Protein mixtures of environmentally friendly zein to understand protein–protein interactions through biomaterials synthesis, hemolysis, and their antimicrobial activities

2014 ◽  
Vol 16 (27) ◽  
pp. 14257-14270 ◽  
Author(s):  
Aabroo Mahal ◽  
Manoj Kumar Goshisht ◽  
Poonam Khullar ◽  
Harsh Kumar ◽  
Narinder Singh ◽  
...  

Protein–protein interactions through biomaterials synthesis for biological applications.

2021 ◽  
Author(s):  
Ameya J. Limaye ◽  
George N. Bendzunas ◽  
Eileen Kennedy

Protein Kinase C (PKC) is a member of the AGC subfamily of kinases and regulates a wide array of signaling pathways and physiological processes. Protein-protein interactions involving PKC and its...


Author(s):  
Fabian Soltermann ◽  
Weston B. Struwe ◽  
Philipp Kukura

Protein–protein interactions are involved in the regulation and function of the majority of cellular processes.


2017 ◽  
Vol 13 (7) ◽  
pp. 1336-1344 ◽  
Author(s):  
Yan-Bin Wang ◽  
Zhu-Hong You ◽  
Xiao Li ◽  
Tong-Hai Jiang ◽  
Xing Chen ◽  
...  

Protein–protein interactions (PPIs) play an important role in most of the biological processes.


2016 ◽  
Vol 12 (4) ◽  
pp. 1378-1387 ◽  
Author(s):  
Meng-Chen Lu ◽  
Zhen-Wei Yuan ◽  
Yong-Lin Jiang ◽  
Zhi-Yun Chen ◽  
Qi-Dong You ◽  
...  

Protein–protein interactions (PPIs) as drug targets have been gaining growing interest, though developing drug-like small molecule PPI inhibitors remains challenging.


2018 ◽  
Vol 35 (10) ◽  
pp. 1082-1096 ◽  
Author(s):  
Greg J. Dodge ◽  
Finn P. Maloney ◽  
Janet L. Smith

Protein–protein interactions of cis-AT polyketide synthases are dominated by the travels of the ACP domain to the active site entrance of each catalytic domain.


Archaea ◽  
2004 ◽  
Vol 1 (4) ◽  
pp. 247-254 ◽  
Author(s):  
Thomas A. Hall ◽  
James W. Brown

A yeast two-hybrid system was used to identify protein–protein interactions between the ribonuclease P (RNase P) protein subunits Mth11p, Mth687p, Mth688p and Mth1618p from the archaeonMethanothermobacter thermoautotrophicus. Clear interactions between Mth688p and Mth687p, and between Mth1618p and Mth11p, were confirmed byHIS3andLacZreporter expression. Weaker interactions of Mth687p and Mth688p with Mth11p, and Mth11p with itself, are also suggested. These interactions resemble, and confirm, those previously seen among the homologs of these proteins in the more complex yeast RNase P holoenzyme.


2014 ◽  
Vol 118 (48) ◽  
pp. 28207-28219 ◽  
Author(s):  
Manoj Kumar Goshisht ◽  
Lovika Moudgil ◽  
Monika Rani ◽  
Poonam Khullar ◽  
Gurinder Singh ◽  
...  

RSC Advances ◽  
2018 ◽  
Vol 8 (2) ◽  
pp. 867-876 ◽  
Author(s):  
Noelle M. do Nascimento ◽  
Augusto Juste-Dolz ◽  
Paulo R. Bueno ◽  
Isidro Monzó ◽  
Roberto Tejero ◽  
...  

Protein–protein interactions are key in virtually all biological processes.


Micromachines ◽  
2019 ◽  
Vol 10 (3) ◽  
pp. 173
Author(s):  
Liang Wu ◽  
Baishu Liu ◽  
Meiling Zhu ◽  
Dameng Guo ◽  
Han Wu ◽  
...  

A method was developed to pattern the surface of perfluorinated materials with graphene oxide thin film, and various biological applications of the patterned perfluorinated surface were illustrated. Perfluorinated surfaces such as Teflon, Cytop, and other perfluorinated materials are known to be both hydrophobic and oleophobic, with low adhesion for most materials. Modifying the perfluorinated surfaces has been difficult due to the extraordinary chemical inertness, which limits the applications of perfluorinated materials as anti-fouling substrates. Herein we successfully patterned Cytop surfaces with graphene oxide. Patterns of the graphene oxide thin film with feature dimension down to 40 microns were formed and remained stable on the Cytop surface against washing with water, ethanol and acetone. The graphene oxide thin film on the Cytop surface allowed non-specific protein adsorption. To illustrate the applications of the patterned Cytop surface, we used the patterned Cytop surface as the substrate to study the protein-protein interactions, stem cell culture, and stem cell proliferation.


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