Evidence map›Paper›PMID 35024976›Full record

ReviewNano convergence2022

Supramolecular assembly of protein building blocks: from folding to function.

Nam Hyeong Kim, Hojae Choi, Zafar Muhammad Shahzad, Heesoo Ki, Jaekyoung Lee, Heeyeop Chae, Yong Ho Kim

Abstract readReview
In one paragraph

Review in Nano convergence, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Assembly-enhanced recognition: A biomimetic pathway to achieve ultrahigh affinities.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. 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

7 authors.

Nam Hyeong Kim *SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University, Suwon, 16419, Republic of Korea.
Hojae Choi *SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University, Suwon, 16419, Republic of Korea.
Zafar Muhammad Shahzad *SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University, Suwon, 16419, Republic of Korea.
Heesoo KiDepartment of Nano Engineering, Sungkyunkwan University, Suwon, 16419, Republic of Korea.
Jaekyoung LeeDepartment of Nano Engineering, Sungkyunkwan University, Suwon, 16419, Republic of Korea.
Heeyeop ChaeSchool of Chemical Engineering, Sungkyunkwan University, Suwon, 16419, Republic of Korea.
Yong Ho KimSKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University, Suwon, 16419, Republic of Korea. yhkim94@skku.edu.ORCID http://orcid.org/0000-0002-9106-3298

Funding

Korea Institute of Science and Technology KIST-2E30641-20-150Nano Convergence Industrial Strategic Technology Development program 200000105National Research Foundation of Korea NRF-2019R1A2C1085712
6 · The paper itself

Abstract

Several phenomena occurring throughout the life of living things start and end with proteins. Various proteins form one complex structure to control detailed reactions. In contrast, one protein forms various structures and implements other biological phenomena depending on the situation. The basic principle that forms these hierarchical structures is protein self-assembly. A single building block is sufficient to create homogeneous structures with complex shapes, such as rings, filaments, or containers. These assemblies are widely used in biology as they enable multivalent binding, ultra-sensitive regulation, and compartmentalization. Moreover, with advances in the computational design of protein folding and protein-protein interfaces, considerable progress has recently been made in the de novo design of protein assemblies. Our review presents a description of the components of supramolecular protein assembly and their application in understanding biological phenomena to therapeutics.

Indexed as

Protein designProtein foldingProtein–protein interactionSupramolecular assembly

Identifiers

PMID35024976
PMCPMC8755899

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.