Relevant bibliographies by topics / Integrin-targeting

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Integrin-targeting'

Author: Grafiati
Published: 3 June 2025
Last updated: 13 July 2025

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Journal articles on the topic "Integrin-targeting"

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Boettner, Benjamin. "Targeting fibrotic integrin." Science-Business eXchange 6, no. 46 (2013): 1308. http://dx.doi.org/10.1038/scibx.2013.1308.

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Estevez, Brian, Bo Shen, and Xiaoping Du. "Targeting Integrin and Integrin Signaling in Treating Thrombosis." Arteriosclerosis, Thrombosis, and Vascular Biology 35, no. 1 (2015): 24–29. http://dx.doi.org/10.1161/atvbaha.114.303411.

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Färber, Stefanie Felicitas, Alexander Wurzer, Florian Reichart та ін. "Therapeutic Radiopharmaceuticals Targeting Integrin αvβ6". ACS Omega 3, № 2 (2018): 2428–36. http://dx.doi.org/10.1021/acsomega.8b00035.

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Egorova, Elena A., and Maxim P. Nikitin. "Delivery of Theranostic Nanoparticles to Various Cancers by Means of Integrin-Binding Peptides." International Journal of Molecular Sciences 23, no. 22 (2022): 13735. http://dx.doi.org/10.3390/ijms232213735.

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Active targeting of tumors is believed to be the key to efficient cancer therapy and accurate, early-stage diagnostics. Active targeting implies minimized off-targeting and associated cytotoxicity towards healthy tissue. One way to acquire active targeting is to employ conjugates of therapeutic agents with ligands known to bind receptors overexpressed onto cancer cells. The integrin receptor family has been studied as a target for cancer treatment for almost fifty years. However, systematic knowledge on their effects on cancer cells, is yet lacking, especially when utilized as an active targeting ligand for particulate formulations. Decoration with various integrin-targeting peptides has been reported to increase nanoparticle accumulation in tumors ≥ 3-fold when compared to passively targeted delivery. In recent years, many newly discovered or rationally designed integrin-binding peptides with excellent specificity towards a single integrin receptor have emerged. Here, we show a comprehensive analysis of previously unreviewed integrin-binding peptides, provide diverse modification routes for nanoparticle conjugation, and showcase the most notable examples of their use for tumor and metastases visualization and eradication to date, as well as possibilities for combined cancer therapies for a synergetic effect. This review aims to highlight the latest advancements in integrin-binding peptide development and is directed to aid transition to the development of novel nanoparticle-based theranostic agents for cancer therapy.
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Ye, Yunpeng, and Xiaoyuan Chen. "Integrin Targeting for Tumor Optical Imaging." Theranostics 1 (2011): 102–26. http://dx.doi.org/10.7150/thno/v01p0102.

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Burkhart, David J., Brian T. Kalet, Michael P. Coleman, Glen C. Post та Tad H. Koch. "Doxorubicin-formaldehyde conjugates targeting αvβ3 integrin". Molecular Cancer Therapeutics 3, № 12 (2004): 1593–604. http://dx.doi.org/10.1158/1535-7163.1593.3.12.

