Evidence map›Paper›PMID 26405690›Full record

ArticleACS central science2015

Human Cancer Antigen Globo H Is a Cell-Surface Ligand for Human Ribonuclease 1.

Chelcie H Eller, Tzu-Yuan Chao, Kiran K Singarapu, Ouathek Ouerfelli, Guangbin Yang, John L Markley, Samuel J Danishefsky, Ronald T Raines

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Emerging biological functions of ribonuclease 1 and angiogenin.Critical reviews in biochemistry and molecular biology · 2022
    Review
  4. Discovery of antitumor effects of leczymes.Glycoconjugate journal · 2022
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. 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

8 authors at 1 institution in 1 country.

Chelcie H EllerDepartment of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Tzu-Yuan ChaoDepartment of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Kiran K SingarapuDepartment of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States ; Department of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Ouathek OuerfelliOrganic Synthesis Core Facility and Laboratory for Bioorganic Chemistry, Memorial Sloan Kettering Cancer Center , New York, New York 10021, United States.
Guangbin YangOrganic Synthesis Core Facility and Laboratory for Bioorganic Chemistry, Memorial Sloan Kettering Cancer Center , New York, New York 10021, United States.
John L MarkleyDepartment of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States ; Department of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Samuel J DanishefskyOrganic Synthesis Core Facility and Laboratory for Bioorganic Chemistry, Memorial Sloan Kettering Cancer Center , New York, New York 10021, United States ; Department of Chemistry, Columbia University , New York, New York 10027, United States.
Ronald T RainesDepartment of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States ; Department of Biochemistry, National Magnetic Resonance Facility at Madison, and Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Columbia University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
RIBONUCLEASES IN CANCER THERAPYR01CA073808 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1997 to 2024
$7.3M
New Synthetic Reactions to Reach Bioactive ProteinsR01GM109760 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI LUO, MINKUI · 2014 to 2017
$1.7M
NCI NIH HHS P30 CA008748NCI NIH HHS R01 CA073808NIGMS NIH HHS P41 GM103399NIGMS NIH HHS R01 GM109760NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Pancreatic-type ribonucleases are secretory enzymes that catalyze the cleavage of RNA. Recent efforts have endowed the homologues from cow (RNase A) and human (RNase 1) with toxicity for cancer cells, leading to a clinical trial. The basis for the selective toxicity of ribonuclease variants for cancerous versus noncancerous cells has, however, been unclear. A screen for RNase A ligands in an array of mammalian cell-surface glycans revealed strong affinity for a hexasaccharide, Globo H, that is a tumor-associated antigen and the basis for a vaccine in clinical trials. The affinity of RNase A and RNase 1 for immobilized Globo H is in the low micromolar-high nanomolar range. Moreover, reducing the display of Globo H on the surface of human breast adenocarcinoma cells with a small-molecule inhibitor of biosynthesis or a monoclonal antibody antagonist decreases the toxicity of an RNase 1 variant. Finally, heteronuclear single quantum coherence (HSQC) NMR spectroscopy showed that RNase 1 interacts with Globo H by using residues that are distal from the enzymic active site. The discovery that a systemic human ribonuclease binds to a moiety displayed on human cancer cells links two clinical paradigms and suggests a mechanism for innate resistance to cancer.

Identifiers

PMID26405690
PMCPMC4571170
OpenAlexW2400165260

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.