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

Analysis of the peptidoglycan structure of Bacillus subtilis endospores.

Journal of bacteriology - 1 Nov 1996

Popham D L, Helin J, Costello C E, Setlow P

Abstract excerpt

Peptidoglycan was prepared from purified Bacillus subtilis spores of wild-type and several mutant strains. Digestion with muramidase resulted in cleavage of the glycosidic bonds adjacent to muramic acid replaced by peptide or alanine side chains but not the bonds adjacent to muramic lactam. Reduction of the resulting muropeptides allowed their separation by reversed-phase high-pressure liquid chromatography. The...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Bacillus subtilis
Share to Bacterial Proteins

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

Share to Carbohydrate Sequence

Share to Carrier Proteins

Share to Chromatography, High Pressure Liquid

Share to Molecular Sequence Data

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 8932300
DOI: 10.1128/jb.178.22.6451-6458.1996
PMCID: PMC178530

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Analysis of the peptidoglycan structure of Bacillus subtilis endospores.PMID 8932300Read ↗

Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties.Semantic proximity Read ↗

Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores.Semantic proximity Read ↗

Identification of sporulation genes in Bacillus anthracis highlights similarities and significant differences with Bacillus subtilis.Semantic proximity Read ↗

Characterization of LytH, a differentiation-associated peptidoglycan hydrolase of Bacillus subtilis involved in endospore cortex maturation.Semantic proximity Read ↗

Spore peptidoglycan structure in a cwlD dacB double mutant of Bacillus subtilis.Semantic proximity Read ↗

Structural analysis of Bacillus subtilis spore peptidoglycan during sporulation.Semantic proximity Read ↗

Two class A high-molecular-weight penicillin-binding proteins of Bacillus subtilis play redundant roles in sporulation.Semantic proximity Read ↗

The Bacillus anthracis SleL (YaaH) protein is an N-acetylglucosaminidase involved in spore cortex depolymerization.Semantic proximity Read ↗

Cell wall peptidoglycan architecture in Bacillus subtilis.Semantic proximity Read ↗

N-Deacetylases required for muramic-δ-lactam production are involved in Clostridium difficile sporulation, germination, and heat resistanceSemantic proximity Read ↗

The Bacillus subtilis dacB gene, encoding penicillin-binding protein 5*, is part of a three-gene operon required for proper spore cortex synthesis and spore core dehydration.Semantic proximity Read ↗

Activity and regulation of various forms of CwlJ, SleB, and YpeB proteins in degrading cortex peptidoglycan of spores of Bacillus species in vitro and during spore germination.Semantic proximity Read ↗

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