Evidence map›Paper›PMID 24811874›Full record

ArticleBiochemistry2014

Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.

Kinsley C French, Nadia R Roan, George I Makhatadze

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018
    Review
  4. Article
  5. Article
  6. Amyloid formation: functional friend or fearful foe?Journal of internal medicine · 2016
    Review
  7. Article
  8. Article
  9. 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

3 authors at 2 institutions in 1 country.

Kinsley C FrenchDepartment of Biological Sciences and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute , Troy, New York 12180, United States.
Nadia R Roan
George I Makhatadze
Rensselaer Polytechnic Institute · USUniversity of California, San Francisco · US

Funding

Virology CoreP30AI027763 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STEVEN Grant DEEKS · 1988 to 2026
$93.6M
Computational and Experimental Studies of the Amyloid Fibril Formation by PAPf39R21GM101134 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI MAKHATADZE, GEORGE I · 2012 to 2013
$418k
Exploring the Role of Semen Amyloids in Promoting HIV Infection and FertilizationK99AI104262 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ROAN, NADIA R · 2013 to 2013
$133k
NIAID NIH HHS 1K99AI104262-01A1NIGMS NIH HHS 1R21GM101134
6 · The paper itself

Abstract

SEM1(86-107) is a 22-residue peptide corresponding to residues 86-107 in the semenogelin I protein. SEM1(86-107) is an abundant component of freshly liquefied semen and forms amyloid fibrils capable of enhancing HIV infection. To probe the factors affecting fibril formation and gain a better understanding of how differences in pH between semen and vaginal fluid affect fibril stability, this study determined the effect of pH on SEM1(86-107) fibril formation and dissociation. The SEM1(86-107) fibril structure (i.e., residues that comprise the fibrillar core) was also probed using hydrogen-deuterium exchange mass spectrometry (HDXMS) and hydroxyl radical-mediated protein modification. The average percent exposure to hydroxyl radical-mediated modification in the SEM1(86-107) fibrils was determined without requiring tandem mass spectrometry spectral acquisition or complete separation of modified peptides. It was found that the residue exposures calculated from HDXMS and hydroxyl radical-mediated modification were similar. These techniques demonstrated that three regions of SEM1(86-107) comprise the amyloid fibril core and that positively charged residues are exposed, suggesting that electrostatic interactions between SEM1(86-107) and HIV or the cell surface may be responsible for mediating HIV infection enhancement by the SEM1(86-107) fibrils.

Indexed as

HIV-1Amino Acid SequenceAmyloidHIV InfectionsHumansMaleMolecular Sequence DataSemenSeminal Vesicle Secretory ProteinsAmyloidSeminal Vesicle Secretory Proteinsseminal vesicle-specific antigen

Identifiers

PMID24811874
PMCPMC4039337
OpenAlexW2318242840

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.