Relevant bibliographies by topics / Carrier and Transport Proteins

Academic literature on the topic 'Carrier and Transport Proteins'

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Published: 6 September 2023

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Journal articles on the topic "Carrier and Transport Proteins"

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Wohlrab, Hartmut. "Mitochondrial Transport (Carrier) Proteins. Homodimers and Heterodimers." Biophysical Journal 96, no. 3 (February 2009): 272a—273a. http://dx.doi.org/10.1016/j.bpj.2008.12.1349.

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James Freeman, Hugh. "Trafficking of Cobalamin Transport Carrier Proteins in Celiac Disease." International Journal of Celiac Disease 10, no. 1 (September 5, 2022): 5–7. http://dx.doi.org/10.12691/ijcd-10-1-2.

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Bai, Xiaoyun, Trevor F. Moraes, and Reinhart A. F. Reithmeier. "Structural biology of solute carrier (SLC) membrane transport proteins." Molecular Membrane Biology 34, no. 1-2 (February 17, 2017): 1–32. http://dx.doi.org/10.1080/09687688.2018.1448123.

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Macara, Ian G. "Transport into and out of the Nucleus." Microbiology and Molecular Biology Reviews 65, no. 4 (December 1, 2001): 570–94. http://dx.doi.org/10.1128/mmbr.65.4.570-594.2001.

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SUMMARY A defining characteristic of eukaryotic cells is the possession of a nuclear envelope. Transport of macromolecules between the nuclear and cytoplasmic compartments occurs through nuclear pore complexes that span the double membrane of this envelope. The molecular basis for transport has been revealed only within the last few years. The transport mechanism lacks motors and pumps and instead operates by a process of facilitated diffusion of soluble carrier proteins, in which vectoriality is provided by compartment-specific assembly and disassembly of cargo-carrier complexes. The carriers recognize localization signals on the cargo and can bind to pore proteins. They also bind a small GTPase, Ran, whose GTP-bound form is predominantly nuclear. Ran-GTP dissociates import carriers from their cargo and promotes the assembly of export carriers with cargo. The ongoing discovery of numerous carriers, Ran-independent transport mechanisms, and cofactors highlights the complexity of the nuclear transport process. Multiple regulatory mechanisms are also being identified that control cargo-carrier interactions. Circadian rhythms, cell cycle, transcription, RNA processing, and signal transduction are all regulated at the level of nucleocytoplasmic transport. This review focuses on recent discoveries in the field, with an emphasis on the carriers and cofactors involved in transport and on possible mechanisms for movement through the nuclear pores.
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Herzig, Sébastien, Etienne Raemy, Sylvie Montessuit, Jean-Luc Veuthey, Nicola Zamboni, Benedikt Westermann, Edmund R. S. Kunji, and Jean-Claude Martinou. "Identification and Functional Expression of the Mitochondrial Pyruvate Carrier." Science 337, no. 6090 (May 24, 2012): 93–96. http://dx.doi.org/10.1126/science.1218530.

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The transport of pyruvate, the end product of glycolysis, into mitochondria is an essential process that provides the organelle with a major oxidative fuel. Although the existence of a specific mitochondrial pyruvate carrier (MPC) has been anticipated, its molecular identity remained unknown. We report that MPC is a heterocomplex formed by two members of a family of previously uncharacterized membrane proteins that are conserved from yeast to mammals. Members of the MPC family were found in the inner mitochondrial membrane, and yeast mutants lacking MPC proteins showed severe defects in mitochondrial pyruvate uptake. Coexpression of mouse MPC1 and MPC2 in Lactococcus lactis promoted transport of pyruvate across the membrane. These observations firmly establish these proteins as essential components of the MPC.
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Kunji, Edmund R. S., Martin S. King, Jonathan J. Ruprecht, and Chancievan Thangaratnarajah. "The SLC25 Carrier Family: Important Transport Proteins in Mitochondrial Physiology and Pathology." Physiology 35, no. 5 (September 1, 2020): 302–27. http://dx.doi.org/10.1152/physiol.00009.2020.