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Abstract We have reported the synthesis and biological evaluation of a prodrug to a doxorubicin active metabolite. Under physiologic conditions, release of the active metabolite, a conjugate of doxorubicin with formaldehyde, occurs with a half-life of 1 hour. To direct this prodrug to tumor, we designed two conjugates of the prodrug, doxsaliform, with the αvβ3-targeting peptides, CDCRGDCFC (RGD-4C) and cyclic-(N-Me-VRGDf) (Cilengitide). We now report the synthesis of these doxsaliform-peptide conjugates and their evaluation using MDA-MB-435 cancer cells. A hydroxylamine ether tether was used to attach 5″-formyldoxsaliform to RGD-4C in its acyclic form via an oxime functional group. The construct acyclic-RGD-4C-doxsaliform showed good binding affinity for αvβ3 in the vitronection cell adhesion assay (IC50 = 10 nmol/L) and good growth inhibition of MDA-MB-435 breast cancer cells (IC50 = 50 nmol/L). In its bicyclic forms, RGD-4C showed less affinity for αvβ3 and significantly less water solubility. Cyclic-(N-Me-VRGDf) was modified by substitution of d-4-aminophenylalanine for d-phenylalanine to provide a novel attachment point for doxsaliform. The conjugate, cyclic-(N-Me-VRGDf-NH)-doxsaliform, maintained a high affinity for αvβ3 (IC50 = 5 nmol/L) in the vitronectin cell adhesion assay relative to the peptide bearing only the tether (0.5 nmol/L). The IC50 for growth inhibition of MDA-MB-435 cells was 90 nmol/L. Flow cytometry and growth inhibition experiments suggest that the complete drug construct does not penetrate through the plasma membrane, but the active metabolite does on release from the targeting group. These drug conjugates could have significantly reduced side effects and are promising candidates for in vivo evaluation in tumor-bearing mice.
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Cai, Weibo, Sanjiv Sam Gambhir та Xiaoyuan Chen. "Multimodality tumor imaging targeting integrin αvβ3". BioTechniques 39, № 6S (2005): S14—S25. http://dx.doi.org/10.2144/000112091.

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E. Hagemeyer, Christoph, and Karlheinz Peter. "Targeting the Platelet Integrin GPIIb/IIIa." Current Pharmaceutical Design 16, no. 37 (2010): 4119–33. http://dx.doi.org/10.2174/138161210794519255.

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Cheng, Tsai-Mu, Wong-Jin Chang, Hsiu-Yi Chu та ін. "Nano-Strategies Targeting the Integrin αvβ3 Network for Cancer Therapy". Cells 10, № 7 (2021): 1684. http://dx.doi.org/10.3390/cells10071684.

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Integrin αvβ3, a cell surface receptor, participates in signaling transduction pathways in cancer cell proliferation and metastasis. Several ligands bind to integrin αvβ3 to regulate proliferation and metastasis in cancer cells. Crosstalk between the integrin and other signal transduction pathways also plays an important role in modulating cancer proliferation. Carcinoembryonic antigen cell adhesion molecule 6 (CEACAM6) activates the downstream integrin FAK to stimulate biological activities including cancer proliferation and metastasis. Blockage of signals related to integrin αvβ3 was shown to be a promising target for cancer therapies. 3,3′,5,5′-tetraiodothyroacetic acid (tetrac) completely binds to the integrin with the thyroid hormone to suppress cancer proliferation. The (E)-stilbene analog, resveratrol, also binds to integrin αvβ3 to inhibit cancer growth. Recently, nanotechnologies have been used in the biomedical field for detection and therapeutic purposes. In the current review, we show and evaluate the potentiation of the nanomaterial carrier RGD peptide, derivatives of PLGA-tetrac (NDAT), and nanoresveratrol targeting integrin αvβ3 in cancer therapies.
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Jiang, Yaqun, Yu Long, Hao Ji та ін. "Development and Evaluation of a Peptide Heterodimeric Tracer Targeting CXCR4 and Integrin αvβ3 for Pancreatic Cancer Imaging". Pharmaceutics 14, № 9 (2022): 1791. http://dx.doi.org/10.3390/pharmaceutics14091791.

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Nowadays, pancreatic cancer is still a formidable disease to diagnose. The CXC chemokine receptor 4 (CXCR4) and integrin αvβ3 play important roles in tumor development, progression, invasion, and metastasis, which are overexpressed in many types of human cancers. In this study, we developed a heterodimeric tracer 68Ga-yG5-RGD targeting both CXCR4 and integrin αvβ3, and evaluated its feasibility and utility in PET imaging of pancreatic cancer. The 68Ga-yG5-RGD could accumulate in CXCR4/integrin αvβ3 positive BxPC3 tumors in a high concentration and was much higher than that of 68Ga-yG5 (p < 0.001) and 68Ga-RGD (p < 0.001). No increased uptake of 68Ga-yG5-RGD was found in MX-1 tumors (CXCR4/integrin αvβ3, negative). In addition, the uptake of 68Ga-yG5-RGD in BxPC3 was significantly blocked by excess amounts of AMD3100 (an FDA-approved CXCR4 antagonist) and/or unlabeled RGD (p < 0.001), confirming its dual-receptor targeting properties. The ex vivo biodistribution and immunohistochemical results were consistent with the in vivo imaging results. The dual-receptor targeting strategy achieved improved tumor-targeting efficiency and prolonged tumor retention in BxPC3 tumors, suggesting 68Ga-yG5-RGD is a promising tracer for the noninvasive detection of tumors that express either CXCR4 or integrin αvβ3 or both, and therefore may have good prospects for clinical translation.
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Dissertations / Theses on the topic "Integrin-targeting"

