ArticleProceedings of the National Academy of Sciences of the United States of America2004
Structure of vaccinia complement protein in complex with heparin and potential implications for complement regulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 16 papers.
What it found
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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.
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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.
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Who cites it
16 citing papers in PubMed, 56 citations in OpenAlex.
- Complement-Independent Modulation of Influenza A Virus Infection by Factor H.Frontiers in immunology · 2020Article
- Heparan Sulfate Regulates the Structure and Function of Osteoprotegerin in Osteoclastogenesis.The Journal of biological chemistry · 2016Article
- Demystifying heparan sulfate-protein interactions.Annual review of biochemistry · 2014Review
- Enhancing complement control on endothelial barrier reduces renal post-ischemia dysfunction.The Journal of surgical research · 2011Article
- Influence of glycosylation and oligomerization of vaccinia virus complement control protein on level and pattern of functional activity and immunogenicity.Protein & cell · 2010Article
- Fraud rocks protein community.Nature · 2009Article
- Poxvirus proteomics and virus-host protein interactions.Microbiology and molecular biology reviews : MMBR · 2009Review
- Smallpox inhibitor of complement enzymes (SPICE): dissecting functional sites and abrogating activity.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Smallpox inhibitor of complement enzymes (SPICE): regulation of complement activation on cells and mechanism of its cellular attachment.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- The structure of complement C3b provides insights into complement activation and regulation.Nature · 2006Article
- Immunophysical properties and prediction of activities for vaccinia virus complement control protein and smallpox inhibitor of complement enzymes using molecular dynamics and electrostatics.Biophysical journal · 2006Article
- Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.The EMBO journal · 2006Article
- Dissecting the regions of virion-associated Kaposi's sarcoma-associated herpesvirus complement control protein required for complement regulation and cell binding.Journal of virology · 2006Article
- Identification of complement regulatory domains in vaccinia virus complement control protein.Journal of virology · 2005Article
- Article
- Electrostatic modeling predicts the activities of orthopoxvirus complement control proteins.Journal of immunology (Baltimore, Md. : 1950) · 2005Article
Corrections and comments
- Retraction · 2018-07-05Investigation by Company/Institution · Investigation by ORI · Misconduct - Official Investigation(s) and/or Finding(s) · Misconduct by Author · · H M Krishna Murthy has NIH finding of misconduct - see https://www.federalregister.gov/documents/2018/04/16/2018-07782/findings-of-research-misconduct;
- Expression of concern · 2010-04-06Concerns/Issues about Data · · H M Krishna Murthy has NIH finding of misconduct
- Commented on by
- Expression of concern
- Retracted
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Vaccinia virus complement control protein (VCP), a homolog of the regulators of the complement activation family of proteins, inhibits complement activation through mechanisms similar to human fluid-phase complement regulators factor H and C4b-binding protein. VCP has a heparin-binding activity that assists vaccinia in host interactions. Interaction with cell-surface polyanions like heparin is centrally important in the functioning of fluid-phase complement regulators and is the basis of host-target discrimination by the alternative pathway. We report the structure of VCP in complex with a heparin decasaccharide, which reveals changes in VCP that might be pertinent to complement regulation. Properties that VCP shares with fluid-phase complement regulators suggest that such conformational changes may be of relevance in the functioning of other complement regulators. Additionally, comparison of VCP-heparin interactions with potentially similar interactions in factor H might enable understanding of the structural basis of familial hemolytic uremic syndrome, attributed to mutational disruption of heparin and C3b binding by factor H.
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Registered trials
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.