression of the dual leucine zipper-bearing kinase (DLK), an upstream activator of the MAP kinase pathways, is sufficient by itself to induce Hsp27 phosphorylation, cell periphery localization, and redistribution to the insoluble protein fraction (cytoskeleton) in poorly differentiated keratinocytes. This redistribution correlates with the insolubilization of cornified envelope-associated proteins such as involucrin. Interestingly, the effects of DLK on Hsp27 were blocked by PD98059, a selective ...

article{28a73216-cb79-4da4-9c2e-f0213dfb2b2d, abstract = {During evolution of land plants, a specific motif occurred in the N-terminal domain of the chloroplast-localized small heat shock protein, Hsp21: a sequence with highly conserved methionines, which is predicted to form an amphipathic -helix with the methionines situated along one side. The functional role of these conserved methionines is not understood. We have found previously that treatment, which causes methionine sulfoxidation in Hsp21, also leads to structural changes and loss of chaperone-like activity. Here, mutants of Arabidopsis thaliana Hsp21 protein were created by site-directed mutagenesis, whereby conserved methionines were substituted by oxidation-resistant leucines. Mutants lacking the only cysteine in Hsp21 were also created. Protein analyses by nondenaturing electrophoresis, size exclusion chromatography, and circular dichroism proved that sulfoxidation of the four highly conserved methionines (M49, M52, M55, and M59) is ...

We report on a new cDNA clone (Qshsp10.4-CI) of a Quercus suber L. class-CI small heat-shock protein (sHsp) obtained from cork (phellem), a highly oxidatively stressed plant tissue. The deduced gene product lacks the C-terminal extension and the consensus I region of the alpha-crystallin domain, bei …

Current models derived from in vitro studies propose that sHsps prevent irreversible substrate aggregation by binding heat-denatured substrates, and then present substrate to other cellular components for ATP-dependent refolding (Waters et al., 1996; Ehrnsperger et al., 1997;Lee et al., 1997; Veinger et al., 1998). Our data extend this model for sHsp chaperone activity in several important ways. First, we determined that the chaperones required for high levels of refolding of Hsp18.1-bound Luc were Hsp/Hsc70 plus DnaJ homologs. The addition of Hsp90 and Hop gave minimal or no further enhancement of refolding. Despite the eukaryotic origin of Hsp18.1, the highest Luc refolding rates were observed when Hsp18.1-bound Luc was reactivated in the presence of the prokaryotic DnaK system. These findings imply that the mechanism of sHsp action in conjunction with Hsp70 systems is universal among eukaryotes and prokaryotes, and suggest that sHsps may not physically interact with the Hsp70 systems. Also, ...

Singh BN, Rao KS, Rao ChM (2010) Ubiquitin-proteasome-mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shock protein, during muscle differentiation. Biochim Biophys Acta 1803, 288-99 20005263 ...

Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a member of the tumor necrosis factor α family of cytokines that preferentially induces apoptosis in transformed cells, making it a promising cancer therapy. However, many neoplasms are resistant to TRAIL-induced apoptosis by mechanisms that are poorly understood. We demonstrate that the expression of the small heat shock protein αB-crystallin (but not other heat shock proteins or apoptosis-regulating proteins) correlates with TRAIL resistance in a panel of human cancer cell lines. Stable expression of wild-type αB-crystallin, but not a pseudophosphorylation mutant impaired in its assembly and chaperone function, protects cancer cells from TRAIL-induced caspase-3 activation and apoptosis in vitro. Furthermore, selective inhibition of αB-crystallin expression by RNA interference sensitizes cancer cells to TRAIL. In addition, wild-type αB-crystallin promotes xenograft tumor growth and inhibits TRAIL-induced apoptosis in vivo in nude

Small heat shock protein HspB8: its distribution in Alzheimers disease brains s inhibition of amyloid-beta protein aggregation and cerebrovascular d-beta toxicity ...

Charcot-Marie-Tooth disease (CMT) is a group of clinically and genetically heterogeneous peripheral neuropathies. HSPB8 gene encodes heat shock protein 22 (HSP22) which belongs to the superfamily of small stress induced proteins. Mutations in HSPB8 are implicated to CMT2L and distal hereditary motor …

Any of a group of proteins in living cells that assist newly synthesized or denatured proteins to fold into their functional three-dimensional structures. The chaperones bind to the protein and prevent improper interactions within the polypeptide chain, so that it assumes the correct folded orientation. This process may require energy in the form of ATP. Other functions include assisting the translocation of proteins across the membranes of cell organelles and binding denatured proteins under stress conditions or in degenerative disease. There are several unrelated families of chaperones, including five classes of heat-shock proteins - HSP25 (small heat-shock proteins), HSP60, HSP70, HSP90, and HSP100 - chaperonins, calnexin, and calreticulin. ...