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Members of the mitochondrial carrier family (SLC25) transport a variety of compounds across the inner membrane of mitochondria. These transport steps provide building blocks for the cell and link the pathways of the mitochondrial matrix and cytosol. An increasing number of diseases and pathologies has been associated with their dysfunction. In this review, the molecular basis of these diseases is explained based on our current understanding of their transport mechanism.
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Dorwart, Michael R., Nikolay Shcheynikov, Dongki Yang, and Shmuel Muallem. "The Solute Carrier 26 Family of Proteins in Epithelial Ion Transport." Physiology 23, no. 2 (April 2008): 104–14. http://dx.doi.org/10.1152/physiol.00037.2007.

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Transepithelial Cl− and HCO3− transport is critically important for the function of all epithelia and, when altered or ablated, leads to a number of diseases, including cystic fibrosis, congenital chloride diarrhea, deafness, and hypotension ( 78 , 111 , 119 , 126 ). HCO3− is the biological buffer that maintains acid-base balance, thereby preventing metabolic and respiratory acidosis ( 48 ). HCO3− also buffers the pH of the mucosal layers that line all epithelia, protecting them from injury ( 2 ). Being a chaotropic ion, HCO3− is essential for solubilization of ions and macromolecules such as mucins and digestive enzymes in secreted fluids. Most epithelia have a Cl−/HCO3 exchange activity in the luminal membrane. The molecular nature of this activity remained a mystery for many years until the discovery of SLC26A3 and the realization that it is a member of a new family of Cl− and HCO3− transporters, the SLC26 family ( 73 , 78 ). This review will highlight structural features, the functional diversity, and several regulatory aspects of the SLC26 transporters.
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Jeschek, D., M. Steiger, D. Mattanovich, and M. Sauer. "Phospholipid vesicles to determine the transport functionality of mitochondrial carrier proteins." New Biotechnology 44 (October 2018): S113. http://dx.doi.org/10.1016/j.nbt.2018.05.1017.

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Wohlrab, Hartmut. "Transport proteins (carriers) of mitochondria." IUBMB Life 61, no. 1 (January 2009): 40–46. http://dx.doi.org/10.1002/iub.139.

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Galano, Melanie, Sathvika Venugopal, and Vassilios Papadopoulos. "Role of STAR and SCP2/SCPx in the Transport of Cholesterol and Other Lipids." International Journal of Molecular Sciences 23, no. 20 (October 11, 2022): 12115. http://dx.doi.org/10.3390/ijms232012115.

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Cholesterol is a lipid molecule essential for several key cellular processes including steroidogenesis. As such, the trafficking and distribution of cholesterol is tightly regulated by various pathways that include vesicular and non-vesicular mechanisms. One non-vesicular mechanism is the binding of cholesterol to cholesterol transport proteins, which facilitate the movement of cholesterol between cellular membranes. Classic examples of cholesterol transport proteins are the steroidogenic acute regulatory protein (STAR; STARD1), which facilitates cholesterol transport for acute steroidogenesis in mitochondria, and sterol carrier protein 2/sterol carrier protein-x (SCP2/SCPx), which are non-specific lipid transfer proteins involved in the transport and metabolism of many lipids including cholesterol between several cellular compartments. This review discusses the roles of STAR and SCP2/SCPx in cholesterol transport as model cholesterol transport proteins, as well as more recent findings that support the role of these proteins in the transport and/or metabolism of other lipids.
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Dissertations / Theses on the topic "Carrier and Transport Proteins"

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Covey, Scott D. Trigatti Bernardo L. "Carrier mediated lipid transport /." *McMaster only, 2003.

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Kwan, Miu-fan, and 關妙芬. "Characterization of TM4 of NRAMP1: implication for FEII transport." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2003. http://hub.hku.hk/bib/B29275143.

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Grabski, Robert. "Using RNA interference to study the function of the tethering protein p115 in ER-Golgi traffic." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2008p/grabski.pdf.

