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Relevant bibliographies by topics / Endocytic pathway

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Academic literature on the topic 'Endocytic pathway'

Author: Grafiati

Published: 4 June 2021

Last updated: 18 September 2022

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Journal articles on the topic "Endocytic pathway"

1

Prosser, Derek C., Theodore G. Drivas, Lymarie Maldonado-Báez, and Beverly Wendland. "Existence of a novel clathrin-independent endocytic pathway in yeast that depends on Rho1 and formin." Journal of Cell Biology 195, no. 4 (2011): 657–71. http://dx.doi.org/10.1083/jcb.201104045.

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Yeast is a powerful model organism for dissecting the temporal stages and choreography of the complex protein machinery during endocytosis. The only known mechanism for endocytosis in yeast is clathrin-mediated endocytosis, even though clathrin-independent endocytic pathways have been described in other eukaryotes. Here, we provide evidence for a clathrin-independent endocytic pathway in yeast. In cells lacking the clathrin-binding adaptor proteins Ent1, Ent2, Yap1801, and Yap1802, we identify a second endocytic pathway that depends on the GTPase Rho1, the downstream formin Bni1, and the Bni1 cofactors Bud6 and Spa2. This second pathway does not require components of the better-studied endocytic pathway, including clathrin and Arp2/3 complex activators. Thus, our results reveal the existence of a second pathway for endocytosis in yeast, which suggests similarities with the RhoA-dependent endocytic pathways of mammalian cells.

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Odorizzi, Greg, and Ian S. Trowbridge. "Structural Requirements for Basolateral Sorting of the Human Transferrin Receptor in the Biosynthetic and Endocytic Pathways of Madin-Darby Canine Kidney Cells." Journal of Cell Biology 137, no. 6 (1997): 1255–64. http://dx.doi.org/10.1083/jcb.137.6.1255.

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In polarized Madin-Darby canine kidney (MDCK) cells, the transferrin receptor (TR) is selectively delivered to the basolateral surface, where it internalizes transferrin via clathrin-coated pits and recycles back to the basolateral border. Mutant tailless receptors are sorted randomly in both the biosynthetic and endocytic pathways, indicating that the basolateral sorting of TR is dependent upon a signal located within the 61–amino acid cytoplasmic domain. To identify the basolateral sorting signal of TR, we have analyzed a series of mutant human TR expressed in MDCK cells. We find that residues 19–41 are sufficient for basolateral sorting from both the biosynthetic and endocytic pathways and that this is the only region of the TR cytoplasmic tail containing basolateral sorting information. The basolateral sorting signal is distinct from the YTRF internalization signal contained within this region and is not tyrosine based. Detailed functional analyses of the mutant TR indicate that residues 29–35 are the most important for basolateral sorting from the biosynthetic pathway. The structural requirements for basolateral sorting of internalized receptors from the endocytic pathway are not identical. The most striking difference is that alteration of G31DNS34 to YTRF impairs basolateral sorting of newly synthesized receptors from the biosynthetic pathway but not internalized receptors from the endocytic pathway. Also, mutations have been identified that selectively impair basolateral sorting of internalized TRs from the endocytic pathway without affecting basolateral sorting of newly synthesized receptors. These results imply that there are subtle differences in the recognition of the TR basolateral sorting signal by separate sorting machinery located within the biosynthetic and endocytic pathways.

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CLAGUE, Michael J. "Molecular aspects of the endocytic pathway." Biochemical Journal 336, no. 2 (1998): 271–82. http://dx.doi.org/10.1042/bj3360271.

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Observation of the flow of material along the endocytic pathway has lead to the description of the basic architecture of the pathway and provided insight into the relationship between compartments. Significant advances have been made in the study of endocytic transport steps at the molecular level, of which studies of cargo selection, vesicle budding and membrane fusion events comprise the major part. Progress in this area has been driven by two approaches, yeast genetics and in vitro or cell-free assays, which reconstitute particular transport steps and allow biochemical manipulation. The complex protein machineries that control vesicle budding and fusion are significantly conserved between the secretory and endocytic pathways such that proteins that regulate particular steps are often part of a larger family of proteins which exercise a conserved function at other locations within the cell. Well characterized examples include vesicle coat proteins, rabs (small GTPases) and soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (SNAP) receptors (SNAREs). Intracompartmental pH, lipid composition and cytoskeletal organization have also been identified as important determinants of the orderly flow of material within the endocytic pathway.

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Clague, Michael J., Sylvie Urbé, and Jane de Lartigue. "Phosphoinositides and the endocytic pathway." Experimental Cell Research 315, no. 9 (2009): 1627–31. http://dx.doi.org/10.1016/j.yexcr.2008.10.005.

