Evidence map›Paper›PMID 26425924›Full record

ArticleJournal of the American Chemical Society2015

Time-Resolved Proteomic Visualization of Dendrimer Cellular Entry and Trafficking.

Linna Wang, Li Yang, Li Pan, Naveen Reddy Kadasala, Liang Xue, Robert J Schuster, Laurie L Parker, Alexander Wei, W Andy Tao

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. 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
1.1field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Tracking Pathogen Infections by Time-Resolved Chemical Proteomics.Angewandte Chemie (International ed. in English) · 2020
    Article
  4. 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

9 authors at 2 institutions in 1 country.

Linna Wang *Department of Biochemistry, Purdue University, West Lafayette, IN, 47907, United States.
Li Yang *Department of Biochemistry, Purdue University, West Lafayette, IN, 47907, United States.
Li PanDepartment of Medicinal Chemistry & Molecular Pharmacology, Purdue University, West Lafayette, IN, 47907, United States.
Naveen Reddy KadasalaDepartment of Chemistry, Purdue University, West Lafayette, IN, 47907, United States.
Liang XueDepartment of Biochemistry, Purdue University, West Lafayette, IN, 47907, United States.
Robert J SchusterDepartment of Medicinal Chemistry & Molecular Pharmacology, Purdue University, West Lafayette, IN, 47907, United States.
Laurie L ParkerDepartment of Medicinal Chemistry & Molecular Pharmacology, Purdue University, West Lafayette, IN, 47907, United States.
Alexander WeiDepartment of Chemistry, Purdue University, West Lafayette, IN, 47907, United States.
W Andy TaoDepartment of Biochemistry, Purdue University, West Lafayette, IN, 47907, United States.
Purdue University West Lafayette · USCenter for Cancer Research · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
New Proteomic Technologies for the Analysis of Tyrosine Kinase Signaling PathwaysR01GM088317 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2010 to 2014
$1.6M
Proteomic Studies of Dendrimer-based NanomedicinesR21RR025802 · NCRR · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2009 to 2011
$555k
NCI NIH HHS P30 CA023168NCRR NIH HHS 5R21RR025802NCRR NIH HHS R21 RR025802NIGMS NIH HHS 5R01GM088317NIGMS NIH HHS R01 GM088317
6 · The paper itself

Abstract

Our understanding of the complex cell entry pathways would greatly benefit from a comprehensive characterization of key proteins involved in this dynamic process. Here we devise a novel proteomic strategy named TITAN (Tracing Internalization and TrAfficking of Nanomaterials) to reveal real-time protein-dendrimer interactions using a systems biology approach. Dendrimers functionalized with photoreactive cross-linkers were internalized by HeLa cells and irradiated at set time intervals, then isolated and subjected to quantitative proteomics. In total, 809 interacting proteins cross-linked with dendrimers were determined by TITAN in a detailed temporal manner during dendrimer internalization, traceable to at least two major endocytic mechanisms, clathrin-mediated and caveolar/raft-mediated endocytosis. The direct involvement of the two pathways was further established by the inhibitory effect of dynasore on dendrimer uptake and changes in temporal profiles of key proteins.

Indexed as

ProteomicsBiological TransportDendrimersHeLa CellsHumansDendrimers

Identifiers

PMID26425924
PMCPMC4766814
OpenAlexW2200905768

What OpenQuestion holds

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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.