Evidence map›Paper›PMID 42573686›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

HiBiT-RR and nLuc

Hanfeng Lin, Xiaoli Qi, Jin Wang

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Hanfeng LinThe Verna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX, USA.
Xiaoli QiThe Verna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX, USA.
Jin WangThe Verna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX, USA. wangj@bcm.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeted protein degradation (TPD) has become a powerful modality in drug discovery. Central to developing TPD molecules like PROTACs is the ability to accurately and sensitively measure the degradation of a target protein. The NanoLuciferase (nLuc) and the complementary split-nLuc system are highly sensitive reporter technologies ideal for this purpose. However, the presence of lysine residues on these tags can lead to ubiquitination of the tag itself, creating potential artifacts where the tag, not the target protein, drives degradation. This chapter details protocols for the generation and use of lysine-free variants, HiBiT-RR and nLuc

Indexed as

ProteolysisGenes, ReporterHEK293 CellsHigh-Throughput Screening AssaysHumansLuciferasesLysineProteolysis Targeting ChimeraUbiquitinationLuciferasesLysineProteolysis Targeting ChimeraHiBiTHigh-throughput screeningLysineNanoBiTNanoLuciferase (nLuc)PROTACReporter assayTargeted protein degradation (TPD)Ubiquitination

Identifiers

PMID42573686

What OpenQuestion holds

Textmetadata
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.