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Toret, C. P., and D. G. Drubin. "The budding yeast endocytic pathway." Journal of Cell Science 119, no. 22 (2006): 4585–87. http://dx.doi.org/10.1242/jcs.03251.

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Toret, C. P., and D. G. Drubin. "The budding yeast endocytic pathway." Journal of Cell Science 120, no. 8 (2007): 1501. http://dx.doi.org/10.1242/jcs.03446.

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McPherson, Peter S., Brian K. Kay, and Natasha K. Hussain. "Signaling on the Endocytic Pathway." Traffic 2, no. 6 (2001): 375–84. http://dx.doi.org/10.1034/j.1600-0854.2001.002006375.x.

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Bauer, Andrea, Narmadha Subramanian, Clarissa Villinger, Giada Frascaroli, Thomas Mertens, and Paul Walther. "Megapinocytosis: a novel endocytic pathway." Histochemistry and Cell Biology 145, no. 6 (2016): 617–27. http://dx.doi.org/10.1007/s00418-015-1395-2.

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von Zastrow, Mark, and Alexander Sorkin. "Signaling on the endocytic pathway." Current Opinion in Cell Biology 19, no. 4 (2007): 436–45. http://dx.doi.org/10.1016/j.ceb.2007.04.021.

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Burgoyne, Robert D., and Michael J. Clague. "Annexins in the endocytic pathway." Trends in Biochemical Sciences 19, no. 6 (1994): 231–32. http://dx.doi.org/10.1016/0968-0004(94)90143-0.

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Dissertations / Theses on the topic "Endocytic pathway"

1

Kozik, Patrycja. "Sorting signals and machinery in the endocytic pathway." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609631.

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Stringer, Daniel Kenneth. "The role of ubiquitination within the endocytic pathway." Diss., University of Iowa, 2010. https://ir.uiowa.edu/etd/2775.

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Ubiquitination is a post-translational modification tht mediates sorting of integral membrane proteins to lysosomes for their degradation. ESCRTs (Endosomal Sorting Complex Required For Transport) bind and sequester ubiquitinated membrane proteins and direct them into multivesicular bodies (MVBs). ESCRTs themselves become covalently ubiquitinated, simply by virtue of non-covalently binding Ub. However, it is unclear whether this regulates a critical aspect of ESCRT function. In yeast, many MVB cargo proteins are ubiquitinated by the HECT-type Ub-ligase Rsp5, sometimes via the action of Rsp5 adaptor proteins. While many Rsp5 targets are modified by polyubiquitination, it remains unclear whether polyubiquitination is a necessary signal for their incorporation into MVBs. Despite years of research, these and related questions have been difficult to resolve because it is technically quite challenging to control the level of a given protein's ubiquitination. The aim of this research was to develop a novel technique, which can render proteins resistant to ubiquitination. The technique involved the fusion of the Ub-peptidase to a protein of interest via a flexible linker, essentially creating a "DUb module". The intent of this module would be to cleave any Ub form the target protein, essentially immunizing it from the effects of ubiquitination. This novel method was used in combination with several conventional methods to examine the role of ubiquitination within the endocytic pathway and in particular focus on the questions of what type of ubiquitin signal was sufficient for sorting into MVB vesicles and whether ubiquitination of ESCRTs was required for their sorting activity. We found that a single Ub was sufficient for membrane protein entry into MVBs in the absence of ESCRT ubiquitination.

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Deinhardt, Katrin. "The endocytic pathway of tetanus neurotoxin in motor neurons." Thesis, University College London (University of London), 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.428573.

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Schnatwinkel, Carsten. "Characterisation of Novel Rab5 Effector Proteins in the Endocytic Pathway." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2004. http://nbn-resolving.de/urn:nbn:de:swb:14-1106824900192-45576.

