ArticleScientific reports2014
Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Intracellular Antibodies for Drug Discovery and as Drugs of the Future.Antibodies (Basel, Switzerland) · 2023Review
- Evolution of nanobodies specific for BCL11A.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Competitive SPR using an intracellular anti-LMO2 antibody identifies novel LMO2-interacting compounds.Journal of immunological methods · 2021Article
- A cell-based screening method using an intracellular antibody for discovering small molecules targeting the translocation protein LMO2.Science advances · 2021Article
- Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect.Medical science monitor basic research · 2020Article
- Small molecule inhibits T-cell acute lymphoblastic leukaemia oncogenic interaction through conformational modulation of LMO2.Oncotarget · 2020Article
- Cancer cell killing by target antigen engagement with engineered complementary intracellular antibody single domains fused to pro-caspase3.Scientific reports · 2019Article
- Structure-based development of new RAS-effector inhibitors from a combination of active and inactive RAS-binding compounds.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Intracellular immunization against HIV infection with an intracellular antibody that mimics HIV integrase binding to the cellular LEDGF protein.Scientific reports · 2017Article
- LMO2 at 25 years: a paradigm of chromosomal translocation proteins.Open biology · 2015Review
- Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
LMO2 was discovered via chromosomal translocations in T-cell leukaemia and shown normally to be essential for haematopoiesis. LMO2 is made up of two LIM only domains (thus it is a LIM-only protein) and forms a bridge in a multi-protein complex. We have studied the mechanism of formation of this complex using a single domain antibody fragment that inhibits LMO2 by sequestering it in a non-functional form. The crystal structure of LMO2 with this antibody fragment has been solved revealing a conformational difference in the positioning and angle between the two LIM domains compared with its normal binding. This contortion occurs by bending at a central helical region of LMO2. This is a unique mechanism for inhibiting an intracellular protein function and the structural contusion implies a model in which newly synthesized, intrinsically disordered LMO2 binds to a partner protein nucleating further interactions and suggests approaches for therapeutic targeting of LMO2.
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Registered trials
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.