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Pilkington-Miksa, Michael. "The synthesis of modified integrin-targeting peptides for incorporation into lipid/integrin-targeting peptide/DNA transfection complexes." Thesis, University College London (University of London), 2005. http://discovery.ucl.ac.uk/1445789/.

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Integrin-targeting peptides have been shown to increase transfection efficiency when included in a number of different non-viral vectors. In the case of Lipofectin/DN A complexes (LD), transfection efficiency has been shown to increase on incorporation of an integrin- targeting peptide (Lipid/Integrin-targeting peptide/DNA complexes), as seen by a 100-fold increase in luciferase expression. Efforts to improve the Lipofectin component of Lipid/Integrin-targeting peptide/DNA complexes continue to be made and consequently ways of increasing transfection efficiency through modifications to the integrin-binding peptide are also been investigated. The integrin- targeting peptide component of Lipid/Integrin-targeting peptide/DNA complexes investigated by Hart et al. has effectively three functionalities a 'head' which is complimentary to a specific integrin, a 'tail' which can bind to and condense DNA and a 'spacer' which links the 'head' and 'tail'. Both alternative spacers and DNA-binding motifs have been synthesised and incorporated into integrin-targeting peptides with the intention of investigating the effects of these modifications on the transfection efficiency as well as physical properties of Lipid/Integrin-targeting peptide/DNA complexes. In this thesis are reported the structures of unnatural amino acids synthesised and incorporated into integrin-targeting peptides, as well as some of the transfection results obtained.
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DiCara, Danielle. "Targeting alpha v beta 6 integrin for cancer imaging." Thesis, Queen Mary, University of London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.522319.

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Forgey, Cady. "Prevention of Chronic Inflammation by Targeting Macrophage Integrin aDb2." Digital Commons @ East Tennessee State University, 2020. https://dc.etsu.edu/etd/3849.

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Macrophage integrin aDb2 promotes macrophage retention and accumulation within inflamed tissue, a key event in development of chronic inflammation. Recently, the P5 peptide was identified as a specific inhibitor for integrin aDb2 interaction with 2-(ω-carboxyethyl) pyrole (CEP), a ligand at inflammatory sites. This thesis aims to identify integrin aD I-domain amino acids involved in binding P5 peptide and likewise to CEP. We propose that non-conserved, basic amino acids of the integrin aDb2 I-domain are responsible for binding to P5 peptide and likewise to CEP. Eight amino acids were analyzed by generating six mutant aD I-domains: K180[A], R189[Q], K205[L], HHK223-225[NIT], K233[A], and K246[A]. Mutagenic constructs were created using PCR site-directed mutagenesis, then transformed into E.coli BL21 cells for IPTG-induced protein expression. Of the 6 mutant I-domains analyzed, amino acid K246 was critical in binding to P5 peptide and CEP through ForteBio Protein-Protein Assay, as well as to CEP by cell adhesion assay.
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Waterhouse, Jodie Elizabeth. "Synthesis and application of integrin targeting lipopeptides in gene therapy." Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.405829.

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Emmons, Michael Foster. "Targeting α4 Integrin Containing Complexes in Multiple Myeloma Using Peptidomimetics". Scholar Commons, 2012. http://scholarcommons.usf.edu/etd/4314.

