Related Experiment Video

Updated: Jun 23, 2026

mRNA Interactome Capture from Plant Protoplasts
12:29

mRNA Interactome Capture from Plant Protoplasts

Published on: July 28, 2017

Calreticulin: conserved protein and diverse functions in plants

Xiao-Yun Jia1, Li-Heng He, Rui-Lian Jing

  • 1Center for Agricultural Biotechnology, Shanxi Agricultural University, Taigu, Shanxi, 030801, China.

Physiologia Plantarum
|May 21, 2009
PubMed

More Related Videos

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis07:54

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Identification of Post-translational Modifications of Plant Protein Complexes10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Related Concept Videos

Cell Signaling in Plants01:25

Cell Signaling in Plants

Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
Cell Adhesion in Plants01:14

Cell Adhesion in Plants

Plants have rigid cell walls that are made up of cell wall polysaccharides that mediate cell-cell adhesion. The primary cell walls of plants consist of two independent and interacting polysaccharide networks: a pectin matrix that embeds the second network comprising cellulose and hemicelluloses.
Pectins are complex heteropolymers mainly composed of negatively-charged α-D-glucopyranosyl uronic acid and some neutral glycosyl residues such as α-L-rhamnopyranose, α-L-arabinofuranose, and...
Introduction to Plant Diversity02:22

Introduction to Plant Diversity

From Water to Land
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...