Evidence map›Paper›PMID 21827164›Full record

ArticleBiochemistry2011

Mechanism of ribonuclease A endocytosis: analogies to cell-penetrating peptides.

Tzu-Yuan Chao, Ronald T Raines

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 61 citations in OpenAlex.

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  14. Endothelial Ribonuclease 1 in Cardiovascular and Systemic Inflammation.Frontiers in cell and developmental biology · 2020
    Review
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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

2 authors at 1 institution in 1 country.

Tzu-Yuan ChaoDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Ronald T Raines
University of Wisconsin–Madison · US

Funding

RIBONUCLEASES IN CANCER THERAPYR01CA073808 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1997 to 2024
$7.3M
NCI NIH HHS R01 CA073808
6 · The paper itself

Abstract

Pancreatic-type ribonucleases can exert toxic activity by catalyzing the degradation of cellular RNA. Their ability to enter cells is essential for their cytotoxicity. Here, we determine the mechanism by which bovine pancreatic ribonuclease (RNase A) enters human cells. Inhibiting clathrin-dependent endocytosis with dynasore or chlorpromazine decreases RNase A-uptake by ~70%. Limited colocalization between RNase A and transferrin indicates that RNase A is not routed through recycling endosomes. Instead, vesicular staining of RNase A overlaps substantially with that of nona-arginine and the cationic peptide corresponding to residues 47-57 of the HIV-1 TAT protein. At low concentrations (<5 μM), internalization of RNase A and these cell-penetrating peptides (CPPs) is inhibited by chlorpromazine as well as the macropinocytosis inhibitors cytochalasin D and 5-(N-ethyl-N-isopropyl)amiloride to a similar extent, indicative of common endocytic mechanism. At high concentrations, CPPs adopt a nonendocytic mechanism of cellular entry that is not shared by RNase A. Collectively, these data suggest that RNase A is internalized via a multipathway mechanism that involves both clathrin-coated vesicles and macropinosomes. The parallel between the uptake of RNase A and CPPs validates reference to RNase A as a "cell-penetrating protein".

Indexed as

AmilorideAnimalsCattleCell-Penetrating PeptidesChlorpromazineCytochalasin DEndocytosisHeLa CellsHumansHydrazonesNystatinPeptide FragmentsRibonuclease, Pancreatictat Gene Products, Human Immunodeficiency VirusAmilorideCell-Penetrating PeptidesChlorpromazineCytochalasin DethylisopropylamilorideHydrazonesN'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazideNystatinPeptide FragmentsRibonuclease, Pancreatictat Gene Products, Human Immunodeficiency Virustat peptide (47-57), Human immunodeficiency virus 1

Identifiers

PMID21827164
PMCPMC3242730
OpenAlexW2062282451

What OpenQuestion holds

Textmetadata
LicenceTDM
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.