FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2496571824> ?p ?o ?g. }

• W2496571824 endingPage "9406" @default.
• W2496571824 startingPage "9404" @default.
• W2496571824 abstract "Protein-based biologics have revolutionized the treatment of many diseases, but low efficacy, occasional undesirable side effects, and rapid clearance from circulation limit their full potential. The majority of pharmaceutically relevant proteins are N-linked glycosylated, and their sugar moieties have significant impact on their folding, assembly, solubility, serum and shelf half-life, and functionality (1). Thus, one approach to enhance the potency, safety, and stability of therapeutic proteins is glycoengineering, altering protein-associated carbohydrate to achieve the desirable protein properties. The challenge is to develop biological systems that can consistently produce glycoproteins with homogeneous glycans on demand. The availability of such systems will lead to breakthroughs in two fronts: ( i ) elucidating the contribution of sugar moieties for various biological functions and ( ii ) developing novel biologics with tailor-made glycosylation based on their functional needs. In PNAS, Kallolimath et al. (2) describe their efforts in bringing one such host system to reality.Unlike the protein backbone that is synthesized based on a defined template, sugar chains are assembled enzymatically. As a result, these chains are diverse in both the number and the linkage patterns of the sugar units. In addition, different host cells may modify the same protein with different sugar structures. Protein N-linked glycosylation involves the addition of an oligosaccharide (Man9) to an asparagine residue on a nascent polypeptide. In eukaryotes, the transfer and initial processing of Man9 start in the endoplasmic reticulum to form Man8, which is further processed in Golgi compartments to form complex N-glycans (3). The early steps of N-glycan processing up to the formation of the intermediate of GnGn are well preserved among most eukaryotic cells (Fig. 1). However, processing beyond this point differs significantly, leading to the formation of different complex N-glycoforms (3). In mammalian cells, there is a large diverse population of glycoenzymes for extensive elongation of the … [↵][1]1Email: qiang.chen.4{at}asu.edu. [1]: #xref-corresp-1-1" @default.
• W2496571824 created "2016-08-23" @default.
• W2496571824 creator A5035961174 @default.
• W2496571824 date "2016-08-09" @default.
• W2496571824 modified "2023-09-27" @default.
• W2496571824 title "Glycoengineering of plants yields glycoproteins with polysialylation and other defined N-glycoforms" @default.
• W2496571824 cites W1980535563 @default.
• W2496571824 cites W1985588717 @default.
• W2496571824 cites W1995631830 @default.
• W2496571824 cites W2026760618 @default.
• W2496571824 cites W2033648590 @default.
• W2496571824 cites W2047604544 @default.
• W2496571824 cites W2069221009 @default.
• W2496571824 cites W2071202867 @default.
• W2496571824 cites W2094993149 @default.
• W2496571824 cites W2107632694 @default.
• W2496571824 cites W2158319246 @default.
• W2496571824 cites W2397218916 @default.
• W2496571824 cites W2470330280 @default.
• W2496571824 cites W2489417518 @default.
• W2496571824 cites W993338644 @default.
• W2496571824 doi "https://doi.org/10.1073/pnas.1610803113" @default.
• W2496571824 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5003273" @default.
• W2496571824 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27506788" @default.
• W2496571824 hasPublicationYear "2016" @default.
• W2496571824 type Work @default.
• W2496571824 sameAs 2496571824 @default.
• W2496571824 citedByCount "28" @default.
• W2496571824 countsByYear W24965718242016 @default.
• W2496571824 countsByYear W24965718242017 @default.
• W2496571824 countsByYear W24965718242018 @default.
• W2496571824 countsByYear W24965718242019 @default.
• W2496571824 countsByYear W24965718242020 @default.
• W2496571824 countsByYear W24965718242021 @default.
• W2496571824 countsByYear W24965718242022 @default.
• W2496571824 countsByYear W24965718242023 @default.
• W2496571824 crossrefType "journal-article" @default.
• W2496571824 hasAuthorship W2496571824A5035961174 @default.
• W2496571824 hasBestOaLocation W24965718241 @default.
• W2496571824 hasConcept C108625454 @default.
• W2496571824 hasConcept C185592680 @default.
• W2496571824 hasConcept C55493867 @default.
• W2496571824 hasConceptScore W2496571824C108625454 @default.
• W2496571824 hasConceptScore W2496571824C185592680 @default.
• W2496571824 hasConceptScore W2496571824C55493867 @default.
• W2496571824 hasFunder F4320337355 @default.
• W2496571824 hasIssue "34" @default.
• W2496571824 hasLocation W24965718241 @default.
• W2496571824 hasLocation W24965718242 @default.
• W2496571824 hasLocation W24965718243 @default.
• W2496571824 hasLocation W24965718244 @default.
• W2496571824 hasOpenAccess W2496571824 @default.
• W2496571824 hasPrimaryLocation W24965718241 @default.
• W2496571824 hasRelatedWork W1500427933 @default.
• W2496571824 hasRelatedWork W1578965502 @default.
• W2496571824 hasRelatedWork W1749420422 @default.
• W2496571824 hasRelatedWork W1975496805 @default.
• W2496571824 hasRelatedWork W2005442970 @default.
• W2496571824 hasRelatedWork W2029686515 @default.
• W2496571824 hasRelatedWork W2033482754 @default.
• W2496571824 hasRelatedWork W2042950603 @default.
• W2496571824 hasRelatedWork W2188749728 @default.
• W2496571824 hasRelatedWork W2414560469 @default.
• W2496571824 hasVolume "113" @default.
• W2496571824 isParatext "false" @default.
• W2496571824 isRetracted "false" @default.
• W2496571824 magId "2496571824" @default.
• W2496571824 workType "article" @default.