Evidence map›Paper›PMID 26715031›Full record

ReviewAntioxidants & redox signaling2016

Regulation of Posttranslational Modifications of HMGB1 During Immune Responses.

Yiting Tang, Xin Zhao, Daniel Antoine, Xianzhong Xiao, Haichao Wang, Ulf Andersson, Timothy R Billiar, Kevin J Tracey, Ben Lu

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Antioxidants & redox signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed, 1 pooled it
4.7field-weighted citation impact, top 4% 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

74 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.

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14 more citing papers are in PubMed but not listed here.

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 6 institutions in 4 countries.

Yiting Tang1 Department of Hematology, The 3rd Xiangya Hospital, Central South University , Changsha, China .
Xin Zhao1 Department of Hematology, The 3rd Xiangya Hospital, Central South University , Changsha, China .
Daniel Antoine4 Department of Molecular and Clinical Pharmacology, Medical Research Council Centre for Drug Safety Science, University of Liverpool , Liverpool, United Kingdom .
Xianzhong Xiao5 Hunan Province Key Laboratory of Sepsis and Translational Medicine, Xiangya School of Medicine, Central South University , Changsha, China .
Haichao Wang7 Department of Emergency Medicine, North Shore University Hospital , Manhasset, New York.
Ulf Andersson8 Department of Women's and Children's Health, Karolinska Institutet , Stockholm, Sweden .
Timothy R Billiar9 Department of Surgery, University of Pittsburgh Medical Center , Pittsburgh, Pennsylvania.
Kevin J Tracey10 Center of Biomedical Science, Feinstein Institute for Medical Research , Manhasset, New York.
Ben Lu1 Department of Hematology, The 3rd Xiangya Hospital, Central South University , Changsha, China .
Central South University · CNFeinstein Institute for Medical Research · USKarolinska Institutet · SENorth Shore University Hospital · USUniversity of Liverpool · GBUniversity of Pittsburgh Medical Center · US

Funding

Molecular Basis of Bioelectronic MedicineR35GM118182 · NIGMS · FEINSTEIN INSTITUTE FOR MEDICAL RESEARCH · PI TRACEY, KEVIN J · 2016 to 2025
$7.3M
Mechanisms of Novel Herbal Therapies for Sepsis.R01AT005076 · NCCIH · FEINSTEIN INSTITUTE FOR MEDICAL RESEARCH · PI WANG, HAICHAO · 2010 to 2023
$4.3M
Regulation of HMGB1 Release in Endotoxemia.R01GM063075 · NIGMS · NORTH SHORE UNIVERSITY HOSPITAL · PI WANG, HAICHAO · 2002 to 2020
$4.2M
NCCIH NIH HHS R01 AT005076NIGMS NIH HHS R01 GM063075
6 · The paper itself

Abstract

significanceHigh-mobility group protein 1 (HMGB1) is an evolutionarily conserved and multifunctional protein. The biological function of HMGB1 depends on its cellular locations, binding partners, and redox states. Extracellular HMGB1 is a mediator of inflammation during infection or tissue injury. Immune cells actively release HMGB1 in response to infection, which in turn orchestrates both innate and adaptive immune responses. RECENT ADVANCES: Hyperacetylation of HMGB1 within its nuclear localization sequences mobilizes HMGB1 from the nucleus to the cytoplasm and subsequently promotes HMGB1 release. The redox states of the cysteines in positions 23, 45, and 106 determine the biological activity of the extracellular HMGB1. CRITICAL ISSUES: The full picture and the detailed molecular mechanisms of how cells regulate the posttranslational modifications and the redox status of HMGB1 during immune responses or under stress not only unravel the molecular mechanisms by which cells regulate the release and the biological function of HMGB1 but may also provide novel therapeutic targets to treat inflammatory diseases. FUTURE DIRECTIONS: It is important to identify the signaling pathways that regulate the posttranslational modifications and the redox status of HMGB1 and find their roles in host immune responses and pathogenesis of diseases.

Indexed as

HMGB1 ProteinHumansProtein Processing, Post-TranslationalHMGB1 ProteinHMGB1 protein, human

Identifiers

PMID26715031
PMCPMC5349223
OpenAlexW2260003929

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.