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In our previous work we demonstrated that the integrin antagonist, HYD1, induced necrotic cell death in myeloma cell lines in vitro and in vivo as a single agent. In order to further delineate biomarkers of response to HYD1 we developed an isogenic drug resistant variant named H929-60. We show that the acquisition of resistance towards HYD1 correlates with reduced expression of the cleaved α4 integrin subunit and beta 1 integrin. Moreover, we demonstrate that HYD1 interacts with α4 integrin in myeloma cells. Consistent with reduced VLA-4 expression, the resistant variant showed ablated functional binding to fibronectin, VCAM-1 and the bone marrow stroma cell line, HS-5. The reduction in binding to extracellular matrices of the resistant variant translated to sensitivity to melphalan and bortezomib induced cell death in the bone marrow stroma co-culture model of drug resistance. Moreover, CD138 positive myeloma cells were more sensitive to HYD1 induced cell death compared to the CD138 negative fraction, and potency of HYD1 induced cell death significantly correlated with α4 integrin expression. We were also able to show that reducing α4 or β1 integrin using shRNA strategies was sufficient to cause resistance in myeloma cell lines. In addition we investigated the effects of cyclized variants of HYD1 to improve potency of the agent. One such compound, named HM-27, was determined to be 30 fold more active in H929 cells when compared to HYD1. HM-27 and HYD1 were determined to have similar mechanisms of action as H929-60 cells were shown to be resistant to both compounds when compared to H929 cells. We further characterized HM-27's mechanism of action by investigating what effects HM-27 induced Ca2+ oscillations had on HM-27 induced cell death. The increases in intracellular Ca2+ seen after treatment with HM-27 were determined to occur via release from ER stores and not through influx through plasma membrane channels. Inhibiting Ca2+ release from the ER also potentiated the effects of HM-27 in MM cells. Furthermore, inhibiting Ca2+ release from the ER was also shown to block the onset of autophagy after ER treatment. Treating cells with the lysosomotropic agent, chloroquine, was shown to potentiate the activity of HM-27 in vitro and ex vivo. HM-27 was also shown to have activity in an in vivo model with combination treatment containing bortezomib and HM-27 increasing mouse survival. Collectively our data indicate that VLA-4 expression is a critical determinant of response to HYD1 induced cell death. We also showed that increases in intracellular Ca2+ seen after treatment with HM-27 had a cytoprotective effect in MM cells. Moreover, neutralizing autophagy potentiates HM-27 induced cell death in vitro and ex vivo while combining bortezomib and HM-27 increased survival in vivo. These data continue to provide rationale for further pre-clinical development of HYD1 as a novel anticancer agent.
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Brunton, Fiona. "Targeting the osteoclast alpha v beta 3 integrin by phage display." Thesis, Queen Mary, University of London, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.511761.

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PINA, ARIANNA. "SYNTHESIS OF NEW RGD PEPTIDOMIMETIC-DRUG CONJUGATES TARGETING ΑVΒ3 INTEGRIN." Doctoral thesis, Università degli Studi di Milano, 2019. http://hdl.handle.net/2434/606167.

