A systems-based framework to computationally describe putative transcription factors and signaling pathways regulating glycan biosynthesis

• Theodore Groth,
• Rudiyanto Gunawan and
• Sriram Neelamegham

Beilstein J. Org. Chem. 2021, 17, 1712–1724, doi:10.3762/bjoc.17.119

• , State University of New York, Buffalo, NY 14260, USA 10.3762/bjoc.17.119 Abstract Glycosylation is a common posttranslational modification, and glycan biosynthesis is regulated by a set of glycogenes. The role of transcription factors (TFs) in regulating the glycogenes and related glycosylation

Semiautomated glycoproteomics data analysis workflow for maximized glycopeptide identification and reliable quantification

• Steffen Lippold,
• Arnoud H. de Ru,
• Jan Nouta,
• Peter A. van Veelen,
• Magnus Palmblad,
• Manfred Wuhrer and
• Noortje de Haan

Beilstein J. Org. Chem. 2020, 16, 3038–3051, doi:10.3762/bjoc.16.253

• features, such as the linkage position and anomeric configuration, make protein glycosylation a highly complex posttranslational modification (PTM). Glycoproteomics has become important for many life science disciplines, in particular for biomedical and biopharmaceutical research [3][4][5]. Glycopeptide

NMR Spectroscopy of supramolecular chemistry on protein surfaces

• Peter Bayer,
• Anja Matena and
• Christine Beuck

Beilstein J. Org. Chem. 2020, 16, 2505–2522, doi:10.3762/bjoc.16.203

• shifts for both 1H and 13C nuclei. Methylation of Lys and Arg occurs as posttranslational modification (PTM) of proteins in nature, often used as a switch to regulate protein interactions and thus their function [112][113]. The Crowley lab has used this advantage to study the binding of sulfonatocalix[4

Aminosugar-based immunomodulator lipid A: synthetic approaches

• Alla Zamyatina

Beilstein J. Org. Chem. 2018, 14, 25–53, doi:10.3762/bjoc.14.3

Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD⁺ analogues

• Sarah Wallrodt,
• Edward L. Simpson and
• Andreas Marx

Beilstein J. Org. Chem. 2017, 13, 495–501, doi:10.3762/bjoc.13.49

• acceptors forming mono- or poly(ADP-ribos)ylated proteins. Out of the 18 members identified, only four are known to synthesise the complex poly(ADP-ribose) biopolymer. The investigation of this posttranslational modification is important due to its involvement in cancer and other diseases. Lately, metabolic

• -ribose); posttranslational modification; Introduction ADP-ribosyl transferases with diphtheria toxin homology [1] (ARTDs), also termed poly(ADP-ribose) polymerases (PARPs), form an enzyme family of 18 human members [2] that mediate their widespread functions in cellular homeostasis through the catalysis

• of ADP-ribosylation [3][4]. This posttranslational modification received considerable attention within the last decade [5][6] and has been linked to tumour biology, oxidative stress, inflammatory, and metabolic diseases [7]. Using NAD+ as a substrate, ARTDs covalently transfer ADP-riboses onto

Posttranslational isoprenylation of tryptophan in bacteria

• Masahiro Okada,
• Tomotoshi Sugita and
• Ikuro Abe

Beilstein J. Org. Chem. 2017, 13, 338–346, doi:10.3762/bjoc.13.37

• ; isoprenylation; post-translational modification; quorum sensing; tryptophan; Introduction Posttranslational modification is the chemical modification of proteins after their translation from mRNAs to the corresponding polypeptide chains synthesized by ribosomes. Since a posttranslational modification generates

• either a geranyl or farnesyl group at the gamma position to form tricyclic skeleton that bears a newly formed pyrrolidine, which is similar to proline (Figure 3A) [26][27][28]. The posttranslational modification of ComX pheromones with an isoprenoid plays an essential role for specific quorum sensing

Adsorption mechanism and valency of catechol-functionalized hyperbranched polyglycerols

• Stefanie Krysiak,
• Qiang Wei,
• Klaus Rischka,
• Andreas Hartwig,
• Rainer Haag and
• Thorsten Hugel

Beilstein J. Org. Chem. 2015, 11, 828–836, doi:10.3762/bjoc.11.92

• -dihydroxyphenylalanine (DOPA, 15–30 mol %) [7][8]. DOPA is formed by posttranslational modification of tyrosine. Mefp 6 is rich in cystein (11 mol %) [6]. It has been found that the DOPA in Mefp 3 and 5 adheres to the surfaces, while the cystein-rich Mefp 6 controls the redox balance and can keep interfacial DOPA in a

Chemoselective O-acylation of hydroxyamino acids and amino alcohols under acidic reaction conditions: History, scope and applications

• Tor E. Kristensen

Beilstein J. Org. Chem. 2015, 11, 446–468, doi:10.3762/bjoc.11.51

Synthesis of isoprenoid bisphosphonate ethers through C–P bond formations: Potential inhibitors of geranylgeranyl diphosphate synthase

• Xiang Zhou,
• Jacqueline E. Reilly,
• Kathleen A. Loerch,
• Raymond J. Hohl and
• David F. Wiemer

Beilstein J. Org. Chem. 2014, 10, 1645–1650, doi:10.3762/bjoc.10.171

• C20 isoprenoid geranylgeranyl diphosphate (GGPP) (Figure 2) [3]. Geranylgeranylation is an important posttranslational modification, especially among proteins in the Ras superfamily of small GTPases that are involved in a variety of signaling pathways [4]. Based on the premise that inhibition of GGDPS