Results 31 to 40 of about 331,855 (331)

Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity [PDF]

open access: yes, 2020
Type III secretion systems are used by many Gram-negative bacterial pathogens to inject proteins, known as effectors, into the cytosol of host cells. These virulence factors interfere with a diverse array of host signal transduction pathways and cellular
Araujo Garrido, Juan Luis   +2 more
core   +1 more source

Studying Lactoferrin N-Glycosylation. [PDF]

open access: yes, 2017
Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and ...
Barile, Daniela   +4 more
core   +2 more sources

Abnormal sialylation and fucosylation of saliva glycoproteins: Characteristics of lung cancer-specific biomarkers

open access: yesCurrent Research in Pharmacology and Drug Discovery, 2022
Dysregulated surface glycoproteins play an important role in tumor cell proliferation and progression. Abnormal glycosylation of these glycoproteins may activate tumor signal transduction and lead to tumor development.
Ziyuan Gao   +6 more
doaj   +1 more source

Glycosylation in the thyroid gland : vital aspects of glycoprotein function in thyrocyte physiology and thyroid disorders [PDF]

open access: yes, 2018
The key proteins responsible for hormone synthesis in the thyroid are glycosylated. Oligosaccharides strongly affect the function of glycosylated proteins.
Ewa Pocheć   +2 more
core   +1 more source

Glycosylation of Conotoxins

open access: yesMarine Drugs, 2013
Conotoxins are small peptides present in the venom of cone snails. The snail uses this venom to paralyze and capture prey. The constituent conopeptides display a high level of chemical diversity and are of particular interest for scientists as tools employed in neurological studies and for drug development, because they target with exquisite ...
Gerwig, G.J.   +4 more
openaire   +6 more sources

Posttranslational modifications of GLUT4 affect its subcellular localization and translocation [PDF]

open access: yes, 2013
The facilitative glucose transporter type 4 (GLUT4) is expressed in adipose and muscle and plays a vital role in whole body glucose homeostasis. In the absence of insulin, only ~1% of cellular GLUT4 is present at the plasma membrane, with the vast ...
Bayer   +64 more
core   +3 more sources

Glycosylation and behavioral symptoms in neurological disorders

open access: yesTranslational Psychiatry, 2023
Glycosylation, the addition of glycans or carbohydrates to proteins, lipids, or other glycans, is a complex post-translational modification that plays a crucial role in cellular function.
Prajitha Pradeep   +2 more
doaj   +1 more source

Glycosyl Formates: Glycosylations with Neighboring-Group Participation [PDF]

open access: yesMolecules, 2022
Protected 2-O-benzyolated glycosyl formates were synthesized in one-step from the corresponding orthoester using formic acid as the sole reagent. Glucopyranosyl, mannopyranosyl and galactopyranosyl donors were synthesized and their glycosylation properties studied using model glycosyl acceptors of varied steric bulk and reactivity. Bismuth triflate was
Liang Yang, Christian Marcus Pedersen
openaire   +4 more sources

Glycosylation and metastases

open access: yesELECTROPHORESIS, 2018
AbstractThe change of cellular glycosylation is one of the key events in malignant transformation and neoplastic progression, and tumor‐related glycosylation alterations are promising targets in both tumor diagnosis and therapy. Both malignant transformation and neoplastic progression are the consequence of gene expression alterations and alterations ...
Krešimir Pavelić   +3 more
openaire   +5 more sources

O-Glycosylation [PDF]

open access: yesMedical Mycology, 2001
O-Glycosylation in many fungal species is initiated in the endoplasmic reticulum by protein mannosyltransferases (Pmt-proteins), which transfer mannose to serine or threonine residues, and it is completed by mannosyltransferases (Mnt-proteins) in the Golgi.
J F, Ernst, S K, Prill
openaire   +2 more sources

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