Computational analysis of heat shock protein (HSP) in Citrus X Sinensis
نویسندگان
چکیده
Heat shock proteins (HSPs) are molecular chaperones and one of the cell’s most important regulatory present in all species. HSPs a multigene family classified into six families according to their weight range between 8KDa 110KDa: HSP100, HSP90, HSP70, HSP60, small heat (sHSPs), ubiquitin. Citrus X Sinensis is very economical, widely grown world. It best sources nutrition, vitamin C, fiber, thiamine, folate, antioxidants. has variety health benefits i.e., protects against cell damage, boosts immune system, heals wounds, etc. For highlighting aspect citrus computing protein, this work great significance. Present studies based on identification characterization sinuses. In silico research was performed; Arabidopsis thaliana protein sequences HSP70 HSP90 were used as reference identify these sinuses through Blast Phytozome. Furthermore, physiochemical properties, multiple sequence alignment, Multiple Expectation Maximization for Motif Elicitation (MEME) phylogeny constructed 44 22 23 HSP90. The expression found Endoplasmic Reticulum. findings provide good understanding families' function site also provides basic knowledge further investigations putative structure dynamic proteins.
منابع مشابه
Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease.
Polyglutamine (polygln) diseases are a group of inherited neurodegenerative disorders characterized by protein misfolding and aggregation. Here, we investigate the role in polygln disease of heat shock proteins (Hsps), the major class of molecular chaperones responsible for modulating protein folding in the cell. In transfected COS7 and PC12 neural cells, we show that Hsp40 and Hsp70 chaperones...
متن کاملLevels of Antibodies against Human Heat Shock Protein (HSP) 60 in Patients with Glaucoma in Poland
BACKGROUND Although elevated intraocular pressure is a major risk factor for the development of glaucoma, there is increasing evidence that the immune system may be involved in the development of normal-tension glaucoma (NTG). The aim of this study was to determine if NTG is associated with elevated levels of antibodies against human heat shock protein (HSP) 60. MATERIAL AND METHODS The study...
متن کاملEvaluation of heat shock protein (HSP-72) expression in retinal ganglion cells of rats with glaucoma
The present study was planned to observe the expression of heat shock protein 72 (HSP72) in retina of rats in a glaucoma model. A total of 50 Wistar rats were randomly divided into the high intraocular tension group (glaucoma model) and the sham control (sham operation) group. Glaucoma rat models were created by application of electrocoagulation on at least three groups of veins, reduction of v...
متن کاملAntisense oligonucleotide inhibition of Heat Shock Protein (HSP) 47 improves bleomycin-induced pulmonary fibrosis in rats
BACKGROUND The most common pathologic form of pulmonary fibrosis arises from excessive deposition of extracellular matrix proteins such as collagen. The 47 kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen. OBJECTIVES To determine whether inhibition of HSP47 could have ben...
متن کاملDiminished phosphorylation of a heat shock protein (HSP 27) in infant acute lymphoblastic leukemia.
We have previously reported lack of expression of a polypeptide designated L3 in infant acute lymphoblastic leukemia (ALL). Expression of L3 occurred predominantly in older children with pre-B ALL. We have recently reported the expression during B cell ontogeny of two other polypeptides, designated L2 and L4 with a similar Mr as L3, which were identified as phosphorylated and non-phosphorylated...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: World journal of biology and biotechnology
سال: 2023
ISSN: ['2522-6746', '2522-6754']
DOI: https://doi.org/10.33865/wjb.008.02.0926