Evidence map›Paper›PMID 30205291›Full record

ArticleJournal of molecular graphics & modelling2018

Understanding the role of glucose regulated protein 170 (GRP170) as a nucleotide exchange factor through molecular simulations.

Piyusha P Pagare, Huiqun Wang, Xiang-Yang Wang, Yan Zhang

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular graphics & modelling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
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

4 authors at 1 institution in 1 country.

Piyusha P PagareDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, 800 East Leigh Street, Richmond, VA, 23298, USA.
Huiqun WangDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, 800 East Leigh Street, Richmond, VA, 23298, USA.
Xiang-Yang WangDepartment of Human and Molecular Genetics, School of Medicine, Virginia Commonwealth University, Richmond, VA, 23298, USA; Institute of Molecular Medicine, Virginia Commonwealth University, Richmond, VA, 23298, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA, 23298, USA.
Yan ZhangDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, 800 East Leigh Street, Richmond, VA, 23298, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA, 23298, USA. Electronic address: yzhang2@vcu.edu.
Virginia Commonwealth University · US

Funding

Non-peptide Mu Opioid Receptor Selective AntagonistsR01DA024022 · NIDA · VIRGINIA COMMONWEALTH UNIVERSITY · PI ZHANG, YAN · 2009 to 2019
$3.5M
Bivalent Ligands as Chemical Probes to Study Opioid Abuse-enhanced HIV InfectionR01DA044855 · NIDA · VIRGINIA COMMONWEALTH UNIVERSITY · PI HAUSER, KURT F, ZHANG, YAN · 2017 to 2021
$2.7M
Host-tumor interactions and cancer relapse after radiation therapyR01CA175033 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI WANG, XIANG-YANG SHAWN · 2014 to 2018
$1.6M
NCI NIH HHS R01 CA175033NIDA NIH HHS R01 DA024022NIDA NIH HHS R01 DA044855
6 · The paper itself

Abstract

Glucose Regulated Protein 170 (GRP170), also called Oxygen Regulated Protein 150 (ORP150), is a major molecular chaperone resident in the endoplasmic reticulum (ER). It belongs to the heat shock protein (HSP70) super family and can be induced by conditions such as hypoxia, ischemia and interferences in calcium homeostasis. It was recently reported that GRP170 may act as a nucleotide exchange factor (NEF) for GRP78 or binding immunoglobulin protein (BiP), and the ER canonical HSP70. However, little is known about the mechanism underlying its NEF activity. In this study, two homology models of GRP170 were constructed based on the X-ray crystal structures of ADP and ATP bound HSP110, a cytosolic homolog of GRP170, in order to characterize the differences in the binding modes of both ligands. It was observed that the differences in the binding modes of ADP and ATP led to a conformation change in the substrate binding domain which could potentially influence the binding of its substrates such as BiP. Our findings help understand the effect of nucleotide binding on the function of this chaperone protein as a NEF as well as the structural differences between GRP170 and its family members.

Indexed as

Molecular Docking SimulationMolecular Dynamics SimulationAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceEndoplasmic Reticulum Chaperone BiPGlycoproteinsHSP70 Heat-Shock ProteinsMolecular ConformationNucleotidesProtein BindingProtein Interaction Domains and MotifsQuantitative Structure-Activity RelationshipAdenosine DiphosphateAdenosine TriphosphateEndoplasmic Reticulum Chaperone BiPglucose-regulated protein 170GlycoproteinsHSP70 Heat-Shock ProteinsHSPA5 protein, humanNucleotidesDockingGRP170Homology modelingNucleotide bindingNucleotide exchange factor (NEF)ORP150

Identifiers

PMID30205291
PMCPMC6197907
OpenAlexW2891046759

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.