ArticleGlycoconjugate journal1996
Primary structure of the N-linked carbohydrate chains of Calreticulin from spinach leaves.
Article in Glycoconjugate journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 47 citations in OpenAlex.
- Targeting Glycoproteins as a therapeutic strategy for diabetes mellitus and its complications.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2020Review
- Localization of rabies virus glycoprotein into the endoplasmic reticulum produces immunoprotective antigen.The protein journal · 2012Article
- Physiological roles of plant glycoside hydrolases.Planta · 2008Review
- Expression of the high capacity calcium-binding domain of calreticulin increases bioavailable calcium stores in plants.Transgenic research · 2002Article
- Influence of KDEL on the fate of trimeric or assembly-defective phaseolin: selective use of an alternative route to vacuoles.The Plant cell · 2001Article
- Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention.The Plant cell · 2000Article
- Calreticulin: one protein, one gene, many functions.The Biochemical journal · 1999Review
- Saturation of the endoplasmic reticulum retention machinery reveals anterograde bulk flowThe Plant cell · 1999Article
- N-glycoprotein biosynthesis in plants: recent developments and future trends.Plant molecular biology · 1998Review
- BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stressThe Plant cell · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calreticulin is a multifunctional Ca(2+)-binding protein of the endoplasmic reticulum of most eukaryotic cells. The 56 kDa Calreticulin glycoprotein isolated from spinach (Spinacia oleracea L.) leaves was N-deglycosylated by PNGase-F digestion. The carbohydrate moiety was isolated by gel permeation chromatography and purified by high-pH anion-exchange chromatography. The fractions were investigated by 500 MHz 1H-NMR spectroscopy, in combination with monosaccharide analysis and fast-atom bombardment-mass spectrometry. The following carbohydrate structure could be established as the major component (Man8GlcNAc2): (sequence see text) Heterogeneity was demonstrated by the presence of two minor components being Man7GlcNAc2 lacking a terminal residue (D1 or D3), compared to the major component. A cross-reactivity with an antibody against the endoplasmic reticulum retention signal HDEL was also found.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.