Larminie

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 57 Experts worldwide ranked by ideXlab platform

Robert J. White - One of the best experts on this subject based on the ideXlab platform.

  • Retinoblastoma Protein Disrupts Interactions Required for RNA Polymerase III Transcription
    Molecular and cellular biology, 2000
    Co-Authors: Josephine E. Sutcliffe, Simon J. Allison, Timothy R. P. Brown, Pamela H. Scott, Robert J. White
    Abstract:

    The retinoblastoma protein (RB) has been shown to suppress RNA polymerase (Pol) III transcription in vivo (R. J. White, D. Trouche, K. Martin, S. P. Jackson, and T. Kouzarides, Nature 382:88-90, 1996). This regulation involves interaction with TFIIIB, a multisubunit factor that is required for the expression of all Pol III templates (C. G. C. Larminie, C. A. Cairns, R. Mital, K. Martin, T. Kouzarides, S. P. Jackson, and R. J. White, EMBO J. 16:2061-2071, 1997; W.-M. Chu, Z. Wang, R. G. Roeder, and C. W. Schmid, J. Biol. Chem. 272:14755-14761, 1997). However, it has not been established why RB binding to TFIIIB results in transcriptional repression. For several Pol II-transcribed genes, RB has been shown to inhibit expression by recruiting histone deacetylases, which are thought to decrease promoter accessibility. We present evidence that histone deacetylases exert a negative effect on Pol III activity in vivo. However, RB remains able to regulate Pol III transcription in the presence of the histone deacetylase inhibitor trichostatin A. Instead, RB represses by disrupting interactions between TFIIIB and other components of the basal Pol III transcription apparatus. Recruitment of TFIIIB to most class III genes requires its binding to TFIIIC2, but this can be blocked by RB. In addition, RB disrupts the interaction between TFIIIB and Pol III that is essential for transcription. The ability of RB to inhibit these key interactions can explain its action as a potent repressor of class III gene expression.

  • RNA Polymerase III Transcription Factor IIIB Is a Target for Repression by Pocket Proteins p107 and p130
    Molecular and cellular biology, 1999
    Co-Authors: Josephine E. Sutcliffe, Carol A. Cairns, Angela Mclees, Simon J. Allison, Kerrie Tosh, Robert J. White
    Abstract:

    RNA polymerase III (Pol III) transcription is subject to repression by the retinoblastoma protein RB, both in vitro and in vivo (R. J. White, D. Trouche, K. Martin, S. P. Jackson, and T. Kouzarides, Nature 382:88-90, 1996). This is achieved through a direct interaction between RB and TFIIIB, a multisubunit factor that is required for the expression of all Pol III templates (C. G. C. Larminie, C. A. Cairns, R. Mital, K. Martin, T. Kouzarides, S. P. Jackson, and R. J. White, EMBO J. 16:2061-2071, 1997; W.-M. Chu, Z. Wang, R. G. Roeder, and C. W. Schmid, J. Biol. Chem. 272:14755-14761, 1997). p107 and p130 are two closely related proteins that display 30 to 35% identity with the RB polypeptide and share some of its functions. We show that p107 and p130 can both repress Pol III transcription in transient transfection assays or when added to cell extracts. Pull-down assays and immunoprecipitations using recombinant components demonstrate that a subunit of TFIIIB interacts physically with p107 and p130. In addition, endogenous TFIIIB is shown by cofractionation and coimmunoprecipitation to associate stably with both p107 and p130. Disruption of this interaction in vivo by using the E7 oncoprotein of human papillomavirus results in a marked increase in Pol III transcription. Pol III activity is also deregulated in fibroblasts derived from p107 p130 double knockout mice. We conclude that TFIIIB is targeted for repression not only by RB but also by its relatives p107 and p130.

Josephine E. Sutcliffe - One of the best experts on this subject based on the ideXlab platform.