Fig. 3. HS-stress-induced degeneration in the flight motor is age dependent. (A,C,D) Degeneration in 7-day-old flies. (A) Confocal immunofluorescence images of DLM neuromuscular synapses from no HS,10d control flies (Aa-Ac) or 7d HS,10d flies (Ad-Af) indicating HS-stress-induced degeneration of axonal and glial processes. Recordings of muscle membrane potential (Ag,Ah) indicate loss of muscle viability in 7d HS,10d flies, consistent with phalloidin staining shown in Fig. 2. (B-D) Young (1-day-old) flies are resistant to HS-stress-induced degeneration. (B) Confocal immunofluorescence images of DLM neuromuscular synapses from no HS,4d control flies (Ba-Bc) or 1d HS,4d flies (Bd-Bf), indicating resistance to HS-stress-induced degeneration. Recordings of muscle membrane potential (Bg,Bh) indicate persistence of muscle viability in 1d HS,4d flies. (C,D) Quantitative comparison of axonal (C) and glial (D) degeneration in 7d HS,10d or 1d HS,4d flies with those of the corresponding no-HS ...

The small heat shock protein HSP20 is known to be cardioprotective during times of stress and the mechanism underlying its protective abilities depends on its phosphorylation on Ser16 by PKA (protein kinase A). Although the external stimuli that trigger Ser16 phosphorylation have been well studied, the events that modulate spatial and temporal control of this modification remain to be clarified. Here, we report that inhibition of cAMP phosphodiesterase-4 (PDE4) induces the phosphorylation of HSP20 in resting cardiac myocytes and augments its phosphorylation by PKA following β-adrenergic stimulation. Moreover, using peptide array technology, in vitro binding studies, co-immunoprecipitation techniques and immunocytochemistry, we show that HSP20 binds directly to PDE4 within a region of the conserved catalytic domain. We also show that FRET-based, genetically-encoded cAMP reporters anchored to HSP20 exhibit a larger response to PDE4 inhibition compared to free cytosolic cAMP reporters, suggesting that the

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.

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Defective protein quality control (PQC) systems are implicated in multiple diseases. Molecular chaperones and co-chaperones play a central role in functioning PQC. Constant mechanical and metabolic stress in cardiomyocytes places great demand on the PQC system. Mutation and downregulation of the co-chaperone protein BCL-2-associated athanogene 3 (BAG3) are associated with cardiac myopathy and heart failure, and a BAG3 E455K mutation leads to dilated cardiomyopathy (DCM). However, the role of BAG3 in the heart and the mechanisms by which the E455K mutation leads to DCM remain obscure. Here, we found that cardiac-specific Bag3-KO and E455K-knockin mice developed DCM. Comparable phenotypes in the 2 mutants demonstrated that the E455K mutation resulted in loss of function. Further experiments revealed that the E455K mutation disrupted the interaction between BAG3 and HSP70. In both mutants, decreased levels of small heat shock proteins (sHSPs) were observed, and a subset of proteins required for ...

Defective protein quality control (PQC) systems are implicated in multiple diseases. Molecular chaperones and co-chaperones play a central role in functioning PQC. Constant mechanical and metabolic stress in cardiomyocytes places great demand on the PQC system. Mutation and downregulation of the co-chaperone protein BCL-2-associated athanogene 3 (BAG3) are associated with cardiac myopathy and heart failure, and a BAG3 E455K mutation leads to dilated cardiomyopathy (DCM). However, the role of BAG3 in the heart and the mechanisms by which the E455K mutation leads to DCM remain obscure. Here, we found that cardiac-specific Bag3-KO and E455K-knockin mice developed DCM. Comparable phenotypes in the 2 mutants demonstrated that the E455K mutation resulted in loss of function. Further experiments revealed that the E455K mutation disrupted the interaction between BAG3 and HSP70. In both mutants, decreased levels of small heat shock proteins (sHSPs) were observed, and a subset of proteins required for ...

Because they are capable of immediately binding unfolding proteins, sHSPs are the first responders to cell stress. Understanding how sHSPs accomplish this feat is critical to defining their roles in protection of cells from stress, says Vierling.. While much remains unknown about these environmental stresses and their associated impacts, Vierlings work is showing that sHSPs may protect plants from heat stress. She and her colleagues have established that molecular chaperone Hsp101 is essential for plants to survive in high temperatures. Heat stress can severely limit crop productivity, particularly at critical stages of plant development.Vierling and her colleagues are also working with Synechocystis (pond scum) to further investigate these effects.. As a post-doctoral researcher in the 1980s, Vierling was part of a group that isolated genes connected to high-temperature stress response-research that formed the foundation for what scientists now refer to as chaperones.. I started out ...

