Results 31 to 40 of about 1,211 (133)

Analysis of congenital disorder of glycosylation-Id in a yeast model system shows diverse site-specific under-glycosylation of glycoproteins [PDF]

, 2012
Asparagine-linked glycosylation is a common post translational modification of proteins in eukaryotes. Mutations in the human ALG3 gene cause changed levels and altered glycan structures on mature glycoproteins and are the cause of a severe congenital ...
Aebi M., Apweiler R., Benjamin L. Schulz, Bova G. S., Breidenbach M. A., Burda P., Chen W., Garshasbi M., Haeuptle M. A., Helenius A., Henquet M., Henquet M., Honma K., Huffaker T. C., Hülsmeier A. J., Izquiedro L., Jamaluddin M. F. B., Janik M. E., Kasturi L., Kelleher D. J., Krokhin O. V., Lizak C., Mohorko E., Molinari F., Muhammad Fairuz Jamaluddin, Nasab F., Palmisano G., Pils D., Robinson N. E., Runge K. W., Sato S., Schulz B. L., Schulz B. L., Schulz B. L., Sun L., Ulla-Maja Bailey, Whitley P., Yin Q. Y., Zhang H.   +38 more
core   +1 more source

Acanthopanax senticosus extract alleviates radiation‐induced learning and memory impairment based on neurotransmitter‐gut microbiota communication

CNS Neuroscience &Therapeutics, Volume 29, Issue S1, Page 129-145, June 2023., 2023
Acanthopanax senticosus extract alleviates radiation‐induced learning and memory impairment based on neurotransmitter‐gut microbiota communication. By Figdraw (www.figdraw.com). Abstract Background Acanthopanax senticosus (AS) is a medicinal and food plant with many physiological functions, especially nerve protection.
Chen Song, Yishu Yin, Yue Qin, Tianzhu Li, Deyong Zeng, Ting Ju, Fangyuan Duan, Yingchun Zhang, Weihong Lu   +8 more
wiley   +1 more source

Deglycosylation systematically improves N-glycoprotein identification in liquid chromatography-tandem mass spectrometry proteomics for analysis of cell wall stress responses in Saccharomyces cerevisiae lacking Alg3p [PDF]

, 2013
Post-translational modification of proteins with glycosylation is of key importance in many biological systems in eukaryotes, influencing fundamental biological processes and regulating protein function. Changes in glycosylation are therefore of interest
Adamczyk, Aebi, Bailey, Benjamin L. Schulz, Boorsma, Burda, Castillo, Comunale, Dall’Olio, Ecker, Helenius, Hennet, Huffaker, Izquiedro, Jaeken, Jensen, Jessani, Jung, Kapteyn, Kelleher, Kimura, Kolarich, Krokhin, Lizak, Lopez-Villar, Marth, Mohorko, Moukadiri, Mrsa, Nasab, Ohtsubo, Orlean, Ossola, Palmisano, Robinson, Rolli, Schulz, Schulz, Schulz, Schulz, Schulz, Selevsek, Sloane, Stahl-Zeng, Teparić, Tian, Ulla-Maja Bailey, Wilson, Yin, Yin, Zhang, Zhang   +51 more
core   +1 more source

A Drosophila screen identifies NKCC1 as a modifier of NGLY1 deficiency [PDF]

, 2020
N-Glycanase 1 (NGLY1) is a cytoplasmic deglycosylating enzyme. Loss-of-function mutations in the NGLY1 gene cause NGLY1 deficiency, which is characterized by developmental delay, seizures, and a lack of sweat and tears.
Chow, Clement Y, Clark, Nathan L, Coelho, Emily, Hope, Kevin A, Lutz, Cathleen, Mercenne, Gaelle, Owings, Katie G, Partha, Raghavendran, Pleinis, John M, Rodan, Aylin R, Talsness, Dana M, Zuberi, Aamir   +11 more
core   +2 more sources

Analysis of urinary oligosaccharide excretion patterns by UHPLC/HRAM mass spectrometry for screening of lysosomal storage disorders

Journal of Inherited Metabolic Disease, Volume 46, Issue 2, Page 206-219, March 2023., 2023
Abstract Oligosaccharidoses, sphingolipidoses and mucolipidoses are lysosomal storage disorders (LSDs) in which defective breakdown of glycan‐side chains of glycosylated proteins and glycolipids leads to the accumulation of incompletely degraded oligosaccharides within lysosomes. In metabolic laboratories, these disorders are commonly diagnosed by thin‐
Marne C. Hagemeijer, Jeroen C. van den Bosch, Michiel Bongaerts, Edwin H. Jacobs, Johanna M. P. van den Hout, Esmee Oussoren, George J. G. Ruijter   +6 more
wiley   +1 more source

A conserved role for AMP-activated protein kinase in NGLY1 deficiency.