  • Retinoblastoma Protein Disrupts Interactions Required for RNA Polymerase III Transcription
    Molecular and cellular biology, 2000
    Co-Authors: Josephine E. Sutcliffe, Simon J. Allison, Timothy R. P. Brown, Pamela H. Scott, Robert J. White
    Abstract:

    The retinoblastoma protein (RB) has been shown to suppress RNA polymerase (Pol) III transcription in vivo (R. J. White, D. Trouche, K. Martin, S. P. Jackson, and T. Kouzarides, Nature 382:88-90, 1996). This regulation involves interaction with TFIIIB, a multisubunit factor that is required for the expression of all Pol III templates (C. G. C. Larminie, C. A. Cairns, R. Mital, K. Martin, T. Kouzarides, S. P. Jackson, and R. J. White, EMBO J. 16:2061-2071, 1997; W.-M. Chu, Z. Wang, R. G. Roeder, and C. W. Schmid, J. Biol. Chem. 272:14755-14761, 1997). However, it has not been established why RB binding to TFIIIB results in transcriptional repression. For several Pol II-transcribed genes, RB has been shown to inhibit expression by recruiting histone deacetylases, which are thought to decrease promoter accessibility. We present evidence that histone deacetylases exert a negative effect on Pol III activity in vivo. However, RB remains able to regulate Pol III transcription in the presence of the histone deacetylase inhibitor trichostatin A. Instead, RB represses by disrupting interactions between TFIIIB and other components of the basal Pol III transcription apparatus. Recruitment of TFIIIB to most class III genes requires its binding to TFIIIC2, but this can be blocked by RB. In addition, RB disrupts the interaction between TFIIIB and Pol III that is essential for transcription. The ability of RB to inhibit these key interactions can explain its action as a potent repressor of class III gene expression.

  • RNA Polymerase III Transcription Factor IIIB Is a Target for Repression by Pocket Proteins p107 and p130
    Molecular and cellular biology, 1999
    Co-Authors: Josephine E. Sutcliffe, Carol A. Cairns, Angela Mclees, Simon J. Allison, Kerrie Tosh, Robert J. White
    Abstract:

    RNA polymerase III (Pol III) transcription is subject to repression by the retinoblastoma protein RB, both in vitro and in vivo (R. J. White, D. Trouche, K. Martin, S. P. Jackson, and T. Kouzarides, Nature 382:88-90, 1996). This is achieved through a direct interaction between RB and TFIIIB, a multisubunit factor that is required for the expression of all Pol III templates (C. G. C. Larminie, C. A. Cairns, R. Mital, K. Martin, T. Kouzarides, S. P. Jackson, and R. J. White, EMBO J. 16:2061-2071, 1997; W.-M. Chu, Z. Wang, R. G. Roeder, and C. W. Schmid, J. Biol. Chem. 272:14755-14761, 1997). p107 and p130 are two closely related proteins that display 30 to 35% identity with the RB polypeptide and share some of its functions. We show that p107 and p130 can both repress Pol III transcription in transient transfection assays or when added to cell extracts. Pull-down assays and immunoprecipitations using recombinant components demonstrate that a subunit of TFIIIB interacts physically with p107 and p130. In addition, endogenous TFIIIB is shown by cofractionation and coimmunoprecipitation to associate stably with both p107 and p130. Disruption of this interaction in vivo by using the E7 oncoprotein of human papillomavirus results in a marked increase in Pol III transcription. Pol III activity is also deregulated in fibroblasts derived from p107 p130 double knockout mice. We conclude that TFIIIB is targeted for repression not only by RB but also by its relatives p107 and p130.

Simon J. Allison - One of the best experts on this subject based on the ideXlab platform.

  • Retinoblastoma Protein Disrupts Interactions Required for RNA Polymerase III Transcription
    Molecular and cellular biology, 2000
    Co-Authors: Josephine E. Sutcliffe, Simon J. Allison, Timothy R. P. Brown, Pamela H. Scott, Robert J. White
    Abstract:

    The retinoblastoma protein (RB) has been shown to suppress RNA polymerase (Pol) III transcription in vivo (R. J. White, D. Trouche, K. Martin, S. P. Jackson, and T. Kouzarides, Nature 382:88-90, 1996). This regulation involves interaction with TFIIIB, a multisubunit factor that is required for the expression of all Pol III templates (C. G. C. Larminie, C. A. Cairns, R. Mital, K. Martin, T. Kouzarides, S. P. Jackson, and R. J. White, EMBO J. 16:2061-2071, 1997; W.-M. Chu, Z. Wang, R. G. Roeder, and C. W. Schmid, J. Biol. Chem. 272:14755-14761, 1997). However, it has not been established why RB binding to TFIIIB results in transcriptional repression. For several Pol II-transcribed genes, RB has been shown to inhibit expression by recruiting histone deacetylases, which are thought to decrease promoter accessibility. We present evidence that histone deacetylases exert a negative effect on Pol III activity in vivo. However, RB remains able to regulate Pol III transcription in the presence of the histone deacetylase inhibitor trichostatin A. Instead, RB represses by disrupting interactions between TFIIIB and other components of the basal Pol III transcription apparatus. Recruitment of TFIIIB to most class III genes requires its binding to TFIIIC2, but this can be blocked by RB. In addition, RB disrupts the interaction between TFIIIB and Pol III that is essential for transcription. The ability of RB to inhibit these key interactions can explain its action as a potent repressor of class III gene expression.