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Endocytosis, a process of plasma membrane invaginations, is a fundamental cellular mechanism, ensuring uptake of nutrients, enhanced communication between cells, protective functions against invasive pathogens and remodelling of the plasma membrane composition. In turn, endocytic mechanisms are exploited by pathogens to enter their host cells. Endocytosis comprises multiple forms of which our molecular understanding has mostly advanced with respect to clathrin-mediated endocytosis and phagocytosis. Studies on the small GTPase Rab5 have provided important insights into the molecular mechanism of endocytosis and transport in the early stages of the endocytic pathways. Rab5 is a key regulator of clathrin-mediated endocytosis, but in addition, localises to several distinct endocytic carriers including phagosomes and pinocytic vesicles. On early endosomes, Rab5 coordinates within a spatially restricted domain enriched in phosphatidylinositol-3 phosphate PI(3)P a complex network of effectors, including PI3-Kinase (PI3-K), the FYVE-finger proteins EEA1 and Rabenosyn-5 that functionally cooperate in membrane transport. Moreover, Rab5 regulates endocytosis from the apical and basolateral plasma membrane in polarised epithelial cells. During my PhD thesis, I investigated the molecular mechanisms of endocytosis both in polarised and non-polarised cells. I obtained new insights into the molecular mechanisms of endocytosis and their coordination through the functional characterization of a novel Rab5 effector, termed Rabankyrin-5. I could demonstrated that Rabankyrin-5 is a novel PI(3)P-binding Rab5 effector that localises to early endosomes and stimulates their fusion activity in vitro. The latter activity depends on the oligomerisation of Rabankyrin-5 on the endosomal membrane via the N-terminal BTB/POZ domain. In addition to early endosomes, however, Rabankyrin-5 localises to large vacuolar structures that correspond to macropinosomes in epithelial cells and fibroblasts. Overexpression of Rabankyrin-5 increases the number of macropinosomes and stimulates fluid phase uptake whereas its downregulation through RNA interference inhibits these processes. In polarised epithelial cells, the function of Rabankyrin-5 is primarily restricted to the apical membrane. It localises to large pinocytic structures underneath the apical surface of kidney proximal tubule cells and its overexpression in polarised MDCK cells specifically stimulates apical but not basolateral, non-clathrin mediated pinocytosis. In demonstrating a regulatory role in endosome fusion and (macro)-pinocytosis, my studies suggest that Rab5 regulates and coordinates different endocytic mechanisms through its effector Rabankyrin-5. Furthermore, the active role in apical pinocytosis in epithelial cells suggests an important function of Rabankyrin-5 in the physiology of polarised cells. The results obtained in this thesis are central not only for our understanding of the basic principles underlying the regulation of multiple endocytic mechanisms. They are also relevant for the biomedical field, since actin-dependent (macro)-pinocytosis is an important mechanism for the physiology of cells and organisms and is upregulated under certain pathological conditions (e.g. cancer).

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Renzis, Stefano de. "Sequential action of Rab proteins along the endocytic-recycling pathway." Thesis, Open University, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.395258.

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Granger, Elizabeth. "The interplay between dynein, accessory proteins and the endocytic pathway." Thesis, University of Manchester, 2014. https://www.research.manchester.ac.uk/portal/en/theses/the-interplay-between-dynein-accessory-proteins-and-the-endocytic-pathway(c456befe-2114-41a1-90cc-e5123624a2d3).html.

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Cytoplasmic dynein 1 (dynein) is a multi-subunit complex that transports cargo along microtubules towards their minus ends. These microtubule minus ends are normally located toward the centre of the cell. Dynein is involved in transport of endocytic and autophagic membranes and is tightly regulated by interactions between dynein subunits and by dynein-accessory proteins. Dynein accessory proteins that are involved in a wide range of dynein-driven transport events include dynactin, Lis1 and the paralogues Nde1 and Ndel1. Lis1 and Nde1/Ndel1 interact with each other and are involved in the recruitment of dynein to cargo and in regulating dynein activity. Although much is known about the specific interactions of dynein and accessory proteins, the interplay between dynein and its network of regulators in living cells is not well defined. This project used RNAi to investigate how the dynein subunits light intermediate chain (LIC) and intermediate chain (IC) as well as Lis1 and Nde1/Ndel1 influence the endocytic pathway, autophagy and cargo recruitment. Biochemical analysis of bulk membrane preparations showed that IC is important for dynein and dynactin association with intracellular membranes. In addition, dynein and dynactin recruitment to Rab interacting lysosomal protein (RILP)-positive membranes was shown to require LIC and there was redundancy between LIC1 and LIC2 in this role. Lis1 was also needed for dynactin-dynein recruitment to these membranes, in a context that was Nde1/Ndel1-independent. Loss of LIC, IC, Lis1 and Nde1 had differing effects on endocytic compartment size and distribution, but they all led to mislocalisation of early endosomes and lysosomes and caused lysosomes to become enlarged. Loss of LIC led to a specific phenotype whereby cells formed lamellipodia-like regions in which early endosomes and lysosomes accumulated. Loss of Lis1 prevented traffic from the early endosome to late endosomes and caused a striking enlargement of late endosomes and lysosomes. These enlarged lysosomes were LC3-positive, indicating that they were autophagic. In addition, loss of IC and LIC also led to an increase in LC3 puncta, but the LC3 did not colocalise specifically with lysosomes. In summary, the results from this project show that i) dynactin recruitment to intracellular membranes, including RILP-postivie membranes, requires dynein, ii) Lis1 and LIC1 or LIC2 are necessary but not sufficient, individually, to recruit dynein and dynactin to RILP-positive membranes iii) LIC, IC, Lis1 and Nde1/Ndel1 influence endocytic progression in specific ways, which may in turn affect autophagic flux.