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Abstract Nowadays, systemic administration of cytotoxic agents is one of the main keystones of modern anticancer chemotherapy. However, many drugs do not selectively localize into solid tumors, as they normally accumulate also in healthy organs (e.g. liver and kidney). As a result, severe side effects are caused by the suboptimal biodistribution profile, in combination with the non-specific mode of action of cytotoxic agents, preventing the drug administration at therapeutic doses. The targeted delivery of anticancer agents into solid tumors is emerging as encouraging approach to overcome the intrinsic drawbacks of cytotoxic drugs. For example, some antibodies with high affinity for accessible tumor markers have been used as vehicles for the targeted drug delivery (Antibody-Drug Conjugates, ADCs). Since they may have limitations due to their high molecular weight, to their possible immunogenicity and to their high production costs, the development of smaller ligands (e.g. vitamins, peptides and peptidomimetics) capable of binding efficiently to tumor-overexpressed receptors, may show some significant therapeutic advantages. Peptides and peptidomimetics with the Arg-Gly-Asp tripeptide (RGD) are known to bind integrin αvβ3, a heterodimeric transmembrane receptor which shows low expression on healthy tissues, while being upregulated in a variety of cancer cells. For these reasons, integrin ligands have been widely explored as homing devices for the selective delivery of anticancer agents. In this PhD thesis, the synthesis and the biological evaluation of new small molecule-drug conjugates (SMDCs) targeting αvβ3 integrin are described. This work started with the preparation of a SMDC for the integrin-targeted delivery of Camptothecin, containing a disulfide linker and a naphtalimide moiety for the real-time monitoring of the cellular uptake (Chapter II). While the design of this complex molecular structure was carried out to reproduce literature data, the biological evaluation of this compound revealed a complex scenario. For this reason, the biological properties of all the three moieties (ligand, drug and linker) have been deeply investigated individually. Firstly, in Chapter III we established the role and the behavior of the ligand, trying to understand its action mechanism. Moreover, modifications of the ligand unit have been carried out to deface the affinity for the receptor and to unambiguously evaluate the capability of the original ligand to selectively target cancer cells that (over)express αvβ3. Later on, linker-related structural features (e.g. stability, linker cleavage experiments, kinetics of drug release, etc.) have been studied and improved (Chapter IV). Finally, the development of other integrin-targeted SMDC products featuring peptide linkers (with their biological evaluation) is reported in Chapter V. In Chapter VII, all the experimental details of synthetic and biological procedures are included, together with spectroscopic data and HPLC profiles of the newly synthesized compounds.
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Harbottle, Richard Paul. "Development of a non-viral gene delivery system based on integrin targeting peptides." Thesis, Imperial College London, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326256.

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CORSO, A. DAL. "TUMOR TARGETING VIA INTEGRIN LIGANDS: SYNTHESIS AND BIOLOGICAL EVALUATION OF RGD PEPTIDOMIMETIC-DRUG CONJUGATES." Doctoral thesis, Università degli Studi di Milano, 2015. http://hdl.handle.net/2434/331100.

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Peptides and peptidomimetics bearing the Arg-Gly-Asp peptide sequence have been demonstrated to bind with high affinity to αvβ3 Integrin, a heterodimeric transmembrane receptor overexpressed in several tumor cells. For these reasons, integrin ligands have been coupled to a variety of anticancer drugs, aiming at the selective delivery of the payload at the tumor site. This PhD work describes the conjugation of the peptidomimetic αvβ3 Integrin ligand cyclo[DKP-RGD] to different anticancer drugs (i.e. paclitaxel, daunorubicin and camptothecin) through peptide and disulfide linkers. The resulting small molecule-drug conjugates (SMDCs) are selective αvβ3 binders and are able to release the drug upon exposure to lysosomal enzymes (e.g. cysteine proteases) or intracellular reducing agents (e.g. glutathione). Cell proliferation assays against isogenic human cancer cells expressing αvβ3 at different levels (αvβ3 +/αvβ3 −) have been performed to evaluate the selective cytotoxic activity of RGD-based SMDCs against integrin-positive cancer cells. Fairly effective integrin targeting was displayed by the cyclo[DKP-RGD]-Val-Ala-PTX conjugate (compound 80), which was found to differentially inhibit proliferation in antigen-positive CCRF CEM αvβ3 versus antigen-negative isogenic CCRF-CEM cells. Next-generation cyclo[DKP-RGD]-Drug conjugates were prepared, aiming at improving the targeting effect shown by the cyclo[DKP-RGD]-Val-Ala-PTX conjugate as well as to deeply analyze the SMDC’s interactions with cancer cells.
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LOPEZ, RIVAS PAULA. "SYNTHESIS OF INTEGRIN-TARGETING PRO-DRUGS FOR THE SELECTIVE RELEASE OF ANTI-TUMOR AGENTS." Doctoral thesis, Università degli Studi di Milano, 2018. http://hdl.handle.net/2434/584099.

