ArticleMolecular biology of the cell1997
Molecular dissection of a LIM domain.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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.
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Who cites it
31 citing papers in PubMed.
- Genome Wide Identification and Characterization of LIM Domain Associated Gene Superfamily in Common Bean (International journal of genomics · 2025Article
- Exploring the Enigma: The Role of the Epithelial Protein Lost in Neoplasm in Normal Physiology and Cancer Pathogenesis.International journal of molecular sciences · 2024Review
- Where all the Roads Meet? A Crossover Perspective on Host Factors Regulating SARS-CoV-2 infection.Journal of molecular biology · 2022Review
- Cyclic GMP-Dependent Regulation of Vascular Tone and Blood Pressure Involves Cysteine-Rich LIM-Only Protein 4 (CRP4).International journal of molecular sciences · 2021Article
- Review
- When signalling goes wrong: pathogenic variants in structural and signalling proteins causing cardiomyopathies.Journal of muscle research and cell motility · 2017Review
- Review
- LMO2 at 25 years: a paradigm of chromosomal translocation proteins.Open biology · 2015Review
- Genome Wide Identification of LIM Genes in Cicer arietinum and Response of Ca-2LIMs in Development, Hormone and Pathogenic Stress.PloS one · 2015Article
- Muscle lim protein isoform negatively regulates striated muscle actin dynamics and differentiation.The FEBS journal · 2014Article
- Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein.BMC evolutionary biology · 2012Article
- Article
- The cytoskeletal regulator zyxin is required for viability in Drosophila melanogaster.Anatomical record (Hoboken, N.J. : 2007) · 2010Article
- The RHO1-specific GTPase-activating protein LRG1 regulates polar tip growth in parallel to Ndr kinase signaling in Neurospora.Molecular biology of the cell · 2008Article
- An actin-binding protein, LlLIM1, mediates calcium and hydrogen regulation of actin dynamics in pollen tubes.Plant physiology · 2008Article
- Coordinate suppression of Sdpr and Fhl1 expression in tumors of the breast, kidney, and prostate.Cancer science · 2008Article
- Novel LMX1B mutation in familial nail-patella syndrome with variable expression of open angle glaucoma.Molecular vision · 2007Article
- Cross-species translocation of mRNA from host plants into the parasitic plant dodder.Plant physiology · 2007Article
- The C. elegans dense body: anchoring and signaling structure of the muscle.Journal of muscle research and cell motility · 2007Review
- Tobacco WLIM1 is a novel F-actin binding protein involved in actin cytoskeleton remodeling.The Plant cell · 2006Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
LIM domains are novel sequence elements that are found in more than 60 gene products, many of which function as key regulators of developmental pathways. The LIM domain, characterized by the cysteine-rich consensus CX2CX16-23HX2CX2CX2CX16-21 CX2-3(C/H/ D), is a specific mental-binding structure that consists of two distinct zinc-binding subdomains. We and others have recently demonstrated that the LIM domain mediates protein-protein interactions. However, the sequences that define the protein-binding specificity of the LIM domain had not yet been identified. Because structural studies have revealed that the C-terminal zinc-binding module of a LIM domain displays a tertiary fold compatible with nucleic acid binding, it was of interest to determine whether the specific protein-binding activity of a LIM domain could be ascribed to one of its two zinc-binding subdomains. To address this question, we have analyzed the protein-binding capacity of a model LIM peptide, called zLIM1, that is derived from the cytoskeletal protein zyxin. These studies demonstrate that the protein-binding function of zLIM1 can be mapped to sequences contained within its N-terminal zinc-binding module. The C-terminal zinc-binding module of zLIM1 may thus remain accessible to additional interactive partners. Our results raise the possibility that the two structural subdomains of a LIM domain are capable of performing distinct biochemical functions.
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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.