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Parry, Geraint. "Investigating the mechanisms of auxin transport." Thesis, University of Nottingham, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.391391.

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Christoffersen, Catherine Anne. "Molecular analysis of the ferric-enterobactin fepDGC transport permease complex in escherichia coli." free to MU campus, to others for purchase, 1997. http://wwwlib.umi.com/cr/mo/fullcit?p9842593.

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Bright, Alison R. "A Role for Intraflagellar Transport Proteins in Mitosis: A Dissertation." eScholarship@UMMS, 2013. https://escholarship.umassmed.edu/gsbs_diss/682.

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Disruption of cilia proteins results in a range of disorders called ciliopathies. However, the mechanism by which cilia dysfunction contributes to disease is not well understood. Intraflagellar transport (IFT) proteins are required for ciliogenesis. They carry ciliary cargo along the microtubule axoneme while riding microtubule motors. Interestingly, IFT proteins localize to spindle poles in non-ciliated, mitotic cells, suggesting a mitotic function for IFT proteins. Based on their role in cilia, we hypothesized that IFT proteins regulate microtubule-based transport during mitotic spindle assembly. Biochemical investigation revealed that in mitotic cells IFT88, IFT57, IFT52, and IFT20 interact with dynein1, a microtubule motor required for spindle pole maturation. Furthermore, IFT88 co-localizes with dynein1 and its mitotic cargo during spindle assembly, suggesting a role for IFT88 in regulating dynein-mediated transport to spindle poles. Based on these results we analyzed spindle poles after IFT protein depletion and found that IFT88 depletion disrupted EB1, γ-tubulin, and astral microtubule arrays at spindle poles. Unlike IFT88, depletion of IFT57, IFT52, or IFT20 did not disrupt spindle poles. Strikingly, the simultaneous depletion of IFT88 and IFT20 rescued the spindle pole disruption caused by IFT88 depletion alone, suggesting a model in which IFT88 negatively regulates IFT20, and IFT20 negatively regulates microtubulebased transport during mitosis. Our work demonstrates for the first time that IFT proteins function with dynein1 in mitosis, and it also raises the important possibility that mitotic defects caused by IFT protein disruption could contribute to the phenotypes associated with ciliopathies.
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Bright, Alison R. "A Role for Intraflagellar Transport Proteins in Mitosis: A Dissertation." eScholarship@UMMS, 2006. http://escholarship.umassmed.edu/gsbs_diss/682.

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Disruption of cilia proteins results in a range of disorders called ciliopathies. However, the mechanism by which cilia dysfunction contributes to disease is not well understood. Intraflagellar transport (IFT) proteins are required for ciliogenesis. They carry ciliary cargo along the microtubule axoneme while riding microtubule motors. Interestingly, IFT proteins localize to spindle poles in non-ciliated, mitotic cells, suggesting a mitotic function for IFT proteins. Based on their role in cilia, we hypothesized that IFT proteins regulate microtubule-based transport during mitotic spindle assembly. Biochemical investigation revealed that in mitotic cells IFT88, IFT57, IFT52, and IFT20 interact with dynein1, a microtubule motor required for spindle pole maturation. Furthermore, IFT88 co-localizes with dynein1 and its mitotic cargo during spindle assembly, suggesting a role for IFT88 in regulating dynein-mediated transport to spindle poles. Based on these results we analyzed spindle poles after IFT protein depletion and found that IFT88 depletion disrupted EB1, γ-tubulin, and astral microtubule arrays at spindle poles. Unlike IFT88, depletion of IFT57, IFT52, or IFT20 did not disrupt spindle poles. Strikingly, the simultaneous depletion of IFT88 and IFT20 rescued the spindle pole disruption caused by IFT88 depletion alone, suggesting a model in which IFT88 negatively regulates IFT20, and IFT20 negatively regulates microtubulebased transport during mitosis. Our work demonstrates for the first time that IFT proteins function with dynein1 in mitosis, and it also raises the important possibility that mitotic defects caused by IFT protein disruption could contribute to the phenotypes associated with ciliopathies.
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Nelson, Bryn D. "Examining the role of MalG in the assembly and function of the maltose transport complex in Escherichia coli : implications for the study of integral membrane proteins /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/11508.

