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

A single amino acid substitution in the antimicrobial defense protein cecropin B is associated with diminished degradation by leaf intercellular fluid.

Molecular plant-microbe interactions : MPMI - 1 May 1997

Owens L D, Heutte T M

Abstract excerpt

Degradation is one of several factors that may affect the level of accumulation of transgene products in plants. In plants engineered to secrete antimicrobial proteins to the intercellular compartment of leaves, the degenerative activity of proteases residing in leaf intercellular fluid (IF) could be critical to achieving the expected transgene function. We synthesized a structural analogue (MB39) of the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Insect Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microbial Sensitivity Tests

Share to Molecular Sequence Data

Share to Mutation

Share to Plants

Share to Recombinant Proteins

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 9150599
DOI: 10.1094/MPMI.1997.10.4.525

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A single amino acid substitution in the antimicrobial defense protein cecropin B is associated with diminished degradation by leaf intercellular fluid.PMID 9150599Read ↗

Transgenic plants expressing cationic peptide chimeras exhibit broad-spectrum resistance to phytopathogens.Semantic proximity Read ↗

Synthetic MicroProteins: Versatile Tools for Posttranslational Regulation of Target Proteins.Semantic proximity Read ↗

Expression of an engineered heterologous antimicrobial peptide in potato alters plant development and mitigates normal abiotic and biotic responses.Semantic proximity Read ↗

Evolution of antimicrobial cysteine-rich peptides in plantsSemantic proximity Read ↗

<i>Botrytis cinerea</i> BcPTP1 is a late infection phase, cysteine rich protein cytotoxic effectorSemantic proximity Read ↗

Biophysical and proteomic analyses suggest functions of <i>Pseudomonas syringae</i> pv <i>tomato</i> DC3000 extracellular vesicles in bacterial growth during plant infectionSemantic proximity Read ↗

Chickpea NCR13 disulfide cross-linking variants exhibit profound differences in antifungal activity and modes of actionSemantic proximity Read ↗

A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogenSemantic proximity Read ↗

The alteration of plant morphology by small peptides released from the proteolytic processing of the bacterial peptide TENGU.Semantic proximity Read ↗

Constitutive expression of transgenes encoding derivatives of the synthetic antimicrobial peptide BP100: impact on rice host plant fitnessSemantic proximity Read ↗

Modes of action and <i>in planta</i> antifungal activity of <i>Olea europaea</i> defensin OefDef1.1-derived peptide variantSemantic proximity Read ↗

P1 peptidase--a mysterious protein of family Potyviridae.Semantic proximity Read ↗

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