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

Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis.

Journal of experimental botany - 1 Jan 2008

Grimaud Florent, Rogniaux Hélène, James Martha G, Myers Alan M, Planchot Véronique

Abstract excerpt

In addition to the exclusively granule-bound starch synthase GBSSI, starch granules also bind significant proportions of other starch biosynthetic enzymes, particularly starch synthases (SS) SSI and SSIIa, and starch branching enzyme (BE) BEIIb. Whether this association is a functional aspect of starch biosynthesis, or results from non-specific entrapment during amylopectin crystallization, is not known. This...

Read the complete abstract on PubMed

Topics

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

Share to 1,4-alpha-Glucan Branching Enzyme
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphorylation

Share to Plant Proteins

Share to Proteomics

Share to Starch

Share to Starch Synthase

Share to Zea mays

Source

Open in PubMed Open full text

Identifiers

PMID: 18653693
DOI: 10.1093/jxb/ern198
PMCID: PMC2529236

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis.PMID 18653693Read ↗

Glucan affinity of starch synthase IIa determines binding of starch synthase I and starch-branching enzyme IIb to starch granules.Semantic proximity Read ↗

The amylose extender mutant of maize conditions novel protein-protein interactions between starch biosynthetic enzymes in amyloplasts.Semantic proximity Read ↗

Protein-protein interactions among enzymes of starch biosynthesis in high-amylose barley genotypes reveal differential roles of heteromeric enzyme complexes in the synthesis of A and B granules.Semantic proximity Read ↗

Allelic variants of the amylose extender mutation of maize demonstrate phenotypic variation in starch structure resulting from modified protein-protein interactions.Semantic proximity Read ↗

The different effects of starch synthase IIa mutations or variation on endosperm amylose content of barley, wheat and rice are determined by the distribution of starch synthase I and starch branching enzyme IIb between the starch granule and amyloplast stroma.Semantic proximity Read ↗

Inactivation of rice starch branching enzyme IIb triggers broad and unexpected changes in metabolism by transcriptional reprogramming.Semantic proximity Read ↗

Biomolecular analyses of starch and starch granule proteins in the high-amylose rice mutant Goami 2.Semantic proximity Read ↗

Starch Synthase 3 isoforms are essential for normal starch granule initiation in wheat endosperm.Semantic proximity Read ↗

The CBM48 domain-containing protein FLO6 regulates starch synthesis by interacting with SSIVb and GBSS in rice.Semantic proximity Read ↗

Starch phosphorylation and the in vivo regulation of starch metabolism and characteristics.Semantic proximity Read ↗

Mutation of the maize sbe1a and ae genes alters morphology and physical behavior of wx-type endosperm starch granules.Semantic proximity Read ↗

Multi-omics analyses reveal mechanism for high resistant starch formation in an indica rice SSIIIa mutant.Semantic proximity Read ↗

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