ArticleProtein science : a publication of the Protein Society1995
Refined solution structure of human profilin I.
Article in Protein science : a publication of the Protein Society, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed, 42 citations in OpenAlex.
- Profilin and Its Isoforms: Unravelling the Functional Diversity Across Life Forms.Current protein & peptide science · 2026Review
- Molecular mechanism analysis of nontuberculous mycobacteria infection in patients with cystic fibrosis.Future microbiology · 2024Article
- Upregulation of Profilin 2 on HDAC6 overexpression in mouse GC-1 cells and its putative role in germ cell migration in the testis.Cell and tissue research · 2023Article
- Article
- Detection of structural and conformational changes in ALS-causing mutant profilin-1 with hydrogen/deuterium exchange mass spectrometry and bioinformatics techniques.Metabolic brain disease · 2022Article
- Abrogation of prenucleation, transient oligomerization of the Huntingtin exon 1 protein by human profilin I.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Changes in biophysical characteristics of PFN1 due to mutation causing amyotrophic lateral sclerosis.Metabolic brain disease · 2018Article
- Article
- A Drosophila model of ALS reveals a partial loss of function of causative human PFN1 mutants.Human molecular genetics · 2017Article
- Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis.Cellular and molecular life sciences : CMLS · 2017Article
- Profilin1 biology and its mutation, actin(g) in disease.Cellular and molecular life sciences : CMLS · 2017Review
- Review
- The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis.Scientific reports · 2015Article
- The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin.Biophysical journal · 2009Article
- An ectromelia virus profilin homolog interacts with cellular tropomyosin and viral A-type inclusion protein.Virology journal · 2007Article
- PAS domains: internal sensors of oxygen, redox potential, and light.Microbiology and molecular biology reviews : MMBR · 1999Review
- The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences.The EMBO journal · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Profilin is a ubiquitous eukaryotic protein that binds to both cytosolic actin and the phospholipid phosphatidylinositol-4,5-bisphosphate. These dual competitive binding capabilities of profilin suggest that profilin serves as a link between the phosphatidyl inositol cycle and actin polymerization, and thus profilin may be an essential component in the signaling pathway leading to cytoskeletal rearrangement. The refined three-dimensional solution structure of human profilin I has been determined using multidimensional heteronuclear NMR spectroscopy. Twenty structures were selected to represent the solution conformational ensemble. This ensemble of structures has root-mean-square distance deviations from the mean structure of 0.58 A for the backbone atoms and 0.98 A for all non-hydrogen atoms. Comparison of the solution structure of human profilin to the crystal structure of bovine profilin reveals that, although profilin adopts essentially identical conformations in both states, the solution structure is more compact than the crystal structure. Interestingly, the regions that show the most structural diversity are located at or near the actin-binding site of profilin. We suggest that structural differences are reflective of dynamical properties of profilin that facilitate favorable interactions with actin. The global folding pattern of human profilin also closely resembles that of Acanthamoeba profilin I, reflective of the 22% sequence identity and approximately 45% sequence similarity between these two proteins.
Indexed as
Identifiers
What OpenQuestion holds
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.