scholarly journals Differential interaction with TREM2 modulates microglial uptake of modified Aβ species

Glia ◽  
2021 ◽  
Vol 69 (12) ◽  
pp. 2917-2932
Author(s):  
Pranav Joshi ◽  
Florian Riffel ◽  
Kanayo Satoh ◽  
Masahiro Enomoto ◽  
Seema Qamar ◽  
...  
Keyword(s):  
Differential Interaction

scholarly journals Differential Interaction of Maize Root Ferredoxin:NADP+ Oxidoreductase with Photosynthetic and Non-Photosynthetic Ferredoxin Isoproteins

2000 ◽  
Vol 123 (3) ◽  
pp. 1037-1046 ◽  
Author(s):  
Yayoi Onda ◽  
Tomohiro Matsumura ◽  
Yoko Kimata-Ariga ◽  
Hitoshi Sakakibara ◽  
Tatsuo Sugiyama ◽  
...  
Keyword(s):  
Maize Root ◽  
Differential Interaction

Difference of MreBCD Complex Interactome in Salmonella Typhimurium ST19 and ST213 Genotypes on Pathogenesis and Stress Response Pathways

2021 ◽  
Vol 22 ◽  
Author(s):  
Reyna Cristina Zepeda-Gurrola ◽  
Gerardo Vázquez-Marrufo ◽  
Xianwu Guo ◽  
Isabel Cristina Rodríguez-Luna ◽  
Alejandro Sánchez-Varela ◽  
...  
Keyword(s):  
Stress Response ◽  
Bacterial Virulence ◽  
Eukaryotic Cells ◽  
Interaction Patterns ◽  
High Infection Rate ◽  
Differential Interaction ◽  
Sequence Variations ◽  
High Infection ◽  
Underlying Mechanisms

: Salmonella enterica is the etiological agent of salmonellosis, with a high infection rate worldwide. In Mexico, ST213 genotype of S. enterica ser. Typhimurium is displacing the ancestral ST19 genotype. Bacterial cytoskeleton protein complex MreBCD play an important role in S. enterica pathogenesis, but underlying mechanisms are unknown. In this study, 106 interactions among MreBCD and 15 proteins from S. Typhimurium Pathogenicity Islands 1 (SP-I) and 2 (SP-2) involved in both bacterial virulence and stress response were predicted in ST213 and ST19 genotypes, of which 12 interactions were confirmed in vitro. In addition, gene cluster analysis in 100 S. Typhimurium genomes was performed for these genes. The in silico and in vitro results showed a novel MreBCD interactome involved in the regulation of pathogenesis and stress response through interactions with virulence factors located at SPI-1 and SPI-2. Furthermore, both pseudogene presence and sequence variations in four tested proteins between genotypes resulted in differential interaction patterns that are involved in Salmonella motility and survival in eukaryotic cells, which could explain replacement of ST19 by ST213 in Mexico.

Differential Interaction ofR-Mexiletine with the Local Anesthetic Receptor Site on Brain and Heart Sodium Channel α-Subunits

1999 ◽  
Vol 56 (6) ◽  
pp. 1238-1244 ◽  
Author(s):  
Thomas Weiser ◽  
Yusheng Qu ◽  
William A. Catterall ◽  
Todd Scheuer
Keyword(s):  
Sodium Channel ◽  
Local Anesthetic ◽  
Receptor Site ◽  
Differential Interaction ◽  
Α Subunits

A Fluorescence Perspective on the Differential Interaction of Riboflavin and Flavin Adenine Dinucleotide with Cucurbit[7]uril

2010 ◽  
Vol 114 (33) ◽  
pp. 10717-10727 ◽  
Author(s):  
Sharmistha Dutta Choudhury ◽  
Jyotirmayee Mohanty ◽  
Achikanath C. Bhasikuttan ◽  
Haridas Pal
Keyword(s):  
Flavin Adenine Dinucleotide ◽  
Differential Interaction

A Differential Interaction of Doxorubicin and Daunorubicin with Human Serum Proteins

1981 ◽  
Vol 67 (5) ◽  
pp. 399-403 ◽  
Author(s):  
Franco Zunino ◽  
Romolo A. Gambetta ◽  
Adriano Zaccara ◽  
Roberto Carsana
Keyword(s):  
Human Serum ◽  
Reaction Mechanisms ◽  
Serum Proteins ◽  
Covalent Bond ◽  
Comparative Investigation ◽  
Experimental Conditions ◽  
Differential Interaction ◽  
Bound Drug ◽  
Human Serum Proteins

The results of a comparative investigation on the interaction of doxorubicin (adriamycin) and daunorubicin with serum proteins are reported. Whereas a strong interaction occurs in vitro between doxorubicin and human serum proteins, no appreciable binding to proteins could be detected for daunorubicin under similar experimental conditions. Since the protein-bound drug is only partially dissociated by physical procedures including gel-electrophoresis, column-chromatography and solvent extraction, the formation of a covalent bond is suggested. The doxorubicin binding to serum proteins is apparently nonselective for a class of proteins; it is strongly reduced in acid conditions and slightly dependent on the ionic strenght. Two tentative reaction mechanisms have been considered.

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