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Bradley, Shannon. "Polymorphisms in the promoter region of the dopamine transporter : a candidate locus for alcohol abuse." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0029/MQ64326.pdf.

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Millman, Jonathan Scott Andrews David. "Characterization of membrane-binding by FtsY, the prokaryote SRP receptor /." *McMaster only, 2002.

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Books on the topic "Carrier and Transport Proteins"

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W, Quick Michael, ed. Transmembrane transporters. New York: Wiley-Liss, 2002.

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Pont, J. J. H. H. M. de., ed. Molecular aspects of transport proteins. Amsterdam: Elsevier, 1992.

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Harris, James R. Cholesterol binding and cholesterol transport proteins: Structure and function in health and disease. Edited by SpringerLink (Online service). Dordrecht: Springer Verlag, 2010.

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Griffith, Jeffrey. The transporter factsbook. San Diego, Calif: Academic Press, 1997.

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A, Baldwin Stephen, ed. Membrane transport: A practical approach. Oxford: Oxford University Press, 2000.

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W, Gould Gwyn, ed. Facilitative glucose transporters. Austin: R.G. Landes, 1997.

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Society of General Physiologists. (46th 1992 Marine Biological Laboratory). Molecular biology and function of carrier proteins. New York: Rockerfeller University Press, 1992.

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S, Rothman S., ed. Membrane protein transport: A multi-volume treatise. Greenwich, Conn: JAI, 1995.

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A, Reith Maarten E., ed. Neurotransmitter transporters: Structure, function, and regulation. 2nd ed. Totowa, NJ: Humana Press, 2002.

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E, Barrett Kim, and Donowitz Mark 1943-, eds. Gastrointestinal transport: Molecular physiology. San Diego: Academic Press, 2001.

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Book chapters on the topic "Carrier and Transport Proteins"

1

Wang, Changmin, and Zhiwei Li. "Transport and Carrier Proteins." In Clinical Molecular Diagnostics, 195–205. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-1037-0_15.

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Schroeder, Friedhelm, Huan Huang, Avery L. McIntosh, Barbara P. Atshaves, Gregory G. Martin, and Ann B. Kier. "Caveolin, Sterol Carrier Protein-2, Membrane Cholesterol-Rich Microdomains and Intracellular Cholesterol Trafficking." In Cholesterol Binding and Cholesterol Transport Proteins:, 279–318. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-8622-8_10.

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R.Adiga, P., P. B. Seshagiri, P. V. Malathy, and S. V. Sandhya. "REPRODUCTION SPECIFIC VITAMIN CARRIER PROTEINS INVOLVED IN TRANSPLACENTAL VITAMIN TRANSPORT IN MAMMALS INCLUDING PRIMATES." In Pregnancy Proteins in Animals, edited by Jann Hau, 317–30. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110858167-032.

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Roelcke, U., E. W. Radü, and K. L. Leenders. "11C-Methionine and 82Rubidium Uptake in Human Brain Tumors: Comparison of Carrier Dependent Blood-Brain Barrier Transport." In PET Studies on Amino Acid Metabolism and Protein Synthesis, 197–201. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1620-6_14.

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Morkoç, Hadis. "Carrier Transport." In Nitride Semiconductors and Devices, 233–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-58562-3_8.

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Böer, Karl W. "Carrier Transport." In Handbook of the Physics of Thin-Film Solar Cells, 271–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36748-9_16.

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Evstigneev, Mykhaylo. "Carrier Transport." In Introduction to Semiconductor Physics and Devices, 197–211. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-08458-4_8.

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Hubbard, Seth. "Carrier Transport." In Photovoltaic Solar Energy, 47–53. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781118927496.ch6.

