A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat.

Christina Geerds, Willem M Bleymüller, Timo Meyer, Christiane Widmann, Hartmut H Niemann

Open access · hybridAbstract read

In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it

0cells of the map it votes in

2citing papers in PubMed

0.4field-weighted citation impact, top 34% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 3 citations in OpenAlex.

Bacterial exo-α-sialidases subvert the complement system through desialylation.bioRxiv : the preprint server for biology · 2026
Article
Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.Acta crystallographica. Section F, Structural biology communications · 2026
Article

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Christina GeerdsDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.

Willem M BleymüllerDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.

Timo MeyerDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.

Christiane WidmannDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.ORCID 0000-0002-3444-9995

Hartmut H NiemannDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.ORCID 0000-0002-8582-0360

Bielefeld University · DE

Funding

Helmholtz-Zentrum Berlin für Materialien und Energie BESSY 2: 65

6 · The paper itself

Abstract

InlB, a bacterial agonist of the human receptor tyrosine kinase MET, consists of an N-terminal internalin domain, a central B repeat and three C-terminal GW domains. In all previous structures of full-length InlB or an InlB construct lacking the GW domains (InlB

Indexed as

Listeria monocytogenesBacterial ProteinsBinding SitesHumansMembrane ProteinsModels, MolecularProto-Oncogene Proteins c-metBacterial ProteinsMembrane ProteinsProto-Oncogene Proteins c-metbinding sitescrystal contactscrystallization propensityInlBListeria monocytogenesprotein–protein interactions

Identifiers

PMID35234145

DOI10.1107/S2059798322000432

PMCPMC8900821

OpenAlexW4212876352

What OpenQuestion holds

Textmetadata

LicenceCC BY

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.