dc.contributor.author
Perez, Serge
dc.contributor.author
Makshakova, Olga
dc.contributor.author
Angulo, Jesus
dc.contributor.author
Bedini, Emiliano
dc.contributor.author
Bisio, Antonella
dc.contributor.author
de Paz, Jose Luis
dc.contributor.author
Fadda, Elisa
dc.contributor.author
Guerrini, Marco
dc.contributor.author
Hricovini, Michal
dc.contributor.author
Pagel, Kevin
dc.date.accessioned
2023-04-20T05:49:45Z
dc.date.available
2023-04-20T05:49:45Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/38987
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-38703
dc.description.abstract
Glycosaminoglycans (GAGs) are complex polysaccharides exhibiting a vast structural diversity and fulfilling various functions mediated by thousands of interactions in the extracellular matrix, at the cell surface, and within the cells where they have been detected in the nucleus. It is known that the chemical groups attached to GAGs and GAG conformations comprise “glycocodes” that are not yet fully deciphered. The molecular context also matters for GAG structures and functions, and the influence of the structure and functions of the proteoglycan core proteins on sulfated GAGs and vice versa warrants further investigation. The lack of dedicated bioinformatic tools for mining GAG data sets contributes to a partial characterization of the structural and functional landscape and interactions of GAGs. These pending issues will benefit from the development of new approaches reviewed here, namely (i) the synthesis of GAG oligosaccharides to build large and diverse GAG libraries, (ii) GAG analysis and sequencing by mass spectrometry (e.g., ion mobility-mass spectrometry), gas-phase infrared spectroscopy, recognition tunnelling nanopores, and molecular modeling to identify bioactive GAG sequences, biophysical methods to investigate binding interfaces, and to expand our knowledge and understanding of glycocodes governing GAG molecular recognition, and (iii) artificial intelligence for in-depth investigation of GAGomic data sets and their integration with proteomics.
en
dc.format.extent
29 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject
glycosaminoglycans
en
dc.subject
chondroitin sulfate
en
dc.subject
dermatan sulfate
en
dc.subject
heparan sulfate
en
dc.subject
keratan sulfate heparosan
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
dc.title
Glycosaminoglycans: What Remains To Be Deciphered?
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.doi
10.1021/jacsau.2c00569
dcterms.bibliographicCitation.journaltitle
JACS Au
dcterms.bibliographicCitation.number
3
dcterms.bibliographicCitation.pagestart
628
dcterms.bibliographicCitation.pageend
656
dcterms.bibliographicCitation.volume
3
dcterms.bibliographicCitation.url
https://doi.org/10.1021/jacsau.2c00569
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
2691-3704
refubium.resourceType.provider
WoS-Alert