Proteomic analysis of the crayfish gastrolith chitinous extracellular matrix reveals putative protein complexes and a central role for GAP 65

2015 ◽  
Vol 128 ◽  
pp. 333-343 ◽  
Author(s):  
Lilah Glazer ◽  
Ziv Roth ◽  
Simy Weil ◽  
Eliahu D. Aflalo ◽  
Isam Khalaila ◽  
...  
2002 ◽  
Vol 3 (3) ◽  
pp. 221-225

In recent months a bumper crop of genomes has been completed, including the fission yeast (Schizosaccharomyces pombe) and rice (Oryza sativa). Two large-scale studies ofSaccharomyces cerevisiaeprotein complexes provided a picture of the eukaryotic proteome as a network of complexes. Amongst the other stories of interest was a demonstration that proteomic analysis of blood samples can be used to detect ovarian cancer, perhaps even as early as stage I.


PROTEOMICS ◽  
2007 ◽  
Vol 7 (16) ◽  
pp. 2688-2697 ◽  
Author(s):  
Ming Zhou ◽  
Timothy D. Veenstra

2012 ◽  
Vol 11 (8) ◽  
pp. 4052-4064 ◽  
Author(s):  
S. Tamir Rashid ◽  
Jonathan D. Humphries ◽  
Adam Byron ◽  
Ameet Dhar ◽  
Janet A. Askari ◽  
...  

2021 ◽  
Vol 9 (1) ◽  
pp. 186-198
Author(s):  
Rita Sobreiro-Almeida ◽  
Maria Elena Melica ◽  
Laura Lasagni ◽  
Hugo Osório ◽  
Paola Romagnani ◽  
...  

Decellularized matrices are attractive substrates, being able to retain growth factors and proteins present in the native tissue.


PROTEOMICS ◽  
2006 ◽  
Vol 6 (21) ◽  
pp. 5868-5879 ◽  
Author(s):  
Delphine Pflieger ◽  
Sandrine Chabane ◽  
Olivier Gaillard ◽  
Bruno Alain Bernard ◽  
Patrick Ducoroy ◽  
...  

2020 ◽  
pp. 002215542094640 ◽  
Author(s):  
Sylvain D. Vallet ◽  
Olivier Clerc ◽  
Sylvie Ricard-Blum

The six mammalian glycosaminoglycans (GAGs), chondroitin sulfate, dermatan sulfate, heparin, heparan sulfate, hyaluronan, and keratan sulfate, are linear polysaccharides. Except for hyaluronan, they are sulfated to various extent, and covalently attached to proteins to form proteoglycans. GAGs interact with growth factors, morphogens, chemokines, extracellular matrix proteins and their bioactive fragments, receptors, lipoproteins, and pathogens. These interactions mediate their functions, from embryonic development to extracellular matrix assembly and regulation of cell signaling in various physiological and pathological contexts such as angiogenesis, cancer, neurodegenerative diseases, and infections. We give an overview of GAG–protein interactions (i.e., specificity and chemical features of GAG- and protein-binding sequences), and review the available GAG–protein interaction networks. We also provide the first comprehensive draft of the GAG interactome composed of 832 biomolecules (827 proteins and five GAGs) and 932 protein–GAG interactions. This network is a scaffold, which in the future should integrate structures of GAG–protein complexes, quantitative data of the abundance of GAGs in tissues to build tissue-specific interactomes, and GAG interactions with metal ions such as calcium, which plays a major role in the assembly of the extracellular matrix and its interactions with cells. This contextualized interactome will be useful to identify druggable GAG–protein interactions for therapeutic purpose:


2008 ◽  
Vol 2 (9) ◽  
pp. 1223-1233 ◽  
Author(s):  
Earle F. Burgess ◽  
Amy-Joan L. Ham ◽  
David L. Tabb ◽  
Dean Billheimer ◽  
Bruce J. Roth ◽  
...  

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Tatiana Martin-Rojas ◽  
Laura Mourino-Alvarez ◽  
Sergio Alonso-Orgaz ◽  
Esther Rosello-Lleti ◽  
Enrique Calvo ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document