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In this PhD work, a variety of new SMDCs were designed and synthesized featuring different types of linkers and cytotoxic payloads. All of them were characterized and conjugated to peptidomimetic ligands bearing the RGD sequence (namely, the cyclo[DKP-RGD] and cyclo[RDGfK] compounds) aimed at targeting αVβ3 integrin receptor, which is overexpressed in many human cancers. Firstly, six new conjugates containing peptide linkers prone to cleavage in intracellular vesicles (such as the lysosomes) were synthesized and evaluated in vitro. The loss of potency generally displayed by these SMDCs in antiproliferative assays prompted us to the design of new conjugates bearing peptide linkers susceptible to proteolysis in the extracellular environment. This strategy has got credits from literature data and it has been proposed as a promising alternative to internalizing conjugates. Based on this, two new conjugates containing aminoacid sequences recognized and cleaved by MMP-2 were synthesized. The conjugates’ binding ability was studied by competitive binding assays on the integrin αVβ3 receptor was studied, and the effective cleavage of the peptide linker in the presence of recombinant human MMP-2 was observed. Finally, two new conjugates that may be activated both in intracellular compartments and in extracellular milieu, by means of the ubiquitous tumor-associated enzyme β-glucuronidase, were synthesized and evaluated by their ability of inhibit biotinylated vitronectin (binding assays). Further evaluation of the efficient drug release from these non-internalizing prodrugs, brought at the diseased site by the RGD affinity for tumor-expressed integrins, will potentially support the clinical investigation of this anticancer devices.
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Books on the topic "Integrin-targeting"

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Patsenker, Eleonora, ed. Integrin Targeting Systems for Tumor Diagnosis and Therapy. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7445-0.

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Integrin Targeting Systems for Tumor Diagnosis and Therapy. Humana, 2018.

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Patsenker, Eleonora. Integrin Targeting Systems for Tumor Diagnosis and Therapy. Springer New York, 2019.

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Book chapters on the topic "Integrin-targeting"

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Kampouri, Eleftheria E., Jonathan Tschopp, and Oriol Manuel. "α4-Integrin (and Other Leukocyte Integrin)-Targeting Agents." In Infectious Complications in Biologic and Targeted Therapies. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-11363-5_14.

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Saraf, Poonam, Xiaoling Li, and Bhaskara Jasti. "Integrin Targeting Using RGD-Based Peptide Amphiphiles." In Methods in Pharmacology and Toxicology. Springer New York, 2015. http://dx.doi.org/10.1007/7653_2015_61.

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Mashreghi, Mohammad, and Mahmoud Reza Jaafari. "Active Targeting for Tumor Microenvironment: Integrin Binding Peptides." In Functional Lipid Nanosystems in Cancer. Jenny Stanford Publishing, 2021. http://dx.doi.org/10.1201/9781003056997-16.

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Brandau, O., and R. Fässler. "Analysis of Integrin Function by Gene Targeting in Mice." In Transgenic Models in Pharmacology. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18934-0_7.

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Majumder, Poulami, and Arabinda Chaudhuri. "Integrin-Mediated Targeting of Liposomally Bound siRNAs to Tumor Vasculatures." In Methods in Pharmacology and Toxicology. Springer New York, 2015. http://dx.doi.org/10.1007/7653_2015_54.

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Neburkova, Jitka, Miroslav Hajek, Ivan Rehor, et al. "Targeting Glioma Cancer Cells with Fluorescent Nanodiamonds via Integrin Receptors." In Methods in Pharmacology and Toxicology. Springer New York, 2017. http://dx.doi.org/10.1007/7653_2017_68.

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Wang, Fei, Gang Wei, and Weiyue Lu. "Preparation and Evaluation of Integrin Receptor-Mediated Targeting Drug Liposomes." In Liposome-Based Drug Delivery Systems. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49231-4_15-1.

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Wang, Fei, Gang Wei, and Weiyue Lu. "Preparation and Evaluation of Integrin Receptor-Mediated Targeting Drug Liposomes." In Biomaterial Engineering. Springer Berlin Heidelberg, 2021. http://dx.doi.org/10.1007/978-3-662-49320-5_15.

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Vehlow, Anne, Katja Storch, Daniela Matzke, and Nils Cordes. "Molecular Targeting of Integrins and Integrin-Associated Signaling Networks in Radiation Oncology." In Molecular Radio-Oncology. Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-49651-0_4.

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Park, Steven I., Renil Manat, Brian Vikstrom, Nail Amro, and Kit S. Lam. "Identification of Peptide Ligands for α4β1 Integrin Receptor as Potential Targeting Agents for Non-Hodgkin’s Lymphoma." In Peptides: The Wave of the Future. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_80.