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Rettinger, Jürgen, Silvia Schwarz, and Wolfgang Schwarz. "Carrier-Transport." In Elektrophysiologie, 119–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-56662-6_7.

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Brunori, Maurizio, Massimiliano Coletta, and Bruno Giardina. "Oxygen carrier proteins." In Metalloproteins, 263–331. London: Palgrave Macmillan UK, 1985. http://dx.doi.org/10.1007/978-1-349-06375-8_6.

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Conference papers on the topic "Carrier and Transport Proteins"

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Cuppoletti, John. "Composite Synthetic Membranes Containing Native and Engineered Transport Proteins." In ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-449.

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Our membrane transport protein laboratory has worked with material scientists, computational chemists and electrical and mechanical engineers to design bioactuators and sensing devices. The group has demonstrated that it is possible to produce materials composed native and engineered biological transport proteins in a variety of synthetic porous and solid materials. Biological transport proteins found in nature include pumps, which use energy to produce gradients of solutes, ion channels, which dissipate ion gradients, and a variety of carriers which can either transport substances down gradients or couple the uphill movement of substances to the dissipation of gradients. More than one type of protein can be reconstituted into the membranes to allow coupling of processes such as forming concentration gradients with ion pumps and dissipating them with an ion channel. Similarly, ion pumps can provide ion gradients to allow the co-transport of another substance. These systems are relevant to bioactuation. An example of a bioactuator that has recently been developed in the laboratory was based on a sucrose-proton exchanger coupled to a proton pump driven by ATP. When coupled together, the net reaction across the synthetic membrane was ATP driven sucrose transport across a flexible membrane across a closed space. As sucrose was transported, net flow of water occurred, causing pressure and deformation of the membrane. Transporters are regulated in nature. These proteins are sensitive to voltage, pH, sensitivity to a large variety of ligands and they can be modified to gain or lose these responses. Examples of sensors include ligand gated ion channels reconstituted on solid and permeable supports. Such sensors have value as high throughput screening devices for drug screening. Other sensors that have been developed in the laboratory include sensors for membrane active bacterial products such as the anthrax pore protein. These materials can be self assembled or manufactured by simple techniques, allowing the components to be stored in a stable form for years before (self) assembly on demand. The components can be modified at the atomic level, and are composed of nanostructures. Ranges of sizes of structures using these components range from the microscopic to macroscopic scale. The transport proteins can be obtained from natural sources or can be produced by recombinant methods from the genomes of all kingdoms including archea, bacteria and eukaryotes. For example, the laboratory is currently studying an ion channel from a thermophile from deep sea vents which has a growth optimum of 90 degrees centigrade, and has membrane transport proteins with very high temperature stability. The transport proteins can also be genetically modified to produce new properties such as activation by different ligands or transport of new substances such as therapeutic agents. The structures of many of these proteins are known, allowing computational chemists to help understand and predict the transport processes and to guide the engineering of new properties for the transport proteins and the composite membranes. Supported by DARPA and USARMY MURI Award and AFOSR.
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Quan, Glen Lelyn, Kentaro Matsumiya, Michiaki Araki, Yasuki Matsumura, and Yoshihiko Hirata. "The role of sophorolipid as carrier of active substances." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/hnkx3869.

