Abstract
Glycosylation plays critical roles in various biological processes and is closely related to diseases. Deciphering the glycocode in diverse cells and tissues offers opportunities to develop new disease biomarkers and more effective recombinant therapeutics. In the past few decades, with the development of glycobiology, glycomics, and glycoproteomics technologies, a large amount of glycoscience data has been generated. Subsequently, a number of glycobiology databases covering glycan structure, the glycosylation sites, the protein scaffolds, and related glycogenes have been developed to store, analyze, and integrate these data. However, these databases and tools are not well known or widely used by the public, including clinicians and other researchers who are not in the field of glycobiology, but are interested in glycoproteins. In this study, the representative databases of glycan structure, glycoprotein, glycan–protein interactions, glycogenes, and the newly developed bioinformatic tools and integrated portal for glycoproteomics are reviewed. We hope this overview could assist readers in searching for information on glycoproteins of interest, and promote further clinical application of glycobiology.
Highlights
Glycosylation is known as one of the most ubiquitous and important post-translational modifications (PTMs) in nature
The complexity is further increased by the fact that glycan expression on a single protein is subject to both macroheterogeneity and microheterogeneity [4]
GlycoStore focuses on ultra-high performance liquid chromatography (U/HPLC), reversed phase (RP)-U/HPLC, porous graphitized carbon (PGC) chromatography, and capillary electrophoresis (CE) elution positions for approximately 850 unique glycan structures with links to taxonomy, glycoprotein, and supporting literature
Summary
Glycosylation is known as one of the most ubiquitous and important post-translational modifications (PTMs) in nature. Due to the different expression of glycogenes such as glycosyltransferase and glucosidase in different cells and tissues, the glycans attached to the same protein are cell-, tissue-, organism-, and physiological state-dependent. The same glycan structure on different proteins may have different functions. The interpretation of the glycosylation sites, the attached glycan structure, the protein scaffolds, and related glycogenes are cruciaIlntf.oJ.rMuoln. In addition to these comprehensive resources, a variety of databases on glycan on thesstreucdtautraeb, agslyecsohgeanvees,bgeleyncodperovteelionps,eadndalla osvereiresthoef bwiooirnlfdo,rmwahtiicchtoaollssobapsreodmoontethtehsee ddeatvaeblaospesment of glyhcoavbeiobloeegny.dHevoewloepveedr,aglleonveerraltlhyeswpeoarlkdi,nwg,htihchesaelsdoatparboamsoetseatnhde dtoeovleslohpamveennt ootfbgeleyncowbieollol gkyn.own and wHidoewleyvuers,egdenbeyratlhlye sppuebakliicn,gi,ntchleusde idnagtacblainseisciaanndstaonodls ohathveernroetsbeeaernchweerlsl kwnhowo naraenndowtiidneltyheusfieedld of glycobiyotlhoegyp,ubbulitc,airnecliundteinrgesctleindiciinangslyacnodportohteerinress.earchers who are not in the field of glycobiology, but Aasregilnytceorpesrtoetdeinsghlyacvoepbroetceoinms.e the promising candidates of disease markers and therapeutic targets, we mainlyAfsocgulyscopnrpotreoinvsidhianvgeabnecoovmerevtiheewporofmmisaiinngfecaantudridesataens doffudniscetaisoenmalaitrikeesrsofatnhdetrheeprarepseeuntitcative databtaasregsetosf, gwlyecmanaisntlryucfotucures ,ognlypcroopvriodtineignsa,ngolyvcearvni–epwrootfeimnaiinntefreaactutiroens sa,nadndfugnlcytcioongaelintieess ionfhtuhme ans and mraepmremseanlitaantisve(Fidgautarbea1s)e.sInofadgdlyitciaonn,swtreucstuumre,mgalryiczoepdrosotemines,negwlyclyand–epvroetleoipnedinbteioraicntfioonrms, aatincdtools and ingdtleeyvgceorlagotepenededsrbeiisnooinuhfruocmremsaanftosicratgnolodylcsmoapnamdromitneatoeligmarnaicstesd(wFriigetsuhoruethrc1ee)s.gofIonarlgaodlfydcmiotipaorknoi,ntewgomethisceussmewbmitihaoritinhzefeodgromsaolamotifecmsnareekwsinolgyurces more wthiedseelbyiokinnofowrmnattoictshreespouubrlciecs, emsopreeciwalildyeltyo krensoewanrcthoetrhseinpuobthliec,r edsipseccipiallilnyetso. FigureFi1g.urSeu1m. mSuamrymaorfyroefprreepserensteanttiavteivgelgylcyocioninfoforrmmaattiicc ddaattaabbaasseessuusisnigngmmemebmrabnreangelygcolypcrootperinosteaisns as exampexlea.mGpBleP. sG,BgPlys,cgalnycbainndbiinndginpgroptreoitneisn. s
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