TY - JOUR. T1 - Rapidly progressive amyotrophic lateral sclerosis is associated with microglial reactivity and small heat shock protein expression in reactive astrocytes. AU - Gorter, R. P.. AU - Stephenson, J.. AU - Nutma, E.. AU - Anink, J.. AU - de Jonge, J. C.. AU - Baron, W.. AU - Jahreiss, M. -C.. AU - Belien, J. A. M.. AU - van Noort, J. M.. AU - Mijnsbergen, C.. AU - Aronica, E.. AU - Amor, S.. N1 - This article is protected by copyright. All rights reserved.. PY - 2019/8. Y1 - 2019/8. N2 - AIMS: Amyotrophic lateral sclerosis (ALS) is a chronic neurodegenerative disease characterised by progressive loss of motor neurons, muscle weakness, spasticity, paralysis and death usually within 2-5 years of onset. Neuroinflammation is a hallmark of ALS pathology characterized by activation of glial cells, which respond by upregulating small heat shock proteins (HSPBs), but the exact underlying pathological mechanisms are still largely unknown. Here, we investigated the association between ALS ...

Rhododendron from Burncoose Nurseries - Page 4 Varieties of Rhododendron available to buy include the following: RHODODENDRON Mrs T.H. Lowinsky ,RHODODENDRON Nova Zembla ,RHODODENDRON Ostara ,RHODODENDRON ...

The content of this thesis concerns the pursuit of protein structures from cradle to grave. This process is illustrated though the progress made on two separate proteins. The first is the serine palmitoyltransferase from Toxoplasma gondii (TgSPT). This protein is of interest as sphingolipid biosynthesis in apicomplexan parasites is currently the subject of study as a possible drug target, most notably in Plasmodium. We begin by looking at the techniques of bioinformatics used to analyse the amino acid sequence of this protein, and by calculation and comparison with other known protein sequences we are able to begin to identify the different domains of the protein and also to begin to identify their respective functions. Bioinformatic techniques are then further used in order to design constructs to be moved forward for overproduction in vivo. A number of different constructs showing significant soluble expression of various truncations of TgSPT are reported, and various techniques relating to ...

Small heat shock proteins (sHsps) are a group of proteins with molecular mass between 12 and 43 kDa. Currently, 11 members of this family have been classified, namely HspB1 to HspB11. HspB1, HspB2, HspB5, HspB6, HspB7, and HspB8, which are expressed in brain have been observed to be related to the pathology of neurodegenerative diseases, including Parkinsons, Alzheimers, Alexanders disease, multiple sclerosis, and human immunodeficiency virus-associated dementia. Specifically, sHsps interact with misfolding and damaging protein aggregates, like Glial fibrillary acidic protein in AxD, β-amyloid peptides aggregates in Alzheimers disease, Superoxide dismutase 1 in Amyotrophic lateral sclerosis and cytosine-adenine-guanine/polyglutamine (CAG/PolyQ) in Huntingtons disease, Spinocerebellar ataxia type 3, Spinal-bulbar muscular atrophy, to reduce the toxicity or increase the clearance of these protein aggregates ...

Small heat shock proteins (sHsps) are a group of proteins with molecular mass between 12 and 43 kDa. Currently, 11 members of this family have been classified, namely HspB1 to HspB11. HspB1, HspB2, HspB5, HspB6, HspB7, and HspB8, which are expressed in brain have been observed to be related to the pathology of neurodegenerative diseases, including Parkinsons, Alzheimers, Alexanders disease, multiple sclerosis, and human immunodeficiency virus-associated dementia. Specifically, sHsps interact with misfolding and damaging protein aggregates, like Glial fibrillary acidic protein in AxD, β-amyloid peptides aggregates in Alzheimers disease, Superoxide dismutase 1 in Amyotrophic lateral sclerosis and cytosine-adenine-guanine/polyglutamine (CAG/PolyQ) in Huntingtons disease, Spinocerebellar ataxia type 3, Spinal-bulbar muscular atrophy, to reduce the toxicity or increase the clearance of these protein aggregates ...

Exposure of cells to environmental or chemical stressors will initiate the heat shock response, which is mediated by heat shock proteins. Heat shock proteins are molecular chaperones which are classified by size into six main families: HSP100, HSP90, HSP70, HSP60, HSP40 and the small heat shock proteins (sHsps). The sHsp family members bind to denatured proteins and maintain them in a folding competent state such that they may be refolded by other molecular chaperones. ,br /,,br /, The present study examined the expression and function of two amphibian sHsps, namely, ,em,Rana catesbeiana,/em, HSP30 and ,em,Xenopus laevis,/em, HSP27. Initially, an antisense riboprobe was produced to study the mRNA accumulation of ,em,Rana hsp30,/em, in cultured tongue fibroblast (FT) cells. Results showed that ,em,Rana hsp30,/em, mRNA was optimally induced when maintained at 35°C for 2 h. An antibody to the recombinant ,em,Rana,/em, HSP30 protein was also produced in order to study HSP30 protein accumulation ...

