Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 177

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

c‐di‐GMP‐binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum

Weinhouse, Haim, Sapir, Shai, Amikam, Dorit, Shilo, Yehudit, Volman, Gail, Ohana, Patricia, Benziman, Moshe·1997·FEBS Letters

Abstract

A protein which specifically binds cyclic diguanylic acid (c‐di‐GMP), the reversible allosteric activator of the membrane‐bound cellulose synthase system of Acetobacter xylinum, has been identified in membrane preparations of this organism. c‐di‐GMP binding is of high affinity (K D 20 nM), saturable and reversible. The equilibrium of the reaction is markedly and specifically shifted towards the binding direction by K+. The c‐di‐GMP binding protein, structurally associated with the cellulose synthase, appears to play a major role in modulating the intracellular concentration of free c‐di‐GMP and thus may constitute an essential factor in regulating cellulose synthesis in vivo.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/s0014-5793(97)01202-7

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Cited by

See all 177

Metadata

Authors
Weinhouse, H., Sapir, S., Amikam, D., Shilo, Y., Volman, G., Ohana, P., & Benziman, M.
Venue
FEBS Letters
Publisher
Wiley
Published
1997-10-20
Volume
416
Issue
2
Pages
207-211
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2041355006
Cited by
177
References
1
FWCI
2.36
Type
journal article
Language
en
Open access
closed

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: c‐di‐GMP‐binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum. https://app.cochat.ai/papers/10.1016/s0014-5793(97)01202-7
The paper
Weinhouse, H., Sapir, S., Amikam, D., Shilo, Y., Volman, G., Ohana, P., & Benziman, M. (1997). c‐di‐GMP‐binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum. FEBS Letters. https://doi.org/10.1016/s0014-5793(97)01202-7

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.