Evidence map›Paper›PMID 33879614›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Transferrin receptor targeting by de novo sheet extension.

Danny D Sahtoe, Adrian Coscia, Nur Mustafaoglu, Lauren M Miller, Daniel Olal, Ivan Vulovic, Ta-Yi Yu, Inna Goreshnik, Yu-Ru Lin, Lars Clark and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Enhanced screening via a pure DNA-encoded peptide library enabled by an Fmoc modification.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Article
  8. Review
  9. De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Design of amyloidogenic peptide traps.Nature chemical biology · 2024
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. bioRxiv : the preprint server for biology · 2023
    Article
  20. Towards Novel BiomimeticBioengineering (Basel, Switzerland) · 2023
    Review
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

16 authors at 5 institutions in 1 country.

Danny D SahtoeDepartment of Biochemistry, University of Washington, Seattle, WA 98195.ORCID 0000-0001-9095-0744
Adrian CosciaDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Nur MustafaogluWyss Institute for Biologically Inspired Engineering at Harvard University, Boston, MA 02115.ORCID 0000-0001-8219-9399
Lauren M MillerDepartment of Biochemistry, University of Washington, Seattle, WA 98195.ORCID 0000-0001-5935-4549
Daniel OlalDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Ivan VulovicDepartment of Biochemistry, University of Washington, Seattle, WA 98195.ORCID 0000-0003-4208-6183
Ta-Yi YuInstitute for Protein Design, University of Washington, Seattle, WA 98195.
Inna GoreshnikDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Yu-Ru LinDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Lars ClarkDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Florian BuschDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.ORCID 0000-0002-4324-6065
Lance StewartDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.ORCID 0000-0003-0495-2538
Donald E IngberWyss Institute for Biologically Inspired Engineering at Harvard University, Boston, MA 02115.
Jonathan AbrahamDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115; abraham@crystal.harvard.edu dabaker@uw.edu.ORCID 0000-0002-7937-3920
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA 98195; abraham@crystal.harvard.edu dabaker@uw.edu.ORCID 0000-0001-7896-6217
University of Washington · USHarvard University · USThe Ohio State University · USBoston Children's Hospital · USBroad Institute · US

Funding

THERAPEUTIC EFFECTS OF INTRA-NASAL INSULIN DETEMIRP50AG005136 · NIA · UNIVERSITY OF WASHINGTON · PI GRABOWSKI, THOMAS J. · 1985 to 2019
$57.2M
Medical Scientist Training ProgramT32GM007753 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALENSKY, LOREN DAVID · 1985 to 2021
$50.0M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
Designed Vehicles for Blood Brain Barrier TraversalR01AG063845 · NIA · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2019 to 2023
$2.5M
Antibody therapeutics for human viral hemorrhagic fevers and prevention of late neurological syndromesDP5OD023084 · OD · HARVARD MEDICAL SCHOOL · PI ABRAHAM, JONATHAN · 2016 to 2020
$2.1M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIA NIH HHS P50 AG005136NIA NIH HHS R01 AG063845NIGMS NIH HHS P30 GM124165NIGMS NIH HHS P41 GM128577NIGMS NIH HHS T32 GM007753NIGMS NIH HHS T32 GM008268NIH HHS DP5 OD023084
6 · The paper itself

Abstract

The de novo design of polar protein-protein interactions is challenging because of the thermodynamic cost of stripping water away from the polar groups. Here, we describe a general approach for designing proteins which complement exposed polar backbone groups at the edge of beta sheets with geometrically matched beta strands. We used this approach to computationally design small proteins that bind to an exposed beta sheet on the human transferrin receptor (hTfR), which shuttles interacting proteins across the blood-brain barrier (BBB), opening up avenues for drug delivery into the brain. We describe a design which binds hTfR with a 20 nM

Indexed as

Blood-Brain BarrierBrainDrug Delivery SystemsHumansProtein EngineeringProteinsReceptors, TransferrinTransferrinProteinsReceptors, TransferrinTransferrinblood–brain barriercomputational protein designdrug deliveryneurological diseasetransferrin receptor

Identifiers

PMID33879614
PMCPMC8092486
OpenAlexW3153543354

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.