This gene encodes a muscle-specific small heat shock protein. A mutation in this gene is the cause of autosomal dominant distal hereditary motor neuropathy type 2C.[provided by RefSeq, Sep 2010 ...

Ischemic preconditioning (IPC) represents the gold standard method of cardioprotection, but it is triggered by repetitive episodes of ischemia/reperfusion (IR), which limits its clinical application, reflecting the need of alternative approaches to activate the mechanisms of IPC. H11 Kinase/Hsp 22 (H11K) is a small heat shock protein up-regulated by IR, which provides cardioprotection equal to IPC through a nitric oxide (NO)-dependent mechanism. A main target of NO-mediated IPC is the mitochondria (M), where NO reduces oxygen consumption (VO2) and radical oxygen species (ROS) production during ischemia. We tested the hypothesis that H11K over-expression modulates M function through NO similarly to IPC. Fresh M were isolated from hearts of transgenic mice (TG) with cardiac-specific over-expression (5-fold) of H11K and compared to wild type mice (WT). Upon equal loading (normalized by PGC1 α abundance and citrate synthase activity) and in presence of either glucose or lipids, M from TG compared ...

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Gardening question - I planted two rhododendrons in May in a raised bed, next to each other. Both have doubled in size in the space of a few months and had been growing ve

Informations sur la culture, lentretien, la propagation des rhododendrons, les ravageurs et maladies, leur rusticité ainsi quun glossaire et références.

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Lysende skarlagenrød klokkeblomst Blomstrer i April Lavt voksende. Mørkegrønne let krusede blade. Planten er ca. 30 cm. høj efter 10 år Sol - halvskygge

Researchers have identified a common variant of the cardiovascular heat shock protein gene, HSPB7, which was found to increase risk for dilated cardiomyopathy by almost 50pc.

I am 37 years old, my youngest Child is 3 months. For 3 days now I have been getting seemingly random hot spots on my legs, they start as a small heat ***** feeling and bloom out into a larger ar...

During the summer when the temperatures in the plant solarium can easily approach 100°, the care of the rhododendron seedlings, which are said to grow only at cool temperatures, has presented something of a problem. Id hate to kill it by moving it. Such care will help prevent them from becoming desiccated, which would cause too much transplant shock and possible loss of the tree. Water thoroughly and use Plant Starter to prevent transplant shock and to stimulate new root growth. Landscape help needed! Balled-and-burlapped Take extra care when planting balled-and-burlapped rhododendrons as they are more susceptible to transplant shock. Messages: 2,710 Likes Received: 0 Location: philly, pa, usa 6b. Azaleas are hardy in USDA zones 4 through 9, which is a very wide range as far as temperature. I live in the northeast and want to know when is the best time for me to transplant it. It is just easier to do when the plant is dormant. Here is a link that might be useful: Rhododendron Culture. Azaleas ...

Rhododendron liliiflorum (百合花杜鹃) is a rhododendron species native to Guangxi, Guizhou, Hunan, and southeast Yunnan, China, where it grows at altitudes of 2800-4500 meters. It is a shrub or small tree that grows to 3 m in height, with leathery, oblong leaves, 7-16 by 2-5 cm in size. Flowers are predominantly white. None recorded. Rhododendron liliiflorum, H. Léveillé, Repert. Spec. Nov. Regni Veg. 12: 102. 1913. The Plant List Flora of China Hirsutum. ...

This Japanese azalea is a hybridization between Rhododendron indcum and Rhododendron simsii and has a compact, low, spreading to rounded form that is twiggy and

Victor is a slow grower with a compact habit and bears an abundance of showy, vivid, light purplish-pink flowers in early April. The P.J.M. group of rhododendrons are smaller, growing to a height of 3 to 6 feet tall. Form is rounded and foliage is leathery and dark green until fall when it turns almost purplish.

Mutations in the small heat shock proteins α-crystallins have been linked to autosomal dominant cataracts in humans. Extensive studies in vitro have revealed a spectrum of alterations to the structure and function of these proteins including shifts in the size of the oligomer, modulation of subunit exchange and modification of their affinity to client proteins. Although mouse models of these mutants were instrumental in identifying changes in cellular proliferation and lens development, a direct comparative analysis of their effects on lens proteostasis has not been performed. Here, we have transgenically expressed cataract-linked mutants of αA- and αB-crystallin in the zebrafish lens to dissect the underlying molecular changes that contribute to the loss of lens optical properties. Zebrafish lines expressing these mutants displayed a range of morphological lens defects. Phenotype penetrance and severity were dependent on the mutation even in fish lines lacking endogenous α-crystallin. The ...