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Conference papers on the topic "Integrin-targeting"

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Biswas, Sanchita, Xuhua Wang, Alma R. Morales, and Kevin D. Belfield. "Fluorescence Bioimaging with Integrin-targeting Block Copolymer Probes." In Biomedical Optics. OSA, 2010. http://dx.doi.org/10.1364/biomed.2010.bsud82.

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Bloch, Sharon, Kexian Liang, Richard B. Dorshow, Yunpeng Ye, and Samuel I. Achilefu. "Targeting the expression of integrin receptors in tumors." In Biomedical Optics 2004, edited by Alexander P. Savitsky, Lubov Y. Brovko, Darryl J. Bornhop, Ramesh Raghavachari, and Samuel I. Achilefu. SPIE, 2004. http://dx.doi.org/10.1117/12.533160.

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Murray, Elizabeth R., Nicholas F. Brown, Philip Howard та ін. "Abstract 958: Effective targeting of pancreatic ductal adenocarcinoma metastases with an integrin αvβ6-targeting peptide-drug conjugate". У Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-958.

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Vallath, Sabari, Emaunela Gadaletta, Claude Chelala та ін. "Abstract B42: Toward targeting integrin αvβ6 for the therapy of pancreatic cancer." У Abstracts: AACR Special Conference on Pancreatic Cancer: Progress and Challenges; June 18-21, 2012; Lake Tahoe, NV. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.panca2012-b42.

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Moore, Kate M., Gareth J. Thomas, Stephen W. Duffy та ін. "Abstract B046: Therapeutic targeting of integrin αvβ6 in high-risk breast cancer". У Abstracts: AACR Special Conference on Advances in Breast Cancer Research: Genetics, Biology, and Clinical Applications - October 3-6, 2013; San Diego, CA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1557-3125.advbc-b046.

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Li, Zhang, Zhang Chun Li, Yan Ping та ін. "Design, activity determination and99mTc labeling of cyclic RGD dimer for targeting integrin αVβ3". У 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6027894.

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Karmakar, Partha, Kostiantyn Ziabrev, Samuel Achilefu, Dorota Grabowska, Gail Sudlow та Nibedita Sanyal. "Effect of linkers on the αvβ3 integrin targeting efficiency of cyclic RGD-conjugates." У Reporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications X, редактори Samuel Achilefu та Ramesh Raghavachari. SPIE, 2018. http://dx.doi.org/10.1117/12.2301223.

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Chu, Po-Chen, Ming-Chen Yang, Samuel K. Kulp, and Ching-Shih Chen. "Abstract 4455: Targeting a novel kras-integrin-linked kinase regulatory circuitry in pancreatic cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4455.

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Wettersten, Hiromi I., Toshiyuki Minami, Megan M. Kaneda та ін. "Abstract 3966: Targeting integrin αvβ3-expressing cancer stem cells to manipulate tumor-associated macrophages". У Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3966.

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Bourn, Matthew, Safoura Mohajerani, Georgia Mavria та ін. "Targeting Tumour Vasculature using Integrin αvβ3 - Observation of Liposome Accumulation in Microfluidic Vasculature Networks". У Emerging Investigators in Microfluidics Conference. Fundació Scito, 2021. http://dx.doi.org/10.29363/nanoge.eimc.2021.024.

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Reports on the topic "Integrin-targeting"

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Andrews, Philip. Targeting Alpha5 Beta1 Integrin to Prevent Metastatic Breast Cancer Cell Invasion: PhScN Target Site Definition and Plasma Stability. Defense Technical Information Center, 2014. http://dx.doi.org/10.21236/ada612844.

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Livant, Donna L. Targeting Alpha5 Beta1 Integrin to Prevent Metastatic Breast Cancer Cell Invasion: PhScN Target Site Definition and Plasma Stability. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada592840.

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Andrews, Phillip C. Targeting Alpha5 Beta1 Integrin to Prevent Metastatic Breast Cancer Cell Invasion: PhScN Target Site Definition and Plasma Stability. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada594182.

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