Evidence map›Paper›PMID 33233627›Full record

ReviewInternational journal of molecular sciences2020

The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins.

Sailen Barik

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
6.0field-weighted citation impact, top 2% 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

112 citing papers in PubMed, 224 citations in OpenAlex.

  1. Article
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  6. Review
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  12. Microorganisms · 2026
    Article
  13. Article
  14. TseCurrent research in microbial sciences · 2026
    Article
  15. Article
  16. Article
  17. A Generalized AI View of Tricopeptide Repeats: What's in a Name.International journal of molecular sciences · 2025
    Review
  18. Article
  19. Article
  20. Article

52 more citing papers are in PubMed but not listed here.

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

1 author.

Sailen Barik3780 Pelham Drive, Mobile, AL 36619, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tryptophan (Trp) holds a unique place in biology for a multitude of reasons. It is the largest of all twenty amino acids in the translational toolbox. Its side chain is indole, which is aromatic with a binuclear ring structure, whereas those of Phe, Tyr, and His are single-ring aromatics. In part due to these elaborate structural features, the biosynthetic pathway of Trp is the most complex and the most energy-consuming among all amino acids. Essential in the animal diet, Trp is also the least abundant amino acid in the cell, and one of the rarest in the proteome. In most eukaryotes, Trp is the only amino acid besides Met, which is coded for by a single codon, namely UGG. Due to the large and hydrophobic π-electron surface area, its aromatic side chain interacts with multiple other side chains in the protein, befitting its strategic locations in the protein structure. Finally, several Trp derivatives, namely tryptophylquinone, oxitriptan, serotonin, melatonin, and tryptophol, have specialized functions. Overall, Trp is a scarce and precious amino acid in the cell, such that nature uses it parsimoniously, for multiple but selective functions. Here, the various aspects of the uniqueness of Trp are presented in molecular terms.

Indexed as

AlcoholsAnimalsCodonDipeptidesHumansHydrophobic and Hydrophilic InteractionsIndolequinonesIndolesKynurenineProtein BiosynthesisProtein Interaction Domains and MotifsProteinsSerotoninStructure-Activity RelationshipThermodynamicsTryptophanAlcoholsCodoncysteine tryptophylquinoneDipeptidesIndolequinonesIndolesKynurenineProteinsSerotoninTryptophantryptophan tryptophylquinonetryptopholcodonimmunityindolekynurenineserotonintryptophanvirus

Identifiers

PMID33233627
PMCPMC7699789
OpenAlexW3105065262

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.