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Sophorolipid is a glycolipid-type biosurfactant, produced from natural sources by fermentation with a nonpathogenic yeast Starmerella bombicola. Its structure is composed of 2 hydrophilic parts, a sophorose unit, a glucose disaccharide glycosically linked to a hydroxyl fatty acid. Its structure spontaneously forms a vesicle of about 100 nm in an aqueous solution, which is similar to that of liposomes used as drug delivery systems and transdermal absorption promoters. It can be expected to have an effect of promoting permeation of active substances such as lactoferrin. Lactoferrin is an iron-binding glycoprotein having a molecular weight of about 80 kDa, and is most abundant in breast milk in the living body. Since it is also present in amniotic fluid that protects the mother and fetus, it is important to study the physiological relationship between skin and lactoferrin. The transdermal administration of lactoferrin with sophorolipid was verified, followed by the investigation protein-surfactant interactions between bovine lactoferrin and sophorolipid. Structural changes were further observed using spectroscopic, microscopic and biochemical methods under weakly acidic and neutral pH conditions. From particle size analysis by dynamic light scattering, microscopic observation by cryo-SEM, and digestion pattern observation by enzyme treatment, it was confirmed that bovine lactoferrin and sophorolipid interact with each other to form a sheet and nanometer-sized coagulation at pH 5.0 and 7.0 forming an aggregate, which was considered to be due to the self-organizing structure characteristic of sophorolipid. It can be concluded that sophorolipid has a potential of being a transport carrier of active substances, which can have vast applications not only in cosmetics but in drug delivery systems as well. Biosurfactants and biopolymers: Between interactions, orthogonality and mutual
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Panta, Yogendra M., Sanket Aryal, and Param C. Adhikari. "Analysis of Electrokinetic Fluid Flow in T-Shaped DNA Chips." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80667.

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Lab-on-chip devices promise for many novel applications concerning the transport of the liquid samples and other solutions in the order of micro-scale dimensions. One of the efficient methods for transporting fluid in the samples is through electrokinetic effects, where an electric field will be applied to charged ions such as DNA, a negatively charged ion or proteins. These ions are carried over in the microchannel by the application of electric fields through the entire solution from inlet via probe region for its detection to outlet and the determination of concentration distribution. COMSOL, commercially available multiphysics software, with its specific MEMS and Chemical Engineering modules were employed and simulated for the analysis of fluid velocity and ionic concentration throughout the channel of various shapes. The ionic fluid concentrations and velocities in the channel and at the outlet are plotted against the potential differences across the two inlets in which DNA sample was introduced from one inlet and a buffer solution was supplied from another inlet.
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Sundaresan, Vishnu Baba, and Donald J. Leo. "Modeling and Characterization of a Chemomechanical Actuator Based on Protein Transporters." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-43712.

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Plants and animal cells are naturally occurring actuators that exhibit force and motion driven by fluid transport through the cell membrane. The protein transporters embedded in the cell membrane serve as the selective gateway for ion and fluid transport. The actuator presented in this work generates force and deformation from mass transport through an artificial membrane with protein transporters extracted from plant cell membranes. The artificial membrane is formed from purified 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-L-Serine] (Sodium Salt) (POPS), 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-Phosphoethanolamine (POPE) lipids and supported on a porous substrate. The protein transporter used in the actuator membrane is a proton-sucrose cotransporter, SUT4, extracted from yeast cells that genetically modified to grow the cotransporter in their cell membranes. The SUT4 transporter conducts proton and sucrose from the side of the membrane with higher concentration and carries water molecules across the membrane. It is observed from transport characterization experiments that fluid flux through the membrane varies with the applied sucrose concentration and hence is chosen as the control stimulus in the actuator. A modified four-state facilitated diffusion model is applied to the transport characterization data to compute the two characteristic parameters for fluid transport, saturation concentration and translocation rate, through the membrane. The flux rate through the membrane is observed to increase with the concentration till a particular value and saturates at a higher concentration. The concentration at which the flux rate through the membrane saturates is referred to as the saturation concentration. The saturation concentration for the actuator is experimentally found to be 6±0.6mM sucrose on the side with lower pH. The corresponding maximum translocation rate is found to be 9.6±1.2 nl/μ.cm2.min. The maximum steady state deformation produced by the actuator is observed at 30 mM sucrose that corresponds to a force of 0.89 mN.
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Hamm, Peter, Marco Schade, Ellen H. G. Backus, Alessandro Moretto, and Claudio Toniolo. "Vibrational Energy Transport in Peptides and Proteins." In International Conference on Ultrafast Phenomena. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/up.2010.thd2.