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Valiathan, Rajeshwari Rajan. "Functional interactions of HIV-1 GAg with the cellular endocytic pathway /." Access full-text from WCMC, 2007. http://proquest.umi.com/pqdweb?did=1481666381&sid=16&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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Piper, Siân Catherine. "The endocytic pathway for downregulation of virally-ubiquitinated MHC class I." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612736.

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Bowers, Katherine Elisabeth. "Sorting of CD4 and the SIV envelope glycoprotein in the endocytic pathway." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.286733.

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Carnell, Michael John. "Identifying a role for WASH in the endocytic pathway of Dictyostelium discoideum." Thesis, University of Birmingham, 2011. http://etheses.bham.ac.uk//id/eprint/1550/.

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Members of the WASP protein family are direct activators of the arp2/3 complex, thereby regulating the nucleation of branched actin assemblies within the cell. Each sub-class possesses a unique N-terminal domain architecture allowing a division of labour between its members, each coupling different signal transduction pathways to the nucleation of specific actin structures. WASH (WASP and SCAR homologue) is a newly identified member of the WASP protein family. Due to its disruption in \(Drosophila\) proving lethal (Linardopopoulou et al., 2007) little is know as to the functional role of WASH at the cellular level. Other than it is important in the development of multicellular organisms. Here we successfully disrupt WASH in the single celled amoebae \(Dictyostelium\) \(discoideum\) and discover a role for WASH in the endocytic pathway. WASH was shown to be essential for the trafficking of indigestible material through the endocytic pathway, with its disruption causing a complete bock in cellular defecation. This was shown to be due to a defect in lysosomal maturation into neutral post-lysosomes. Using fluorescently tagged fusion proteins we show that WASH recruitment coincides with removal of the Vacuolar H+ ATPase from lysosomal membranes, and suggests a possible role for WASH and actin in regulating the luminal pH of intracellular compartments.

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Books on the topic "Endocytic pathway"

1

A, Lauffenburger Douglas, ed. Receptor/ligand sorting along the endocytic pathway. Springer-Verlag, 1989.

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Linderman, Jennifer J., and Douglas A. Lauffenburger. Receptor/Ligand Sorting Along the Endocytic Pathway. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-48892-4.

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Bassil, Nicholas. Molecular characterisation of the endocytic pathway using the fission yeast Schizosaccaromyces pombe. University of Birmingham, 1991.

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Vaux, D. J. The Endocytic Pathway & How It Fails. Landes Bioscience, 1996.

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Book chapters on the topic "Endocytic pathway"

1

Conibear, Elizabeth, and Yuen Yi C. Tam. "The Endocytic Pathway." In Trafficking Inside Cells. Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-93877-6_4.

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Hopkins, Colin R., and Karen M. Miller. "New Insights into the Endocytic Pathway." In Endocytosis. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-84295-5_8.

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Griffiths, Gareth. "The Compartments of the Endocytic Pathway." In Endocytosis. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-84295-5_9.

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Barbieri, M. Alejandro, Maria Isabel Colombo, Guangpu Li, Luis Segundo Mayorga, and Philip Stahl. "GTPases: Key regulatory components of the endocytic pathway." In Trafficking of Intracellular Membranes:. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79547-3_14.

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Pauza, C. David. "The Endocytic Pathway for Human Immunodeficiency Virus Infection." In Mechanisms and Specificity of HIV Entry into Host Cells. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5976-0_8.

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Felberbaum-Corti, Michela, Raluca Flukiger-Gagescu, and Jean Gruenberg. "Membrane Traffic in the Endocytic Pathway of Eukaryotic Cells." In Cellular Microbiology. ASM Press, 2014. http://dx.doi.org/10.1128/9781555817633.ch9.

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Davey, John, and Graham Warren. "Characterisation of a fusion event from the endocytic pathway." In Molecular Biology of the Arterial Wall. Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-83118-8_17.

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Chu, Victor C., Lisa J. McElroy, A. Damon Ferguson, Beverley E. Bauman, and Gary R. Whittaker. "Avian Infectious Bronchitis Virus Enters Cells Via the Endocytic Pathway." In Advances in Experimental Medicine and Biology. Springer US, 2006. http://dx.doi.org/10.1007/978-0-387-33012-9_54.

