A Boronic Acid-Based Enrichment for Site-Specific Identification of the N-glycoproteome Using MS-Based Proteomics

2015 ◽  
pp. 31-41 ◽  
Author(s):  
Haopeng Xiao ◽  
George X. Tang ◽  
Weixuan Chen ◽  
Ronghu Wu
Keyword(s):  
Boronic Acid ◽  
Site Specific ◽  
Specific Identification

Site-Specific Identification of Lysine Acetylation Stoichiometries in Mammalian Cells

2016 ◽  
Vol 15 (3) ◽  
pp. 1103-1113 ◽  
Author(s):  
Tong Zhou ◽  
Ying-hua Chung ◽  
Jianji Chen ◽  
Yue Chen
Keyword(s):  
Mammalian Cells ◽  
Lysine Acetylation ◽  
Site Specific ◽  
Specific Identification

scholarly journals Site-Specific Identification of an Aβ Fibril-Heparin Interaction Site by Using Solid-State NMR Spectroscopy

2012 ◽  
Vol 124 (52) ◽  
pp. 13317-13320
Author(s):  
Jillian Madine ◽  
Maya J. Pandya ◽  
Matthew R. Hicks ◽  
Alison Rodger ◽  
Edwin A. Yates ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Site Specific ◽  
Specific Identification ◽  
Interaction Site ◽  
Solid State Nmr Spectroscopy ◽  
Heparin Interaction

scholarly journals A comparative ‘bottom up’ proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids

2012 ◽  
Vol 75 (18) ◽  
pp. 5724-5733 ◽  
Author(s):  
Bingnan Han ◽  
Michael Hare ◽  
Samanthi Wickramasekara ◽  
Yi Fang ◽  
Claudia S. Maier
Keyword(s):  
Bottom Up ◽  
Site Specific ◽  
Protein Modifications ◽  
Specific Identification ◽  
Electrophilic Lipids ◽  
Identification And Quantification

scholarly journals High-throughput and site-specific identification of 2′-O-methylation sites using ribose oxidation sequencing (RibOxi-seq)

RNA ◽  
2017 ◽  
Vol 23 (8) ◽  
pp. 1303-1314 ◽  
Author(s):  
Yinzhou Zhu ◽  
Stephan P. Pirnie ◽  
Gordon G. Carmichael
Keyword(s):  
High Throughput ◽  
Site Specific ◽  
Specific Identification

scholarly journals Comparative Biochemical and Computational Study of the Role of Naturally Occurring Mutations at Ambler Positions 104 and 170 in GES β-Lactamases

2010 ◽  
Vol 54 (11) ◽  
pp. 4864-4871 ◽  
Author(s):  
Stathis D. Kotsakis ◽  
Vivi Miriagou ◽  
Eva Tzelepi ◽  
Leonidas S. Tzouvelekis
Keyword(s):  
Boronic Acid ◽  
Computational Study ◽  
Dynamic Simulations ◽  
Site Specific ◽  
Catalytic Behavior ◽  
Naturally Occurring ◽  
Hydrolysis Rates ◽  
Hydrolysis Of ◽  
Precise Role

ABSTRACT In GES-type β-lactamases, positions 104 and 170 are occupied by Glu or Lys and by Gly, Asn, or Ser, respectively. Previous studies have indicated an important role of these amino acids in the interaction with β-lactams, although their precise role, especially that of residue 104, remains uncertain. In this study, we constructed GES-1 (Glu104, Gly170), GES-2 (Glu104, Asn170), GES-5 (Glu104, Ser170), GES-6 (Lys104, Ser170), GES-7 (Lys104, Gly170), and GES-13 (Lys104, Asn170) by site-specific mutagenesis and compared their hydrolytic properties. Isogenic comparisons of β-lactam resistance levels conferred by these GES variants were also performed. Data indicated the following patterns: (i) Lys104-containing enzymes exhibited enhanced hydrolysis of oxyimino-cephalosporins and reduced efficiency against imipenem in relation to enzymes possessing Glu104, (ii) Asn170-containing enzymes showed reduced hydrolysis rates of penicillins and older cephalosporins, (iii) Ser170 enabled GES to hydrolyze cefoxitin efficiently, and (iv) Asn170 and Ser170 increased the carbapenemase character of GES enzymes but reduced their activity against ceftazidime. Molecular dynamic simulations of GES apoenzyme models, as well as construction of GES structures complexed with cefoxitin and an achiral ceftazidime-like boronic acid, provided insights into the catalytic behavior of the studied mutants. There were indications that an increased stability of the hydrogen bonding network of Glu166-Lys73-Ser70 and an altered positioning of Trp105 correlated with the substrate spectra, especially with acylation of GES by imipenem. Furthermore, likely effects of Ser170 on GES interactions with cefoxitin and of Lys104 on interactions with oxyimino-cephalosporins were revealed. Overall, the data unveiled the importance of residues 104 and 170 in the function of GES enzymes.

scholarly journals Site-Specific Identification of an Aβ Fibril-Heparin Interaction Site by Using Solid-State NMR Spectroscopy

2012 ◽  
Vol 51 (52) ◽  
pp. 13140-13143 ◽  
Author(s):  
Jillian Madine ◽  
Maya J. Pandya ◽  
Matthew R. Hicks ◽  
Alison Rodger ◽  
Edwin A. Yates ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Site Specific ◽  
Specific Identification ◽  
Interaction Site ◽  
Solid State Nmr Spectroscopy ◽  
Heparin Interaction

scholarly journals Site specific identification of endogenous S-nitrosocysteine proteomes

2013 ◽  
Vol 92 ◽  
pp. 195-203 ◽  
Author(s):  
Paschalis-Thomas Doulias ◽  
Margarita Tenopoulou ◽  
Karthik Raju ◽  
Lynn A. Spruce ◽  
Steven H. Seeholzer ◽  
...  
Keyword(s):  
Site Specific ◽  
Specific Identification

scholarly journals Site-Specific Identification of SUMO-2 Targets in Cells Reveals an Inverted SUMOylation Motif and a Hydrophobic Cluster SUMOylation Motif

2010 ◽  
Vol 39 (4) ◽  
pp. 641-652 ◽  
Author(s):  
Ivan Matic ◽  
Joost Schimmel ◽  
Ivo A. Hendriks ◽  
Maria A. van Santen ◽  
Frans van de Rijke ◽  
...  
Keyword(s):  
Site Specific ◽  
Specific Identification ◽  
Hydrophobic Cluster ◽  
In Cells
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