Results 281 to 290 of about 10,718,710 (345)

Potential Proteins Associated with Canine Epididymal Sperm Motility. [PDF]

Cells
Mogielnicka-Brzozowska M, Cichowska-Likszo AW, Likszo P, Fraser L, Popielarczyk W, Pieklik J, Kamińska M, Luvoni GC.   +7 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Protein–protein interactions

Biochemical Society Transactions, 2010
In the present article, we describe the two standard high-throughput methods for identification of protein complexes: two-hybrid screens and TAP (tandem affinity purification) tagging. These methods have been used to characterize the interactome of Saccharomyces cerevisiae, showing that the majority of proteins are part of complexes, and that complexes
Williamson, Mike P., Sutcliffe, Michael J.   +1 more
openaire   +3 more sources

DISCOVERING PROTEIN–PROTEIN INTERACTIONS

Journal of Bioinformatics and Computational Biology, 2004
The ongoing genomics and proteomics efforts have helped identify many new genes and proteins in living organisms. However, simply knowing the existence of genes and proteins does not tell us much about the biological processes in which they participate. Many major biological processes are controlled by protein interaction networks.
See-Kiong, Ng, Soon-Heng, Tan
openaire   +2 more sources

Analyzing Protein–Protein Interaction Networks

Journal of Proteome Research, 2012
The advent of the "omics" era in biology research has brought new challenges and requires the development of novel strategies to answer previously intractable questions. Molecular interaction networks provide a framework to visualize cellular processes, but their complexity often makes their interpretation an overwhelming task.
Koh GC, Porras P, Aranda B, Hermjakob H, Orchard SE.   +4 more
openaire   +2 more sources

Protein-catalysed protein folding

Trends in Biotechnology, 1990
A number of proteins, termed chaperonins, have been identified as part of the mechanism of folding other proteins into their biologically active forms. The role of chaperonins appears to be twofold--to prevent illegitimate interactions with other proteins and to facilitate folding, possibly through an energy-dependent, catalytic function.
A L, Horwich, W, Neupert, F U, Hartl
openaire   +2 more sources

Protein myristoylation in protein–lipid and protein–protein interactions

Biophysical Chemistry, 1999
Various proteins in signal transduction pathways are myristoylated. Although this modification is often essential for the proper functioning of the modified protein, the mechanism by which the modification exerts its effects is still largely unknown. Here we discuss the roles played by protein myristoylation, in both protein-lipid and protein-protein ...
openaire   +2 more sources

Measuring protein—protein interactions

Current Opinion in Structural Biology, 1998
The binding of one protein to another provokes a variety of biophysical changes that can then be used as a measure of the binding reaction. Optical spectroscopy, particularly fluorescence, is the most flexible technique, but surface plasmon resonance biosensors, microcalorimetry and mass spectroscopy have recently shown significant development.
J H, Lakey, E M, Raggett
openaire   +2 more sources

Protein-Protein Interactions

1954
Publisher Summary This chapter focuses on protein–protein interaction. The unique characteristics of different proteins are developed in the interactions of proteins with each other, with ions, and with nonprotein materials such as lipids, nucleic acids, and carbohydrates.
openaire   +2 more sources