Evidence map›Paper›PMID 30254158›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

The interaction of talin with the cell membrane is essential for integrin activation and focal adhesion formation.

Krishna Chinthalapudi, Erumbi S Rangarajan, Tina Izard

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Synergistic effect of PIPBiophysical journal · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Novel Drug Targets in Diastolic Heart Disease.International journal of molecular sciences · 2025
    Review
  10. CLIC1 Supports Mechanisms Related to Platelet Activation and Thrombosis.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2025
    Article
  11. Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. Review
  13. Article
  14. Biochemical and structural bases for talin ABSs-F-actin interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Krishna ChinthalapudiCell Adhesion Laboratory, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458.
Erumbi S RangarajanCell Adhesion Laboratory, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458.
Tina IzardCell Adhesion Laboratory, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458 cmorrow@scripps.edu.
Scripps Research Institute · US

Funding

Mechanisms Directing Adherens Junctions and Actin Network InteractionsR01GM094483 · NIGMS · SCRIPPS FLORIDA · PI IZARD, TINA · 2011 to 2019
$3.2M
NIGMS NIH HHS R01 GM094483
6 · The paper itself

Abstract

Multicellular organisms have well-defined, tightly regulated mechanisms for cell adhesion. Heterodimeric αβ integrin receptors play central roles in this function and regulate processes for normal cell functions, including signaling, cell migration, and development, binding to the extracellular matrix, and senescence. They are involved in hemostasis and the immune response, participate in leukocyte function, and have biological implications in angiogenesis and cancer. Proper control of integrin activation for cellular communication with the external environment requires several physiological processes. Perturbation of these equilibria may lead to constitutive integrin activation that results in bleeding disorders. Furthermore, integrins play key roles in cancer progression and metastasis in which certain tumor types exhibit higher levels of various integrins. Thus, the integrin-associated signaling complex is important for cancer therapy development. During inside-out signaling, the cytoskeletal protein talin plays a key role in regulating integrin affinity whereby the talin head domain activates integrin by binding to the cytoplasmic tail of β-integrin and acidic membrane phospholipids. To understand the mechanism of integrin activation by talin, we determined the crystal structure of the talin head domain bound to the acidic phospholipid phosphatidylinositol 4,5-bisphosphate (PIP

Indexed as

Allosteric RegulationAnimalsBinding SitesCell MembraneCHO CellsCricetulusCrystallography, X-RayFocal AdhesionsIntegrinsModels, MolecularPhosphatidylinositol 4,5-DiphosphateProtein ConformationProtein DomainsTalinIntegrinsPhosphatidylinositol 4,5-DiphosphateTalinangiogenesiscell adhesionintegrin activationphospholipidstalin activation

Identifiers

PMID30254158
PMCPMC6187153
OpenAlexW2893450916

What OpenQuestion holds

Textmetadata
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.