نتایج جستجو برای: glycosylated protein

تعداد نتایج: 1244008  

Journal: :Majalah kedokteran Sriwijaya 2022

AGTR1 is a modulator of angiotensin II-induced signal transduction. This article aims to examine the biomolecular characteristics and role in renal fibrosis pathway Rattus norvegicus rats. The gene ID NC 051352.1 protein NP 112271.2 for were retrieved from National Center Biotechnology Information's website. 'NCBI' website has details on AGTR1's structure, location, expression. Protease predict...

Journal: :The Biochemical journal 2007
Yiguo Zhang John M Lucocq Masayuki Yamamoto John D Hayes

Nrf1 (nuclear factor-erythroid 2 p45 subunit-related factor 1) is negatively controlled by its NTD (N-terminal domain) that lies between amino acids 1 and 124. This domain contains a leucine-rich sequence, called NHB1 (N-terminal homology box 1; residues 11-30), which tethers Nrf1 to the ER (endoplasmic reticulum). Electrophoresis resolved Nrf1 into two major bands of approx. 95 and 120 kDa. Th...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1983
H Fan H Chute E Chao M Feuerman

Murine leukemia virus (MuLV) encodes two independent pathways for expression of the gag gene. One pathway results in processing and cleavage of the precursor Pr65gag to yield the internal capsid proteins of the virion and is analogous to gag polyprotein precursors for all classes of retroviruses. The other pathway, which is not encoded by several other classes of retroviruses, begins with a gly...

Journal: :Plant Journal 2021

Lysin motif (LysM) is a carbohydrate-binding module often found in secreted or transmembrane proteins living organisms from prokaryotes to eukaryotes. Thus far, all characterized LysM-containing plants are plasma membrane-resident receptors co-receptors playing roles plant–microbe interactions. Here, we interrogate the Arabidopsis LysM/F-box-containing protein InLYP1 and reveal its function gly...

2012
Karen De Pourcq Wouter Vervecken Isabelle Dewerte Albena Valevska Annelies Van Hecke Nico Callewaert

BACKGROUND Protein-based therapeutics represent the fastest growing class of compounds in the pharmaceutical industry. This has created an increasing demand for powerful expression systems. Yeast systems are widely used, convenient and cost-effective. Yarrowia lipolytica is a suitable host that is generally regarded as safe (GRAS). Yeasts, however, modify their glycoproteins with heterogeneous ...

2012
James A Dias

Studies of human follitropin (hFSH) structure-activity relationships from the author' s laboratory are reviewed. These include mutagenesis studies that complemented the determination of the three dimensIonal structure of hFSH. Despite a large extracellular domain of the FSH receptor and the complexity and size of both the receptor and the hFSH molecule, only a handful of hFSH amino acids are re...

2007
C. GOOSEN M. J. E. C. VAN DER MAAREL L. DIJKHUIZEN

The purified exo-inulinase enzyme ofAspergillus nigerN402 (AngInuE; heterologously expressed in Escherichia coli) displayed a sucrose:inulin (S/I) hydrolysis ratio of 2.3, characteristic for a typical exo-inulinase. The enzyme also had significant transfructosylating activity with increasing sucrose concentrations, producing various oligosaccharides. The AngInuE protein molecular mass was 57 kD...

Journal: :Bioscience, biotechnology, and biochemistry 2012
Yoshiyuki Tatsumi Yoshimasa Sasahara Noriki Kohyama Satomi Ayano Michio Endo Tadashi Yoshida Kiyoshi Yamada Mamoru Totsuka Makoto Hattori

To reduce the immunogenicity of β-lactoglobulin (BLG), we prepared wild-type bovine BLG variant A (wt) and three site-specifically glycosylated BLGs (D28N, D137N/A139S, and P153A), and expressed them in the methylotrophic yeast Pichia pastoris by fusion of the cDNA to the sequence coding for the α-factor signal peptide from Saccharomyces cerevisiae. Sodium dodecyl sulfate polyacrylamide gel ele...

2006
Ikjin Kim Jungmi Ahn Chang Liu Kaori Tanabe Jennifer Apodaca Tadashi Suzuki Hai Rao

Misfolded proteins in the endoplasmic reticulum (ER) are destroyed by a pathway termed ER-associated protein degradation (ERAD). Glycans are often removed from glycosylated ERAD substrates in the cytosol before substrate degradation, which maintains the efficiency of the proteasome. Png1, a deglycosylating enzyme, has long been suspected, but not proven, to be crucial in this process. We demons...

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