Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

In Vitro Characterization of Guanylyl Cyclase BdPepR2 from Brachypodium distachyon Identified through a Motif-Based Approach.

International journal of molecular sciences - 10 Jun 2021

Duszyn Maria, Świeżawska-Boniecka Brygida, Wong Aloysius, Jaworski Krzysztof, Szmidt-Jaworska Adriana

Abstract excerpt

In recent years, cyclic guanosine 3',5'-cyclic monophosphate (cGMP) and guanylyl cyclases (GCs), which catalyze the formation of cGMP, were implicated in a growing number of plant processes, including plant growth and development and the responses to various stresses. To identify novel GCs in plants, an amino acid sequence of a catalytic motif with a conserved core was designed through bioinformatic analysis. In...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to Brachypodium

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Cyclic GMP

Share to Guanylate Cyclase

Share to In Vitro Techniques

Share to Mutagenesis, Site-Directed

Share to Sequence Homology

Source

Open in PubMed Open full text

Identifiers

PMID: 34200573
DOI: 10.3390/ijms22126243
PMCID: PMC8228174

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

In Vitro Characterization of Guanylyl Cyclase BdPepR2 from Brachypodium distachyon Identified through a Motif-Based Approach.PMID 34200573Read ↗

Identification of soybean CNGC gene family and screening of root rot resistance genesSemantic proximity Read ↗

Dynamic Expression, Differential Regulation and Functional Diversity of the CNGC Family Genes in Cotton.Semantic proximity Read ↗

Canonical G-protein coupled receptors of vascular plantsSemantic proximity Read ↗

Guanylate cyclase-activating proteins: structure, function, and diversitySemantic proximity Read ↗

An unusual and physiologically vital protein with guanylate cyclase and P-type ATPase like domain in a pathogenic protistSemantic proximity Read ↗

Dynamic Phosphoproteome Analysis of Seedling Leaves in Brachypodium distachyon L. Reveals Central Phosphorylated Proteins Involved in the Drought Stress Response.Semantic proximity Read ↗

Regions in vertebrate photoreceptor guanylyl cyclase ROS-GC1 involved in Ca(2+)-dependent regulation by guanylyl cyclase-activating protein GCAP-1.Semantic proximity Read ↗

Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles.Semantic proximity Read ↗

[Diversity and evolution of the guanylyl cyclase/cGMP signal transduction systems].Semantic proximity Read ↗

Identification of new members of the MAPK gene family in plants shows diverse conserved domains and novel activation loop variants.Semantic proximity Read ↗

Functional analysis of GmCPDs and investigation of their roles in flowering.Semantic proximity Read ↗

Brachypodium distachyon and Setaria viridis: Model Genetic Systems for the Grasses.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.