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Burkhardt, Janis K., Ariel Blocker, Andrea Jahraus, and Gareth Griffiths. "Microtubule Dependent Transport and Fusion of Phagosomes with the Endocytic Pathway." In Trafficking of Intracellular Membranes:. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79547-3_13.

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Blau, Dianna M., and Kathryn V. Holmes. "Human Coronavirus HCoV-229E Enters Susceptible Cells via the Endocytic Pathway." In Advances in Experimental Medicine and Biology. Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1325-4_31.

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Conference papers on the topic "Endocytic pathway"

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Kessel, David. "Effects of PDT on the endocytic pathway." In BiOS, edited by David H. Kessel. SPIE, 2010. http://dx.doi.org/10.1117/12.840530.

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Elkenawi, Asmaa E., and John K. Cowell. "Abstract 1029: Involvement of endocytic pathway in vorinostat-induced EGFR degradation." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1029.

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Wang, S., RE Pagano, and RD Hubmayr. "Pathway Selective Endocytic Trafficking in Type I Alveolar Epithelial Cells during Hypertonic Stress." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4991.

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Delehanty, James B., Christopher M. Spillmann, Jawad Naciri, W. Russ Algar, Banahalli R. Ratna, and Igor L. Medintz. "Fluorescent nanocolloids for differential labeling of the endocytic pathway and drug delivery applications." In SPIE BiOS, edited by Wolfgang J. Parak, Marek Osinski, and Kenji Yamamoto. SPIE, 2013. http://dx.doi.org/10.1117/12.2007749.

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Morad, Golnaz, Christopher V. Carman, and Marsha A. Moses. "Abstract 1989: Breast cancer-derived exosomes modulate the endocytic pathway in brain endothelial cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1989.

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Morad, Golnaz, Christopher V. Carman, and Marsha A. Moses. "Abstract 1989: Breast cancer-derived exosomes modulate the endocytic pathway in brain endothelial cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1989.

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Joensuu, Merja. "Super-resolving botulinum neurotoxin’s endocytic pathway dynamics: from plasma membrane binding to internalization in synaptic vesicles and retrograde transport." In European Microscopy Congress 2020. Royal Microscopical Society, 2021. http://dx.doi.org/10.22443/rms.emc2020.536.

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Pang, Hongbo, Gary B. Braun, Tomas Friman, et al. "Abstract NG03: A novel endocytic and intercellular transport pathway for drug delivery across blood vessels and into nutrient-deprived tumor cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-ng03.

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Yum, Kyungsuk, Sungsoo Na, Yang Xiang, Ning Wang, and Min-Feng Yu. "Nanomechanochemical Delivery of Nanoparticles for Nanomechanics Inside Living Cells." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13039.

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Studying biological processes and mechanics in living cells is challenging but highly rewarding. Recent advances in experimental techniques have provided numerous ways to investigate cellular processes and mechanics of living cells. However, most of existing techniques for biomechanics are limited to experiments outside or on the membrane of cells, due to the difficulties in physically accessing the interior of living cells. On the other hand, nanomaterials, such as fluorescent quantum dots (QDs) and magnetic nanoparticles, have shown great promise to overcome such limitations due to their small sizes and excellent functionalities, including bright and stable fluorescence and remote manipulability. However, except a few systems, the use of nanoparticles has been limited to the study of biological studies on cell membranes or related to endocytosis, because of the difficulty of delivering dispersed and single nanoparticles into living cells. Various strategies have been explored, but delivered nanoparticles are often trapped in the endocytic pathway or form aggregates in the cytoplasm, limiting their further use. Here we show a nanoscale direct delivery method, named nanomechanochemical delivery, where we manipulate a nanotube-based nanoneedle, carrying “cargo” (QDs in this study), to mechanically penetrate the cell membrane, access specific areas inside cells, and release the cargo [1]. We selectively delivered well-dispersed QDs into either the cytoplasm or the nucleus of living cells. We quantified the dynamics of the delivered QDs by single-molecule tracking and demonstrated the applicability of the QDs as a nanoscale probe for studying nanomechanics inside living cells (by using the biomicrorhology method), revealing the biomechanical heterogeneity of the cellular environment. This method may allow new strategies for studying biological processes and mechanics in living cells with spatial and temporal precision, potentially at the single-molecule level.

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Qian, Yanrong, Xuan Wang, Yunsheng Li, Yanyang Cao, and Xiaozhuo Chen. "Abstract 33: NSCLC cells internalize ATPin vitroandin vivousing multiple endocytotic pathways." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-33.

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