Evidence map›Paper›PMID 20959092›Full record

ArticleBiophysical journal2010

Electrostatic interactions and binding orientation of HIV-1 matrix studied by neutron reflectivity.

Hirsh Nanda, Siddhartha A K Datta, Frank Heinrich, Mathias Lösche, Alan Rein, Susan Krueger, Joseph E Curtis

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  4. Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  10. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

7 authors at 4 institutions in 1 country.

Hirsh NandaNIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland, USA. hirsh.nanda@nist.gov
Siddhartha A K Datta
Frank Heinrich
Mathias Lösche
Alan Rein
Susan Krueger
Joseph E Curtis
National Cancer Institute · USNational Institute of Standards and Technology · USNIST Center for Neutron Research · USCarnegie Mellon University · US

Funding

Retrovirus Assembly and MaturationZIABC010511 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI REIN, ALAN · 2009 to 2025
$9.4M
STRUCTURAL&FUNCTIONAL INESTIGATIONS OF AB OLIGOMER INTERACTION/SYNTHETIC MEMBRANEP01AG032131 · NIA · CARNEGIE-MELLON UNIVERSITY · PI DESEMO, MARKUS · 2009 to 2011
$1.9M
Intramural NIH HHSNIA NIH HHS 1P01 AG032131NIA NIH HHS P01 AG032131
6 · The paper itself

Abstract

The N-terminal matrix (MA) domain of the HIV-1 Gag protein is responsible for binding to the plasma membrane of host cells during viral assembly. The putative membrane-binding interface of MA was previously mapped by means of mutagenesis and analysis of its trimeric crystal structure. However, the orientation of MA on membranes has not been directly determined by experimental measurements. We present neutron reflectivity measurements that resolve the one-dimensional scattering length density profile of MA bound to a biomimetic of the native viral membrane. A molecular refinement procedure was developed using atomic structures of MA to determine the orientation of the protein on the membrane. The orientation defines a lipid-binding interface consistent with previous mutagenesis results. The MA protein maintains this orientation without the presence of a myristate group, driven only by electrostatic interactions. Furthermore, MA is found to penetrate the membrane headgroup region peripherally such that only the side chains of specific Lys and Arg residues interact with the surface. The results suggest that electrostatic interactions are sufficient to favorably orient MA on viral membrane mimics. The spatial determination of the membrane-bound protein demonstrates the ability of neutron reflectivity to discern orientation and penetration under physiologically relevant conditions.

Indexed as

Neutron DiffractionStatic ElectricityCell Membranegag Gene Products, Human Immunodeficiency VirusHIV-1Models, MolecularMonte Carlo MethodProtein BindingProtein Structure, TertiarySoftwaregag Gene Products, Human Immunodeficiency Virus

Identifiers

PMID20959092
PMCPMC2955346
OpenAlexW2151296405

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.