Results 221 to 230 of about 155,076 (257)

N-Glycosylation and Plant Cell Growth

2014
N-linked glycosylation is one of the most prevalent cotranslational protein modifications in plants. It is initiated by a conserved process in the endoplasmic reticulum and subsequently involves a series of different N-glycan maturation steps that take place in the ER and Golgi apparatus.
Christiane, Veit, Ulrike, Vavra, Richard, Strasser   +2 more
openaire   +2 more sources

N-Glycosylation in Chrysosporium lucknowense enzymes

Carbohydrate Research, 2008
Twenty-eight enzymes, encoded by different genes and secreted by different mutant strains of Chrysosporium lucknowense, were subjected to MALDI-TOF MS peptide fingerprinting followed by analysis of the MS data using the GlycoMod tool from the ExPASy proteomic site. Various N-linked glycan structures were discriminated in the C.
Alexander V, Gusakov, Alexey I, Antonov, Boris B, Ustinov   +2 more
openaire   +2 more sources

Characterization of Protein N‐Glycosylation

2005
Although mass spectrometry (MS)-based protein identification is a straightforward task, the characterization of most posttranslational modifications still represents a challenge. N-glycosylation with its well known consensus sequence, common core structure, and "universally" active endoglycosidase seems to belong to the easier category. In this chapter,
openaire   +2 more sources

N-Glycosylation in progression of skin cancer

Medical Oncology, 2019
Skin cancer can be classified as cutaneous malignant melanoma, basal cell carcinoma, and squamous cell carcinoma. Due to the high level of morbidity and mortality, skin cancer has become a global public health issue worldwide while the pathogenesis of skin cancer is still unclear.
Ling Tang, Xiaoping Chen, Xu Zhang, Yeye Guo, Juan Su, Jianglin Zhang, Cong Peng, Xiang Chen   +7 more
openaire   +2 more sources

Integrin α5β1 and Its N-Glycosylation

2014
Integrins are transmembrane heterodimeric proteins sensing the cell microenvironment and modulating numerous signaling pathways. Changes in integrin function and expression between normal and tumor cells support involvement of specific integrins in tumor progression and aggressiveness.
Jianguo Gu, Qinglei Hang, Tomohiko Fukuda, Tomoya Isaji   +3 more
openaire   +1 more source

Characterization of Site-Specific N-Glycosylation

2019
Even if a consensus sequence has been identified for a posttranslational modification, the presence of such a sequence motif only indicates the possibility, not the certainty that the modification actually occurs. Proteins can be glycosylated on certain amino acid side chains, and these modifications are designated as C-, N-, and O-glycosylation.
Hevér, Helga, Darula, Zsuzsanna, Medzihradszky F., Katalin   +2 more
openaire   +3 more sources

N-Glycosylation of Plant Recombinant Pharmaceuticals

2009
N-glycosylation is a maturation event necessary for the correct function, efficiency, and stability of a high number of biopharmaceuticals. This chapter presented here proposes various methods to determine whether, how, and where a plant pharmaceutical is N-glycosylated.
Bardor, Muriel, Cabrera, Gleysin, Stadlmann, Johannes, Lerouge, Patrice, Cremata, José, Gomord, Veronique, Fitchette, Anne-Catherine   +6 more
openaire   +4 more sources

The role of CD147 N-glycosylation and IgG N-glycosylation in the inflammatory modulation of atherogenesis

Atherosclerosis, an immunoinflammatory cardiovascular disease progressing with ageing, is the leading cause of death globally. Research demonstrates that cluster of differentiation 147 (CD147) and immunoglobulin G (IgG) in blood are closely associated with the development of atherosclerosis.
openaire   +1 more source

Global view of human protein glycosylation pathways and functions

Nature Reviews Molecular Cell Biology, 2020
Katrine T Schjoldager, Yoshiki Narimatsu, Hiren J Joshi   +2 more
exaly  

By N-Glycosylation

2004
F. Seela, N. Ramzaeva, H. Rosemeyer
openaire   +1 more source