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Berger, Michael, Sarah Ruepp, and Henrik Wessing. "High capacity carrier ethernet transport." In 2010 International Conference on High Performance Switching and Routing (HPSR). IEEE, 2010. http://dx.doi.org/10.1109/hpsr.2010.5580254.

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Tang, D. D., F. F. Fang, M. Scheuermann, T. C. Chen, and G. Sai-Halasz. "Minority carrier transport in silicon." In 1986 International Electron Devices Meeting. IRE, 1986. http://dx.doi.org/10.1109/iedm.1986.191100.

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Kantola, Raimo, Marko Luoma, and Olli-Pekka Lamminen. "Transport for Carrier Grade Internet." In 2009 IEEE Globecom Workshops. IEEE, 2009. http://dx.doi.org/10.1109/glocomw.2009.5360778.

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FERRY, David K., Richard AKIS, Sujeeth UDIPI, Dragica VASILESKA, David P. PIVIN, Kevin M. CONNOLLY, Jonathon P. BIRD, et al. "Carrier Transport in Nanoscale Structures." In 1996 International Conference on Solid State Devices and Materials. The Japan Society of Applied Physics, 1996. http://dx.doi.org/10.7567/ssdm.1996.a-7-1.

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Boland, Wilhelm. "Sequestration and transport proteins in leaf beetle larvae." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.91462.

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Reports on the topic "Carrier and Transport Proteins"

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Martinelli, R. U., D. Z. Garbuzov, H. Lee, N. Morris, T. Odubanjo, and J. C. Connolly. Minority-carrier transport in InGaAsSb thermophotovoltaic diodes. Office of Scientific and Technical Information (OSTI), May 1997. http://dx.doi.org/10.2172/319871.

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Williams, Timothy J., Ramesh Balakrishnan, Brian K. Radak, James C. Phillips, Wei Jiang, Sunhwan Jo, Laxmikant V. Kale, Klaus Schulten, and Benoit Roux. Free Energy Landscapes of Membrane Transport Proteins. Office of Scientific and Technical Information (OSTI), September 2017. http://dx.doi.org/10.2172/1483996.

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S.E. Salzman. CLASSIFICATION OF THE MGR CARRIER/CASK TRANSPORT SYSTEM. Office of Scientific and Technical Information (OSTI), August 1999. http://dx.doi.org/10.2172/860581.

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Itoh, Kohei. Low temperature carrier transport properties in isotopically controlled germanium. Office of Scientific and Technical Information (OSTI), December 1994. http://dx.doi.org/10.2172/29414.

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Kim, Ki Wook, and M. A. Littlejohn. Solid-State Dynamics and Carrier Transport in Supervelocity Semiconductors. Fort Belvoir, VA: Defense Technical Information Center, April 2004. http://dx.doi.org/10.21236/ada421810.

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Guerinot, Mary Lou, and David Eide. Characterization of a New Family of Metal Transport Proteins. Office of Scientific and Technical Information (OSTI), June 1999. http://dx.doi.org/10.2172/829905.

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Hess, Henry. Active Transport of Nanomaterials Using Motor Proteins -Final Report. Office of Scientific and Technical Information (OSTI), September 2005. http://dx.doi.org/10.2172/859095.

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Giles, Durham, Harry Frankel, Michael Delwiche, Avshalom Grinstein, and Miriam Austerweil. Spray Target Architecture and Turbulent Transport in Air-Carrier Pesticide Application Systems. United States Department of Agriculture, March 1994. http://dx.doi.org/10.32747/1994.7604315.bard.

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Sundqvist, Kyle Michael. Carrier Transport and Related Effects in Detectors of the Cryogenic Dark Matter Search. Office of Scientific and Technical Information (OSTI), January 2012. http://dx.doi.org/10.2172/1128107.

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Guerinot, M. L. Characterization of a new family of metal transport proteins. 1998 annual progress report. Office of Scientific and Technical Information (OSTI), June 1998. http://dx.doi.org/10.2172/13718.

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