scholarly journals Identification and Characterization of a Cleavage Site in the Proteolysis of Orf Virus 086 Protein

2016 ◽  
Vol 7 ◽  
Author(s):  
Xiaoping Wang ◽  
Bin Xiao ◽  
Jiafeng Zhang ◽  
Daxiang Chen ◽  
Wei Li ◽  
...  
Keyword(s):  
Cleavage Site ◽  
Orf Virus ◽  
Identification And Characterization

Identification and characterization of Orf virus 050 protein proteolysis

Virus Genes ◽  
2017 ◽  
Vol 53 (3) ◽  
pp. 400-409 ◽  
Author(s):  
Han Wang ◽  
Junyi Jiang ◽  
Rui Ding ◽  
Xiaoping Wang ◽  
Meiying Liao ◽  
...  
Keyword(s):  
Orf Virus ◽  
Identification And Characterization

Identification and Characterization of a Divalent Metal Ion-Dependent Cleavage Site in the Hammerhead Ribozyme†

Biochemistry ◽  
2001 ◽  
Vol 40 (46) ◽  
pp. 13849-13856 ◽  
Author(s):  
John C. Markley ◽  
Frédéric Godde ◽  
Snorri Th. Sigurdsson
Keyword(s):  
Cleavage Site ◽  
Metal Ion ◽  
Hammerhead Ribozyme ◽  
Divalent Metal ◽  
Divalent Metal Ion ◽  
Identification And Characterization

scholarly journals Identification and characterization of the orf virus type I topoisomerase

Virology ◽  
1995 ◽  
Vol 206 (1) ◽  
pp. 203-215 ◽  
Author(s):  
Nancy Klemperer ◽  
David J. Lyttle ◽  
Dominique Tauzin ◽  
Paula Traktman ◽  
Anthony J. Robinson
Keyword(s):  
Virus Type ◽  
Orf Virus ◽  
Type I ◽  
Identification And Characterization

Identification and Characterization of an Orf Virus Homologue of the Vaccinia Virus Gene Encoding the Major Envelope Antigen p37K

Virology ◽  
1994 ◽  
Vol 202 (2) ◽  
pp. 968-973 ◽  
Author(s):  
John T. Sullivan ◽  
Andrew A. Mercer ◽  
Stephen B. Fleming ◽  
Anthony J. Robinson
Keyword(s):  
Vaccinia Virus ◽  
Orf Virus ◽  
Gene Encoding ◽  
Virus Gene ◽  
Identification And Characterization ◽  
Envelope Antigen

Identification and characterization of monoclonal antibodies against the ORFV059 protein encoded by Orf virus

Virus Genes ◽  
2012 ◽  
Vol 44 (3) ◽  
pp. 429-440 ◽  
Author(s):  
Hong Li ◽  
Zhangyong Ning ◽  
Wenbo Hao ◽  
Shimeng Zhang ◽  
Xiaoqing Liao ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Orf Virus ◽  
Identification And Characterization

scholarly journals Identification of the Murine Coronavirus MP1 Cleavage Site Recognized by Papain-Like Proteinase 2

2003 ◽  
Vol 77 (13) ◽  
pp. 7376-7382 ◽  
Author(s):  
Amornrat Kanjanahaluethai ◽  
Dalia Jukneliene ◽  
Susan C. Baker
Keyword(s):  
Cleavage Site ◽  
Edman Degradation ◽  
Putative Cleavage Site ◽  
Amino Terminal ◽  
Cleavage Assay ◽  
Degradation Reaction ◽  
Methionine Residues ◽  
Identification And Characterization ◽  
Murine Coronavirus

ABSTRACT The replicase polyprotein of murine coronavirus is extensively processed by three proteinases, two papain-like proteinases (PLPs), termed PLP1 and PLP2, and a picornavirus 3C-like proteinase (3CLpro). Previously, we established a trans-cleavage assay and showed that PLP2 cleaves the replicase polyprotein between p210 and membrane protein 1 (MP1) (A. Kanjanahaluethai and S. C. Baker, J. Virol. 74:7911-7921, 2000). Here, we report the results of our studies identifying and characterizing this cleavage site. To determine the approximate position of the cleavage site, we expressed constructs that extended various distances upstream from the previously defined C-terminal end of MP1. We found that the construct extending from the putative PLP2 cleavage site at glycine 2840-alanine 2841 was most similar in size to the processed MP1 replicase product generated in a trans-cleavage assay. To determine which amino acids are critical for PLP2 recognition and processing, we generated 14 constructs with amino acid substitutions upstream and downstream of the putative cleavage site and assessed the effects of the mutations in the PLP2 trans-cleavage assay. We found that substitutions at phenylalanine 2835, glycine 2839, or glycine 2840 resulted in a reduction in cleavage of MP1. Finally, to unequivocally identify this cleavage site, we isolated radiolabeled MP1 protein and determined the position of [35S]methionine residues released by Edman degradation reaction. We found that the amino-terminal residue of MP1 corresponds to alanine 2841. Therefore, murine coronavirus PLP2 cleaves the replicase polyprotein between glycine 2840 and alanine 2841, and the critical determinants for PLP2 recognition and processing occupy the P6, P2, and P1 positions of the cleavage site. This study is the first report of the identification and characterization of a cleavage site recognized by murine coronavirus PLP2 activity.

Identification and characterization of peptidases secreted by quahog parasite unknown (QPX), the protistan parasite of hard clams

2016 ◽  
Vol 122 (1) ◽  
pp. 21-33 ◽  
Author(s):  
E Rubin ◽  
GT Werneburg ◽  
E Pales Espinosa ◽  
DG Thanassi ◽  
B Allam
Keyword(s):  
Quahog Parasite Unknown ◽  
Hard Clams ◽  
Identification And Characterization

Identification and characterization of Vibrio harveyi associated with diseased abalone Haliotis diversicolor

2013 ◽  
Vol 103 (2) ◽  
pp. 133-139 ◽  
Author(s):  
Q Jiang ◽  
L Shi ◽  
C Ke ◽  
W You ◽  
J Zhao
Keyword(s):  
Vibrio Harveyi ◽  
Haliotis Diversicolor ◽  
Identification And Characterization

IDENTIFICATION AND CHARACTERIZATION OF 1,2-BN CYCLOHEXENE USING MICROWAVE SPECTROSCOPY

2016 ◽  
Author(s):  
Stephen Kukolich ◽  
Shih-Yuan Liu ◽  
Jacob Ishibashi ◽  
Adam Daly ◽  
Ming Sun
Keyword(s):  
Microwave Spectroscopy ◽  
Identification And Characterization

Identification and characterization of a CRM1/XPO1-dependent nuclear export signal in the human androgen receptor

2016 ◽  
Author(s):  
Stefanie V Schutz ◽  
Axel Merseburger ◽  
Anca Azoitei ◽  
Marcus V Cronauer
Keyword(s):  
Androgen Receptor ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Export Signal ◽  
Identification And Characterization ◽  
Human Androgen Receptor
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