Evidence map›Paper›PMID 36180783›Full record

ArticleCommunications biology2022

Structural analysis of human CEACAM1 oligomerization.

Amit K Gandhi, Zhen-Yu J Sun, Yu-Hwa Huang, Walter M Kim, Chao Yang, Gregory A Petsko, Nicole Beauchemin, Richard S Blumberg

Abstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024
    Review
  3. CEACAM1 in vascular homeostasis and inflammation.European journal of clinical investigation · 2024
    Review
  4. Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024
    Review
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

8 authors.

Amit K Gandhi *Division of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA, 02115, USA. agandhi2@bwh.harvard.edu.ORCID 0000-0003-0654-1097
Zhen-Yu J Sun *Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, 02215, USA.ORCID 0000-0001-7527-6026
Yu-Hwa HuangDivision of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA, 02115, USA.
Walter M KimDivision of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA, 02115, USA.
Chao YangDivision of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA, 02115, USA.
Gregory A PetskoAnn Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, 02115, USA.ORCID 0000-0003-3668-3694
Nicole BeaucheminRosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC, Canada.
Richard S BlumbergDivision of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA, 02115, USA. rblumberg@bwh.harvard.edu.ORCID 0000-0002-9704-248X

Funding

Regulation of Mucosal LymphocytesR01DK051362 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI Richard S Blumberg, Yu-Hwa Huang Blumberg · 1997 to 2026
$13.5M
600 MHz NMR Spectrometer ConsoleS10OD028526 · OD · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2020 to 2020
$649k
NIDDK NIH HHS R01 DK051362NIH HHS S10 OD028526
6 · The paper itself

Abstract

The human (h) CEACAM1 GFCC' face serves as a binding site for homophilic and heterophilic interactions with various microbial and host ligands. hCEACAM1 has also been observed to form oligomers and micro-clusters on the cell surface which are thought to regulate hCEACAM1-mediated signaling. However, the structural basis for hCEACAM1 higher-order oligomerization is currently unknown. To understand this, we report a hCEACAM1 IgV oligomer crystal structure which shows how GFCC' face-mediated homodimerization enables highly flexible ABED face interactions to arise. Structural modeling and nuclear magnetic resonance (NMR) studies predict that such oligomerization is not impeded by the presence of carbohydrate side-chain modifications. In addition, using UV spectroscopy and NMR studies, we show that oligomerization is further facilitated by the presence of a conserved metal ion (Zn

Indexed as

Antigens, CDCell Adhesion MoleculesBinding SitesCarbohydratesHumansAntigens, CDCarbohydratesCD66 antigensCell Adhesion Molecules

Identifiers

PMID36180783
PMCPMC9525683

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.