Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Rajan K. Tripathy"'
Publikováno v:
The Scientific World Journal, Vol 2014 (2014)
Human PON1 (h-PON1) is a multifaceted enzyme and can hydrolyze (and inactivate) a wide range of substrates. The enzyme shows anti-inflammatory, antioxidative, antiatherogenic, ant-diabetic, antimicrobial, and organophosphate (OP)-detoxifying properti
Externí odkaz:
https://doaj.org/article/50b05939f8794a4a95d05f0662cc8fed
Autor:
Geetika Aggarwal, Rameshwar Prajapati, Rajan K Tripathy, Priyanka Bajaj, A R Satvik Iyengar, Abhay T Sangamwar, Abhay H Pande
Publikováno v:
PLoS ONE, Vol 11, Iss 2, p e0147999 (2016)
Human paraoxonase 1 (h-PON1) is a serum enzyme that can hydrolyze a variety of substrates. The enzyme exhibits anti-inflammatory, anti-oxidative, anti-atherogenic, anti-diabetic, anti-microbial and organophosphate-hydrolyzing activities. Thus, h-PON1
Externí odkaz:
https://doaj.org/article/64d5a5198b80438fbdb76b5448dfeb6e
Autor:
Geetika Aggarwal, Rajan K. Tripathy, Abhay H. Pande, Prasad V. Bharatam, Priyanka Bajaj, Deepika Kathuria
Publikováno v:
Applied Biochemistry and Biotechnology. 182:1642-1662
Human paraoxonase 1 (h-PON1) is a ~45-kDa serum enzyme that can hydrolyze a variety of substrates, including organophosphate (OP) compounds. It is a potential candidate for the development of antidote against OP poisoning in humans. However, insuffic
Autor:
Priyanka Bajaj, Abhay H. Pande, Shyam S. Sharma, Rajan K. Tripathy, Geetika Aggarwal, Ashok Kumar Datusalia
Publikováno v:
Applied Biochemistry and Biotechnology. 180:165-176
Organophosphate (OP) compounds are neurotoxic chemicals, and current treatments available for OP-poisoning are considered as unsatisfactory and inadequate. There is an urgent need for the development of more effective treatment(s) for OP-poisoning. H
Publikováno v:
Protein & Peptide Letters. 22:1098-1103
SsoPox, a ~35 kDa enzyme from Sulfolobus solfataricus, can hydrolyze and inactivate a variety of organophosphate (OP)-compounds. The enzyme is a potential candidate for the development of prophylactic and therapeutic agent against OP-poisoning in hum
Publikováno v:
Protein Expression and Purification. 115:95-101
Human PON1 (h-PON1) is a Ca(2+)-dependent serum enzyme and can hydrolyze (and inactivate) a wide range of substrates. It is a multifaceted enzyme and exhibit anti-inflammatory, anti-oxidative, anti-atherogenic, anti-diabetic, anti-microbial, and orga
Autor:
Uttam Chand Banerjee, Madaka Surya Teja, Mukesh Kumar, Abhay H. Pande, Dharam Pal, Rajan K. Tripathy
Recombinant human interferon-β (rhIFN-β), a therapeutic protein, is produced using both prokaryotic and eukaryotic expression systems. However, instability of recombinant plasmid during cultivation of Escherichia coli results in low yield of the re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96b3b9b06a139d394020763d23163cca
https://europepmc.org/articles/PMC5745201/
https://europepmc.org/articles/PMC5745201/
Publikováno v:
Protein Expression and Purification. 113:56-62
AiiA is a "28-kDa lactonase" from Gram-positive Bacillus sp. 240B1. The enzyme can hydrolyze and inactivate a variety of acyl homoserine lactones (AHLs), quorum sensor molecules involve in bacterial quorum sensing (QS). AiiA is a strong candidate for
Publikováno v:
Biochimie. 105:202-210
Human paraoxonase 1 (h-PON1) is a Ca2+-dependent serum enzyme that catalyzes the hydrolysis of different types of substrates. The crystal structure of h-PON1 is not solved yet and the molecular details of how the enzyme catalyzes different types of r
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1831:1714-1720
Paraoxonase 1 (PON1) is an HDL-associated enzyme and exhibits anti-inflammatory, anti-diabetic, and anti-atherogenic properties. Association of PON1 to HDL particles increases the stability and activity of PON1 and is important for the normal functio