Characterization of Urtica dioica agglutinin isolectins and the encoding gene family. (Q47979761)

7 February 2018

title

Characterization of Urtica dioica agglutinin isolectins and the encoding gene family. (English)

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7 February 2018

main subject

Urtica dioica

object named as

Urtica dioica

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6

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author name string

M P Does

1

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7 February 2018

D K Ng

2

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7 February 2018

H L Dekker

3

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7 February 2018

W J Peumans

4

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7 February 2018

P M Houterman

5

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7 February 2018

B J Cornelissen

7

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7 February 2018

publication date

1 January 1999

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7 February 2018

number of pages

13

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inferred from page(s)

published in

Plant Molecular Biology

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7 February 2018

volume

39

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7 February 2018

issue

2

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page(s)

335-347

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7 February 2018

https://scigraph.springernature.com/pub.10.1023/a:1006134932290

exact match

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cites work

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12 December 2020

The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase

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The Urtica dioica Agglutinin Is a Complex Mixture of Isolectins.

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Urtica dioica agglutinin. A superantigenic lectin from stinging nettle rhizome

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12 December 2020

Wheat germ agglutinin. Evidence for a genetic basis of multiple forms

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12 December 2020

Lectins, lectin genes, and their role in plant defense

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12 December 2020

The proteins of Hevea brasiliensis Latex. 4. Isolation and characterization of crystalline hevein

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Amino acid sequence and some properties of lectin-D from the roots of pokeweed (Phytolacca americana)

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12 December 2020

Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D.

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DNA sequencing with chain-terminating inhibitors

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Lectins as plant defense proteins

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Ligand-induced perturbations in Urtica dioica agglutinin

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Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II

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The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core

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Extracellular targeting of the vacuolar tobacco proteins AP24, chitinase and beta-1,3-glucanase in transgenic plants

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Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif

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Purification of lectins by biospecific affinity chromatography

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A genetic basis for the origin of six different isolectins in hexaploid wheat

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The mannose-specific plant lectins from Cymbidium hybrid and Epipactis helleborine and the (N-acetylglucosamine)n-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replic

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12 December 2020

Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 A resolution

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12 December 2020

The primary structure of stinging nettle (Urtica dioica) agglutinin. A two-domain member of the hevein family

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12 December 2020

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12 December 2020

Isolation and characterization of a cDNA clone encoding wheat germ agglutinin

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12 December 2020

Carbohydrate binding properties of the stinging nettle (Urtica dioica) rhizome lectin

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12 December 2020

A small-scale procedure for the rapid isolation of plant RNAs.

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12 December 2020

2.2 A resolution structure analysis of two refined N-acetylneuraminyl-lactose--wheat germ agglutinin isolectin complexes

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H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus

1 reference

12 December 2020

Identifiers

DOI

10.1023/A:1006134932290

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7 February 2018

Dimensions Publication ID

0 references

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7 February 2018