PLoS Genetics, 2020
Mutations in human N-glycanase 1 (NGLY1) cause the first known congenital disorder of deglycosylation (CDDG). Patients with this rare disease, which is also known as NGLY1 deficiency, exhibit global developmental delay and other phenotypes including ...
Seung Yeop Han, Ashutosh Pandey, Tereza Moore, Antonio Galeone, Lita Duraine, Tina M Cowan, Hamed Jafar-Nejad   +6 more
doaj   +1 more source

Characterization of Cell Glycocalyx with Mass Spectrometry Methods. [PDF]

, 2019
The cell membrane plays an important role in protecting the cell from its extracellular environment. As such, extensive work has been devoted to studying its structure and function.
Lebrilla, Carlito B, Li, Qiongyu, Wong, Maurice, Xie, Yixuan   +3 more
core   +2 more sources

NGLY1 Deficiency: A Rare Genetic Disorder Unlocks Therapeutic Potential for Common Diseases

Israel Journal of Chemistry, Volume 63, Issue 1-2, February 2023., 2023
Abstract The enzyme catalysing the removal of N‐linked glycans from misfolded glycoproteins in the cytosol is an evolutionary well‐conserved glycanase called Peptide:N‐glycanase (PNGase; NGLY1 in humans). NGLY1 hydrolyses the amide bond between an Asn and the proximal N‐acetylglucosamine (GlcNAc) of the attached N‐glycan, thereby converting that ...
Simon Walber, Georgia Partalidou, Ulla I. M. Gerling‐Driessen   +2 more
wiley   +1 more source

Aquaporins: important but elusive drug targets. [PDF]

, 2014
The aquaporins (AQPs) are a family of small, integral membrane proteins that facilitate water transport across the plasma membranes of cells in response to osmotic gradients.
A Bergamo, A Burykin, A Kimura, A Rossi, A Warth, A Warth, AB Chepelinsky, AJ Smith, AJ Yool, AJ Yool, Alan S. Verkman, AP Martins, AP Martins, AS Verkman, AS Verkman, B Bassarak, B Bertrand, B Ma, B Yang, B Yang, B Yang, B Yang, B Zhang, BC Kieseier, BJ Baum, BJ Baum, BJ Jin, BK Tamarappoo, BL de Groot, C Esteva-Font, C Goubau, C Maurel, CL Chou, CM Niemietz, D Fu, D Fu, D Seeliger, D Wesche, D Zhang, DC Blaydon, DG Bichet, DK Binder, DM Wingerchuk, E Beitz, E Lindahl, E Migliati, E Solenov, E Soupene, EM Muller, EM Nagy, ET Olesen, EW Miller, F Baumgart, FJ Detmers, G Di Giusto, G Fischer, G Soveral, G Soveral, GM Preston, GM Preston, GP Bienert, GP Nicchia, GT Manley, H Chen, H Hasegawa, H Sui, H Tsukaguchi, H Zhang, HJ Jung, HL Brooks, J Badaut, J Farinas, J Farinas, J Farinas, J Gao, J Hu, J Li, J Li, J Liu, J Palace, J Schnermann, JD Ho, JE Rash, JF Kun, JJ Iliff, JJ Irwin, JL Edelman, JM Crane, JP Morello, JR Thiagarajah, JS Hub, K Ishibashi, K Miranda, K Murata, K Oshio, K Oshio, K Oshio, KI Auguste, L Janosi, L Tradtrantip, L Tradtrantip, L Tradtrantip, L Tradtrantip, LJ Galietta, LM Holm, LS King, M Amiry-Moghaddam, M Araki, M Boone, M Dumas, M Endo, M Hara, M Hara-Chikuma, M Hara-Chikuma, M Hara-Chikuma, M Hara-Chikuma, M Herrera, M Kato, M Moore, M Ozu, M Ozu, Marc O. Anderson, Marios C. Papadopoulos, MC Papadopoulos, MC Papadopoulos, MC Papadopoulos, MC Papadopoulos, MC Papadopoulos, MG Mola, MH Levin, MH Levin, MJ Tait, MP Marrades, N Chihara, N Maeda, N Roudier, N Roudier, N Zhu, NN Haj-Yasein, O Bloch, O Bloch, P Padmawar, PM Deen, PW Phuan, R Gao, R Katada, R Musa-Aziz, R Zhang, RB Zhang, RI Macey, S Jelen, S Jelen, S Nielsen, S Nielsen, S Pavlovic-Djuranovic, S Saadoun, S Saadoun, S Saadoun, S Saadoun, S Saadoun, S Saadoun, S Saadoun, S Sasaki, S Tornroth-Horsefield, SD Shields, SJ Wacker, SR Hinson, SR Hinson, T Gonen, T Hibuse, T Ma, T Ma, T Ma, T Ma, T Ma, T Yamamoto, T Zeuthen, TH Kwon, TL Pallone, V Berry, VA Lennon, VA Lennon, VJ Huber, VJ Huber, W Castro-Borges, X Cao, Y Liu, Y Morishita, Y Song, Y Song, Y Wang, YB Zhang, YH Huang, Z Zhang, ZH Li   +194 more
core   +1 more source

NGLY1 deficiency: Novel patient, review of the literature and diagnostic algorithm

JIMD Reports, 2020
Objectives Together with the lysosomal storage diseases, NGLY1 deficiency is a congenital disorder of deglycosylation (NGLY1‐CDDG). Since the first report in 2012, 26 patients have been described. All but one were diagnosed by exome or genome sequencing;
Patryk Lipiński, Anna Bogdańska, Agnieszka Różdżyńska‐Świątkowska, Aldona Wierzbicka‐Rucińska, Anna Tylki‐Szymańska   +4 more
doaj   +1 more source