Evidence map›Paper›PMID 31535027›Full record

ArticleScience advances2019

Structure of human Vitronectin C-terminal domain and interaction with

Kyungsoo Shin, Bernhard C Lechtenberg, Lynn M Fujimoto, Yong Yao, Sara Schesser Bartra, Gregory V Plano, Francesca M Marassi

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Complement System.Advances in experimental medicine and biology · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Peptide location fingerprinting identifies structural alterations within basement membrane components in ageing kidney.Matrix biology : journal of the International Society for Matrix Biology · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Engineering a HyperstableJournal of the American Chemical Society · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Nanonewton forces betweenNanoscale advances · 2020
    Article
  20. 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

7 authors at 2 institutions in 1 country.

Kyungsoo ShinCancer Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.ORCID 0000-0003-4836-8798
Bernhard C LechtenbergCancer Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.ORCID 0000-0002-5674-6894
Lynn M FujimotoCancer Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.ORCID 0000-0002-7239-1501
Yong YaoCancer Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.ORCID 0000-0002-9113-7656
Sara Schesser BartraDepartment of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, FL 33101, USA.
Gregory V PlanoDepartment of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, FL 33101, USA.
Francesca M MarassiCancer Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.ORCID 0000-0003-2695-5844
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of Miami · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI ELENA B PASQUALE · 1985 to 2026
$107.2M
Membrane Protein Effectors of Pathogen Interactions With HostR35GM118186 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Francesca M Marassi · 2016 to 2026
$8.5M
Role of Yersinia pestis Ail-host ligand interactions in plagueR01AI130009 · NIAID · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI PLANO, GREGORY V · 2017 to 2021
$2.2M
NCI NIH HHS P30 CA030199NIAID NIH HHS R01 AI130009NIGMS NIH HHS R35 GM118186
6 · The paper itself

Abstract

Vitronectin (Vn) is a major component of blood that controls many processes central to human biology. It is a drug target and a key factor in cell and tissue engineering applications, but despite long-standing efforts, little is known about the molecular basis for its functions. Here, we define the domain organization of Vn, report the crystal structure of its carboxyl-terminal domain, and show that it harbors the binding site for the

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBinding SitesCrystallography, X-RayHumansProtein BindingProtein ConformationSequence HomologyVirulence FactorsVitronectinYersinia pestisAil protein, Yersinia pestisBacterial Outer Membrane ProteinsVirulence FactorsVitronectin

Identifiers

PMID31535027
PMCPMC6739113
OpenAlexW2972812798

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.