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Molecular chaperones
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Ebook "Networking of chaperones by co-chaperones" describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets.
152p
ladongphongthanh1008
22-04-2024
4
4
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Ebook "Folding for the synapse" addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Molecular chaperones have been studied in relation to de novo protein folding, but there is increasing awareness that chaperone function is required for the regulation of protein dynamics when functioning physiologically as an isolated moiety or part of a protein complex.
315p
tracanhphuonghoa1007
22-04-2024
3
2
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Ebook "Molecular chaperones (Topics in Current chemistry, 328)" describes all three families of known peptidyl prolyl isomerases (PPIases) including the FKBPs, cyclophilins and parvulins. These chaperones catalyse conformational interconversions of peptide bonds which can be critical to the correct folding of many proteins. The structural and chemical features of PPIases and the catalytic cycle are described, and a discussion of chaperoning versus catalysis is also included.
281p
coduathanh1122
27-03-2024
5
1
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Ebook "Protein misfolding, aggregation, and conformational diseases - Part A: Protein aggregation and conformational diseases" fills the gap in protein review and protocal literature while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders.
450p
cotieubac1004
15-03-2024
1
0
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In ebook "Molecular aspects of the stress response: Chaperones, membranes and networks (Advances in experimental medicine and biology, Volume 594)" the reader will learn the role of chaperone classes such as Hsp27 or Hsp90, the action of highly organized chaperone networks in various cellular compartments such as the ER or mitochondrial/ER networks as well as the molecular details of the signaling mechanisms leading to chaperone induction during stress.
218p
tachieuhoa
28-01-2024
3
2
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In ebook "Heat shock protein inhibitors: Success stories" the science of medicinal chemistry offers mankind one of its best hopes for improving the quality of life. The art of medicinal chemistry continues to challenge its practitioners with the need for both intuition and experience to discover new drugs. Hence sharing the experience of drug research is uniquely beneficial to the field of medicinal chemistry.
243p
lamquandat
28-12-2023
5
2
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Fungal fruiting bodies are complex three-dimensional structures that are formed to protect and disperse the sexual spores. Their morphogenesis requires the concerted action of numerous genes; however, at the molecular level, the spatio-temporal sequence of events leading to the mature fruiting body is largely unknown.
21p
vihagrid
30-01-2023
4
3
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Small heat shock proteins (sHSPs) belong to the class of molecular chaperones that respond to biotic and abiotic stresses in plants. A previous study has showed strong induction of the gene GmHsp22.4 in response to the nematode Meloidogyne javanica in a resistant soybean genotype, while repression in a susceptible one.
12p
vijichea2711
28-05-2021
15
1
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Pirfenidone is a novel anti-fibrotic and anti-inflammatory agent that inhibits the progression of fibrosis in animal models and in patients with idiopathic pulmonary fibrosis (IPF). We previously showed that pirfenidone inhibits the over-expression of collagen type I and of heat shock protein (HSP) 47, a collagen-specific molecular chaperone, in human lung fibroblasts stimulated with transforming growth factor (TGF)-β1 in vitro.
9p
vianthony2711
16-04-2021
7
1
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Heat shock protein (HSP) 47, a collagen-specific molecular chaperone, is involved in the processing and/or secretion of procollagen. We hypothesized that HSP47 could be a useful marker for fibrotic lung disease. The aim of this study was to evaluate serum levels of HSP47 in patients with various idiopathic interstitial pneumonias (IIPs).
8p
vimontana2711
05-04-2021
9
1
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Temperature affects virtually all cellular processes. A quick increase in temperature challenges the cells to undergo a heat shock response to maintain cellular homeostasis. Heat shock factor-1 (HSF-1) functions as a major player in this response as it activates the transcription of genes coding for molecular chaperones (also called heat shock proteins) that maintain structural integrity of proteins.
12p
vimariana2711
22-12-2020
8
0
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Coilia nasus oogenesis/spawning migration is a well-defined synchronous arrangement process. DnaJs are indispensable molecular chaperones for oogenesis process. However, how DnaJs involved the anadromous spawning migration mechanism is outstanding and plausible.
11p
viwyoming2711
16-12-2020
10
1
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Phosphorylation is one of the most important post-translational modifications (PTM) employed by cells to regulate several cellular processes. Studying the effects of phosphorylations on protein structures allows to investigate the modulation mechanisms of several proteins including chaperones, like the small HSPs, which display different multimeric structures according to the phosphorylation of a few serine residues.
10p
vioklahoma2711
19-11-2020
11
1
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The Bag (Bcl-2 associated athanogene) family of proteins consists of 6 members sharing a common, single-copied Bag domain through which they interact with the molecular chaperone Hsp70. Bag5 represents an exception in the Bag family since it consists of 5 Bag domains covering the whole protein.
11p
vijisoo2711
29-09-2020
8
1
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Heat shock protein (Hsp) 90 and Hsp70 are indispensable for cell survival under conditions of stress. They bind to client proteins to assist in protein stabilization, translocation of polypeptides across the cell membrane, and recovery of proteins from aggregates in the cell.
12p
vilisa271
22-09-2020
31
1
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Tomato leaf curl virus (ToLCV) is a very important pathogen in the tomato grown belt of India and world as a whole. It persist wide diversity and many isolate has been identified however molecular marker has represented its usability for the same. ToLCV can’t transmit by itself, it require a vector for the transmission and Bemisia tabaci serve the purpose. This vector has a vast host range and show a wide diversity. Many biotypes were identified based on their morphological characteristics and RAPD–PCR analysis viz B, Q, Cv biotypes.
10p
trinhthamhodang7
31-08-2020
19
1
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Undifferentiated pleomorphic sarcoma (UPS) is a heterogeneous tumor group, and little is known about molecular target therapy for UPS. Heat shock protein 90 (HSP90) is an expressed chaperone that refolds certain denatured proteins under stress conditions.
11p
vimoscow2711
29-08-2020
9
2
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Heat Shock Protein 70 (HSP70) is one of the important molecular chaperon that can protect cells from thermal damage by involving in the maintenance of the intra cellular homeostasis primarily by controlling the process of protein folding. The indigenous breeds of cattle have been found to be more resistant to heat stress in comparison to the exotic breeds by way of expressing HSP70 as an adaptive response.
9p
nguaconbaynhay7
15-08-2020
12
1
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For several decades now an antagonism between Trypanosoma cruzi infection and tumor development has been detected. The molecular basis of this phenomenon remained basically unknown until our proposal that T. cruzi Calreticulin (TcCRT), an endoplasmic reticulum-resident chaperone, translocated-externalized by the parasite, may mediate at least an important part of this effect.
12p
vimale2711
25-08-2020
16
2
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Due to the lack of effective therapies and poor prognosis in TNBC (triple-negative breast cancer) patients, there is a strong need to develop effective novel targeted therapies for this subtype of breast cancer. Inhibition of heat shock protein 90 (HSP90), a conserved molecular chaperone that is involved in the regulation of oncogenic client proteins, has shown to be a promising therapeutic approach for TNBC.
14p
viputrajaya2711
22-06-2020
7
0
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