Institution
Agriculture and Agri-Food Canada
Facility•Ottawa, Ontario, Canada•
About: Agriculture and Agri-Food Canada is a facility organization based out in Ottawa, Ontario, Canada. It is known for research contribution in the topics: Population & Soil water. The organization has 10921 authors who have published 21332 publications receiving 748193 citations. The organization is also known as: Department of Agriculture and Agri-Food.
Topics: Population, Soil water, Gene, Manure, Tillage
Papers published on a yearly basis
Papers
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TL;DR: In this article, a chitin nanoparticles of about 50-100nm were obtained after consecutive acid hydrolysis and mechanical ultrasonication treatments, and the morphology, structural, thermal and mechanical properties of the nanocomposites were evaluated by electron microscopy, X-ray diffraction, dynamic mechanical thermal analysis, and tensile tests.
175 citations
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TL;DR: Investigation of the use of an automated, RFID driven, noninvasive infrared thermography technology to determine BRD in cattle demonstrated that true positive animals for BRD based on a gold standard displayed higher peak infrared thermal values than true negative animals.
175 citations
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TL;DR: What is known about the predominant storage proteins of commercially produced Brassicaceae seeds relative to the chemistry, nutritional value, as well as the functionality in foods, and associated non-protein components of canola/rapeseed storage proteins is critically reviewed.
Abstract: Among the commercially cultivated Brassicaceae (Cruciferae) plants, Brassica juncea, Brassica napus, Brassica rapa, and Sinapis alba store significant amounts of oil and protein in the seed. At present, Brassica seed proteins are primarily used for livestock feeding based on the nutritional value. The point of curiosity is whether the present knowledge on the protein structure, biochemical characteristics, nutritive value, and the recovery processes are inadequate to develop Brassica proteins into a usable plant protein source or these proteins are of substandard for uses beyond animal nutrition applications. Cruciferin (11S) and napin (2S) are the predominant storage proteins of Brassicaceae seeds that contribute to different properties and functions. A gamut of information is available on the chemistry, nutritional value, as well as the functionality in foods, and associated non-protein components of canola/rapeseed storage proteins. The intention of this article is to critically review what is known about the predominant storage proteins of commercially produced Brassicaceae seeds relative to the above aspects and identify the knowledge gaps.
175 citations
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TL;DR: In this article, an approach to integrate crop stressors and crop descriptors derived from optical remote sensing data with the Monteith radiation use efficiency model was developed for estimating crop aboveground dry biomass and yield.
174 citations
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TL;DR: In situ localization of PCP-A1 transcripts revealed that they accumulate specifically in pollen at the late binucleate/trinucleate stage of development rather than in the tapetum, which previously was taken to be the principal source of the pollen coat.
Abstract: Self-incompatibility (SI) in Brassica species is controlled by a single polymorphic locus (S) with multiple specificities. Two stigmatically expressed genes that have been cloned from this region encode the S locus glycoprotein (SLG) and S receptor kinase (SRK). Both appear to be essential for the operation of SI. It is believed that rejection of incompatible pollen grains is effected by recognition events between an as yet unidentified S locus-encoded pollen coating-borne protein and the SLG/SRK. We previously identified a small pollen coat protein PCP7 (renamed here PCP-A1, for pollen coat protein, class A, 1) that binds with high affinity to SLGs irrespective of S genotype. Here, we report the cloning of PCP-A1 from Brassica oleracea and demonstrate that it is unlinked to the S locus. In situ localization of PCP-A1 transcripts revealed that they accumulate specifically in pollen at the late binucleate/trinucleate stage of development rather than in the tapetum, which previously was taken to be the principal source of the pollen coat. PCP-A1 is characterized by the presence of a structurally important motif consisting of eight cysteine residues shared by the plant defensins. Based on the presence of this motif and other data, homology modeling has been used to produce a putative structure for PCP-A1. Protein-protein interaction analyses demonstrate that SLG exists in monomeric and dimeric forms, both of which bind PCP-A1. Evidence is also presented for the existence of putative membrane-associated PCP-A1 binding proteins in stigmatic tissue.
174 citations
Authors
Showing all 10964 results
Name | H-index | Papers | Citations |
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Fereidoon Shahidi | 119 | 951 | 57796 |
Miao Liu | 111 | 993 | 59811 |
Xiang Li | 97 | 1472 | 42301 |
Eviatar Nevo | 95 | 848 | 40066 |
Tim A. McAllister | 85 | 862 | 32409 |
Hubert Kolb | 84 | 420 | 25451 |
Daniel M. Weary | 83 | 437 | 22349 |
Karen A. Beauchemin | 83 | 423 | 22351 |
Nanthi Bolan | 83 | 550 | 31030 |
Oene Oenema | 80 | 361 | 23810 |
Santosh Kumar | 80 | 1196 | 29391 |
Yueming Jiang | 79 | 452 | 20563 |
Denis A. Angers | 76 | 256 | 19321 |
Tong Zhu | 72 | 472 | 18205 |
Christophe Lacroix | 69 | 353 | 15860 |