ArticleInternational journal of peptides2012
Proline rich motifs as drug targets in immune mediated disorders.
Article in International journal of peptides, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Enhancing prediction of short linear protein motifs with Wregex 3.0.Computational and structural biotechnology journal · 2024Article
- Effects of a β-Glucan-Rich Blend of Medicinal Mushrooms and Botanicals on Innate Immune Cell Activation and Function Are Enhanced by a Very Low Dose of Bovine Colostrum Peptides.Molecules (Basel, Switzerland) · 2024Article
- AP-2δ Is the Most Relevant Target of AP-2 Family-Focused Cancer Therapy and Affects Genome Organization.Cells · 2022Article
- Impact of a conserved N-terminal proline-rich region of the α-subunit of CAAX-prenyltransferases on their enzyme properties.Cell communication and signaling : CCS · 2022Article
- Identification of an LPS-Induced Chemo-Attractive Peptide fromMarine drugs · 2020Article
- Membrane-associated mucins of the ocular surface: New genes, new protein functions and new biological roles in human and mouse.Progress in retinal and eye research · 2020Review
- Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs.Frontiers in cellular and infection microbiology · 2020Article
- Mechanisms of NF-κB p65 and strategies for therapeutic manipulation.Journal of inflammation research · 2018Review
- Nuclear factor-kappa B: Glucocorticoid-induced leucine zipper interface analogs suppress pathology in an Alzheimer's disease model.Alzheimer's & dementia (New York, N. Y.) · 2018Article
- Novel Nuclear Factor-KappaB Targeting Peptide Suppresses β-Amyloid Induced Inflammatory and Apoptotic Responses in Neuronal Cells.PloS one · 2016Article
- Functional characterization of a competitive peptide antagonist of p65 in human macrophage-like cells suggests therapeutic potential for chronic inflammation.Drug design, development and therapy · 2014Article
- Polyproline and triple helix motifs in host-pathogen recognition.Current protein & peptide science · 2012Review
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The current version of the human immunome network consists of nearly 1400 interactions involving approximately 600 proteins. Intermolecular interactions mediated by proline-rich motifs (PRMs) are observed in many facets of the immune response. The proline-rich regions are known to preferentially adopt a polyproline type II helical conformation, an extended structure that facilitates transient intermolecular interactions such as signal transduction, antigen recognition, cell-cell communication and cytoskeletal organization. The propensity of both the side chain and the backbone carbonyls of the polyproline type II helix to participate in the interface interaction makes it an excellent recognition motif. An advantage of such distinct chemical features is that the interactions can be discriminatory even in the absence of high affinities. Indeed, the immune response is mediated by well-orchestrated low-affinity short-duration intermolecular interactions. The proline-rich regions are predominantly localized in the solvent-exposed regions such as the loops, intrinsically disordered regions, or between domains that constitute the intermolecular interface. Peptide mimics of the PRM have been suggested as potential antagonists of intermolecular interactions. In this paper, we discuss novel PRM-mediated interactions in the human immunome that potentially serve as attractive targets for immunomodulation and drug development for inflammatory and autoimmune pathologies.
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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.