Evidence map›Paper›PMID 33229551›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Development of cyclic peptides with potent in vivo osteogenic activity through RaPID-based affinity maturation.

Nasir K Bashiruddin, Mikihito Hayashi, Masanobu Nagano, Yan Wu, Yukiko Matsunaga, Junichi Takagi, Tomoki Nakashima, Hiroaki Suga

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Nasir K BashiruddinDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan.ORCID 0000-0001-9175-0947
Mikihito HayashiDepartment of Cell Signaling, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo 113-8549, Japan.ORCID 0000-0001-6576-1466
Masanobu NaganoDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan.
Yan WuDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan.ORCID 0000-0003-1316-4867
Yukiko MatsunagaLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita-shi, Osaka 565-0871, Japan.
Junichi TakagiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita-shi, Osaka 565-0871, Japan.ORCID 0000-0002-1219-475X
Tomoki NakashimaDepartment of Cell Signaling, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo 113-8549, Japan; naka.csi@tmd.ac.jp hsuga@chem.s.u-tokyo.ac.jp.ORCID 0000-0001-6779-8617
Hiroaki SugaDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan; naka.csi@tmd.ac.jp hsuga@chem.s.u-tokyo.ac.jp.ORCID 0000-0002-5298-9186
The University of Tokyo · JPProtein Research Foundation · JPTokyo Medical and Dental University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Osteoporosis is caused by a disequilibrium between bone resorption and bone formation. Therapeutics for osteoporosis can be divided into antiresorptives that suppress bone resorption and anabolics which increase bone formation. Currently, the only anabolic treatment options are parathyroid hormone mimetics or an anti-sclerostin monoclonal antibody. With the current global increases in demographics at risk for osteoporosis, development of therapeutics that elicit anabolic activity through alternative mechanisms is imperative. Blockade of the PlexinB1 and Semaphorin4D interaction on osteoblasts has been shown to be a promising mechanism to increase bone formation. Here we report the discovery of cyclic peptides by a novel RaPID (Random nonstandard Peptides Integrated Discovery) system-based affinity maturation methodology that generated the peptide PB1m6A9 which binds with high affinity to both human and mouse PlexinB1. The chemically dimerized peptide, PB1

Indexed as

Amino Acid SequenceAnimalsAnimals, NewbornFemurHumansMice, Inbred C57BLOsteogenesisOvariectomyPeptide LibraryPeptides, CyclicProtein MultimerizationX-Ray MicrotomographyPeptide LibraryPeptides, Cycliccyclic peptidesin vitro selectionosteoporosisPlexinB1

Identifiers

PMID33229551
PMCPMC7733813
OpenAlexW3110390608

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.