Label-free sensing and atomic force spectroscopy for the characterization of protein-DNA and protein-protein interactions: application to estrogen receptors

2011 ◽  
Vol 24 (3) ◽  
pp. 429-435 ◽  
Author(s):  
A. Berthier ◽  
C. Elie-Caille ◽  
E. Lesniewska ◽  
R. Delage-Mourroux ◽  
W. Boireau
Keyword(s):  
Estrogen Receptors ◽  
Protein Interactions ◽  
Force Spectroscopy ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

scholarly journals Unraveling protein–protein interactions in clathrin assemblies via atomic force spectroscopy

Methods ◽  
2013 ◽  
Vol 59 (3) ◽  
pp. 316-327 ◽  
Author(s):  
Albert J. Jin ◽  
Eileen M. Lafer ◽  
Jennifer Q. Peng ◽  
Paul D. Smith ◽  
Ralph Nossal
Keyword(s):  
Protein Interactions ◽  
Force Spectroscopy ◽  
Protein Protein Interactions ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

scholarly journals Label-free methods for optical in vitro characterization of protein–protein interactions

2021 ◽  
Author(s):  
Fabian Soltermann ◽  
Weston B. Struwe ◽  
Philipp Kukura
Keyword(s):  
Protein Interactions ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Cellular Processes ◽  
P Protein ◽  
In Vitro Characterization ◽  
And Function

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

Atomic force spectroscopy-based study of antibody pesticide interactions for characterization of immunosensor surface

2004 ◽  
Vol 20 (2) ◽  
pp. 284-293 ◽  
Author(s):  
Jasdeep Kaur ◽  
Kanwar Vikas Singh ◽  
Ashwini Hirlekar Schmid ◽  
Grish C Varshney ◽  
C.Raman Suri ◽  
...  
Keyword(s):  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

scholarly journals Developing Nanodisc-ID for label-free characterizations of membrane proteins

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Huan Bao
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Gel Electrophoresis ◽  
Low Cost ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Peripheral Membrane Proteins ◽  
Wide Range ◽  
Neural Transmission

AbstractMembrane proteins (MPs) influence all aspects of life, such as tumorigenesis, immune response, and neural transmission. However, characterization of MPs is challenging, as it often needs highly specialized techniques inaccessible to many labs. We herein introduce nanodisc-ID that enables quantitative analysis of membrane proteins using a gel electrophoresis readout. By leveraging the power of nanodiscs and proximity labeling, nanodisc-ID serves both as scaffolds for encasing biochemical reactions and as sensitive reagents for detecting membrane protein-lipid and protein-protein interactions. We demonstrate this label-free and low-cost tool by characterizing a wide range of integral and peripheral membrane proteins from prokaryotes and eukaryotes.

Dysfunction of endothelial cells exposed to nanomaterials assessed by atomic force spectroscopy

Micron ◽  
2021 ◽  
Vol 145 ◽  
pp. 103062
Author(s):  
Agnieszka Maria Kolodziejczyk ◽  
Paulina Sokolowska ◽  
Aleksandra Zimon ◽  
Magdalena Grala ◽  
Marcin Rosowski ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

scholarly journals Analysis of Zika virus capsid-Aedes aegypti mosquito interactome reveals pro-viral host factors critical for establishing infection

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Rommel J. Gestuveo ◽  
Jamie Royle ◽  
Claire L. Donald ◽  
Douglas J. Lamont ◽  
Edward C. Hutchinson ◽  
...  
Keyword(s):  
Aedes Aegypti ◽  
Protein Interactions ◽  
Zika Virus ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Zikv Infection ◽  
Ubiquitin Protein Ligase ◽  
Mosquito Cells ◽  
Endoplasmic Reticulum Protein ◽  
Arboviral Diseases

AbstractThe escalating global prevalence of arboviral diseases emphasizes the need to improve our understanding of their biology. Research in this area has been hindered by the lack of molecular tools for studying virus-mosquito interactions. Here, we develop an Aedes aegypti cell line which stably expresses Zika virus (ZIKV) capsid proteins in order to study virus-vector protein-protein interactions through quantitative label-free proteomics. We identify 157 interactors and show that eight have potentially pro-viral activity during ZIKV infection in mosquito cells. Notably, silencing of transitional endoplasmic reticulum protein TER94 prevents ZIKV capsid degradation and significantly reduces viral replication. Similar results are observed if the TER94 ortholog (VCP) functioning is blocked with inhibitors in human cells. In addition, we show that an E3 ubiquitin-protein ligase, UBR5, mediates the interaction between TER94 and ZIKV capsid. Our study demonstrates a pro-viral function for TER94/VCP during ZIKV infection that is conserved between human and mosquito cells.

scholarly journals Genetic and Molecular Characterization of the Caenorhabditis elegans Gene, mel-26, a Postmeiotic Negative Regulator of MEI-1, a Meiotic-Specific Spindle Component

Genetics ◽  
1998 ◽  
Vol 150 (1) ◽  
pp. 119-128
Author(s):  
M Rhys Dow ◽  
Paul E Mains
Keyword(s):  
Caenorhabditis Elegans ◽  
Protein Interactions ◽  
Negative Regulator ◽  
Meiotic Spindle ◽  
Loss Of Function ◽  
Protein Protein Interactions ◽  
Gain Of Function ◽  
Recessive Mutations ◽  
Female Germline

Abstract We have previously described the gene mei-1, which encodes an essential component of the Caenorhabditis elegans meiotic spindle. When ectopically expressed after the completion of meiosis, mei-1 protein disrupts the function of the mitotic cleavage spindles. In this article, we describe the cloning and the further genetic characterization of mel-26, a postmeiotic negative regulator of mei-1. mel-26 was originally identified by a gain-of-function mutation. We have reverted this mutation to a loss-of-function allele, which has recessive phenotypes identical to the dominant defects of its gain-of-function parent. Both the dominant and recessive mutations of mel-26 result in mei-1 protein ectopically localized in mitotic spindles and centrosomes, leading to small and misoriented cleavage spindles. The loss-of-function mutation was used to clone mel-26 by transformation rescue. As suggested by genetic results indicating that mel-26 is required only maternally, mel-26 mRNA was expressed predominantly in the female germline. The gene encodes a protein that includes the BTB motif, which is thought to play a role in protein-protein interactions.

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