[38] Glycoprotein processing enzymes of plants

1989 ◽  
pp. 452-475 ◽  
Author(s):  
Gur P. Kaushal ◽  
Alan D. Elbein
Keyword(s):  
Processing Enzymes ◽  
Glycoprotein Processing

Effects of Macromolecular Crowding on Glycoprotein Processing Enzymes

2008 ◽  
Vol 130 (6) ◽  
pp. 2101-2107 ◽  
Author(s):  
Kiichiro Totani ◽  
Yoshito Ihara ◽  
Ichiro Matsuo ◽  
Yukishige Ito
Keyword(s):  
Macromolecular Crowding ◽  
Processing Enzymes ◽  
Glycoprotein Processing

Synthesis of oligosaccharide substrates for N-linked glycoprotein processing enzymes

1995 ◽  
Vol 271 (2) ◽  
pp. 185-196 ◽  
Author(s):  
Rakesh K. Jain ◽  
Xiao-Gao Liu ◽  
Subba Rao Oruganti ◽  
E.V. Chandrasekaran ◽  
Khushi L. Matta
Keyword(s):  
Processing Enzymes ◽  
Glycoprotein Processing

Naturally Occurring Pyrrolizidines: Inhibition of α-Glucosidase 1 and Anti-HIV Activity of One Stereoisomer

1992 ◽  
Vol 3 (5) ◽  
pp. 273-277 ◽  
Author(s):  
D. L. Taylor ◽  
R. Nash ◽  
L. E. Fellows ◽  
M. S. Kang ◽  
A. S. Tyms
Keyword(s):  
Inhibitory Activity ◽  
Pyrrolizidine Alkaloid ◽  
Virus Growth ◽  
Processing Enzymes ◽  
Naturally Occurring ◽  
Antiviral Effects ◽  
Castanospermum Australe ◽  
Glycoprotein Processing ◽  
Anti Hiv ◽  
Hiv 1

Alexine, a naturally occurring pyrrolizidine alkaloid, isolated from Alexa leiopetala, and four stereoisomers, isolated from Castanospermum australe, were investigated for inhibitory activity against the growth of HIV-1. Only treatment with the 7,7a-diepialexine restricted virus growth (IC50 0.38 mm) although it was less active than the indolizidine alkaloid castanospermine (IC50 0.02 mm). The antiviral effects of 7,7a-diepialexine, like castanospermine, correlated with the inhibitory activity against purified pig kidney α-glucosidase 1 of the glycoprotein processing enzymes and the reduced cleavage of the precursor HIV-1 glycoprotein gp160.

Unique nCoV-2019 (COVID 19) spike glycoprotein processing by host protease: Analysis and Implication on infection

2020 ◽  
Vol 17 ◽  
Author(s):  
Ajoy Basak ◽  
Sarmistha Basak
Keyword(s):  
World Health ◽  
Spike Glycoprotein ◽  
Binding Domains ◽  
Corona Virus ◽  
Global Pandemic ◽  
High Infection ◽  
Crucial Information ◽  
Glycoprotein Processing ◽  
Health Organization ◽  
Host Reservoir

: The current global pandemic outbreak of a novel type of corona virus termed by World Health Organization as COVID-19 became an grave concern and worry to human health and world economy. Intense research efforts are now underway worldwide to combat and prevent the spread of this deadly disease. This zoonotic virus, a native to bat population is most likely transmitted to human via a host reservoir. Due to its close similarity to previously known SARS CoV (Severe Acute Respiratory Syndrome Corona Virus) of 2002 and related MERS CoV (Middle East Respiratory Syndrome Corona Virus) of 2012, it is also known as SARS CoV2. But unlike them it is far too infectious, virulent and lethal. Among its various proteins, the surface spike glycoprotein “S” has drawn significant attention because of its implication in viral recognition and host-virus fusion process. A detail comparative analysis of “S” proteins of SARS CoV (now called SARS CoV1), SARS CoV2 (COVID-19) and MERS CoV based on structure, sequence alignment, host cleavage sites, receptor binding domains, potential glycosylation and Cys-disulphide bridge locations has been performed. It revealed some key features and variations that may elucidate the high infection and virulence character of COVID-19. Moreover this crucial information may become useful in our quest for COVID-19 therapeutics and vaccines.

Glycoprotein processing in mutants of HSV-1 that induce cell fusion

Virology ◽  
1982 ◽  
Vol 117 (2) ◽  
pp. 293-306 ◽  
Author(s):  
Stanley Person ◽  
Konstantin G. Kousoulas ◽  
Robert W. Knowles ◽  
G. Sullivan Read ◽  
Thomas C. Holland ◽  
...  
Keyword(s):  
Cell Fusion ◽  
Glycoprotein Processing ◽  
Hsv 1

scholarly journals Repair of DNA Strand Breaks by the Overlapping Functions of Lesion-Specific and Non-Lesion-Specific DNA 3′ Phosphatases

2001 ◽  
Vol 21 (21) ◽  
pp. 7191-7198 ◽  
Author(s):  
John R. Vance ◽  
Thomas E. Wilson
Keyword(s):  
Dna Damage ◽  
Oxidative Dna Damage ◽  
Synthetic Lethality ◽  
Dna Strand Breaks ◽  
Triple Mutant ◽  
Phosphatase Domain ◽  
Strand Breaks ◽  
Alternative Pathways ◽  
Processing Enzymes ◽  
Dna Strand

ABSTRACT In Saccharomyces cerevisiae, the apurinic/apyrimidinic (AP) endonucleases Apn1 and Apn2 act as alternative pathways for the removal of various 3′-terminal blocking lesions from DNA strand breaks and in the repair of abasic sites, which both result from oxidative DNA damage. Here we demonstrate that Tpp1, a homologue of the 3′ phosphatase domain of polynucleotide kinase, is a third member of this group of redundant 3′ processing enzymes. Unlike Apn1 and Apn2, Tpp1 is specific for the removal of 3′ phosphates at strand breaks and does not possess more general 3′ phosphodiesterase, exonuclease, or AP endonuclease activities. Deletion ofTPP1 in an apn1 apn2 mutant background dramatically increased the sensitivity of the double mutant to DNA damage caused by H2O2 and bleomycin but not to damage caused by methyl methanesulfonate. The triple mutant was also deficient in the repair of 3′ phosphate lesions left by Tdp1-mediated cleavage of camptothecin-stabilized Top1-DNA covalent complexes. Finally, the tpp1 apn1 apn2 triple mutation displayed synthetic lethality in combination with rad52, possibly implicating postreplication repair in the removal of unrepaired 3′-terminal lesions resulting from endogenous damage. Taken together, these results demonstrate a clear role for the lesion-specific enzyme, Tpp1, in the repair of a subset of DNA strand breaks.

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