  • RNA Polymerase III Transcription Factor IIIB Is a Target for Repression by Pocket Proteins p107 and p130
    Molecular and cellular biology, 1999
    Co-Authors: Josephine E. Sutcliffe, Carol A. Cairns, Angela Mclees, Simon J. Allison, Kerrie Tosh, Robert J. White
    Abstract:

    RNA polymerase III (Pol III) transcription is subject to repression by the retinoblastoma protein RB, both in vitro and in vivo (R. J. White, D. Trouche, K. Martin, S. P. Jackson, and T. Kouzarides, Nature 382:88-90, 1996). This is achieved through a direct interaction between RB and TFIIIB, a multisubunit factor that is required for the expression of all Pol III templates (C. G. C. Larminie, C. A. Cairns, R. Mital, K. Martin, T. Kouzarides, S. P. Jackson, and R. J. White, EMBO J. 16:2061-2071, 1997; W.-M. Chu, Z. Wang, R. G. Roeder, and C. W. Schmid, J. Biol. Chem. 272:14755-14761, 1997). p107 and p130 are two closely related proteins that display 30 to 35% identity with the RB polypeptide and share some of its functions. We show that p107 and p130 can both repress Pol III transcription in transient transfection assays or when added to cell extracts. Pull-down assays and immunoprecipitations using recombinant components demonstrate that a subunit of TFIIIB interacts physically with p107 and p130. In addition, endogenous TFIIIB is shown by cofractionation and coimmunoprecipitation to associate stably with both p107 and p130. Disruption of this interaction in vivo by using the E7 oncoprotein of human papillomavirus results in a marked increase in Pol III transcription. Pol III activity is also deregulated in fibroblasts derived from p107 p130 double knockout mice. We conclude that TFIIIB is targeted for repression not only by RB but also by its relatives p107 and p130.

J. Cathelin - One of the best experts on this subject based on the ideXlab platform.

  • Design of a high voltage input - output ratio dc-dc converter dedicated to small power fuel cell systems
    European Physical Journal: Applied Physics, 2017
    Co-Authors: Olivier Bethoux, J. Cathelin
    Abstract:

    Consuming chemical energy, fuel cells produce simultaneously heat, water and useful electrical power [J.M. Andújar, F. Segura, Renew. Sust. Energy Rev. , 2309 (2009)], [J. Larminie, A. Dicks, , 2nd edn. (John Wiley & Sons, 2003)]. As a matter of fact, the voltage generated by a fuel cell strongly depends on both the load power demand and the operating conditions. Besides, as a result of many design aspects, fuel cells are low voltage and high current electric generators. On the contrary, electric loads are commonly designed for small voltage swing and a high V/I ratio in order to minimize Joule losses. Therefore, electric loads supplied by fuel cells are typically fed by means of an intermediate power voltage regulator. The specifications of such a power converter are to be able to step up the input voltage with a high ratio (a ratio of 10 is a classic situation) and also to work with an excellent efficiency (in order to minimize its size, its weight and its losses) [A. Shahin, B. Huang, J.P. Martin, S. Pierfederici, B. Davat, Energy Conv. Manag. , 56 (2010)]. This paper deals with the design of this essential ancillary device. It intends to bring out the best structure for fulfilling this function. Several dc-dc converters with large voltage step-up ratios are introduced. A topology based on a coupled inductor or tapped inductor is closely studied. A detailed modelling is performed with the purpose of providing designing rules. This model is validated with both simulation and implementation. The experimental prototype is based on the following specifications: the fuel cell output voltage ranges from a 50 V open-voltage to a 25 V rated voltage while the load requires a constant 250 V voltage. The studied coupled inductor converter is compared with a classic boost converter commonly used in this voltage elevating application. Even though the voltage regulator faces severe FC specifications, the measured efficiency reaches 96% at the rated power whereas conventional boost efficiency barely achieves 91.5% in the same operating conditions.

  • Design of a high voltage input – output ratio dc-dc converter dedicated to small power fuel cell systems
    The European Physical Journal Applied Physics, 2010
    Co-Authors: Olivier Bethoux, J. Cathelin
    Abstract:

    Consuming chemical energy, fuel cells produce simultaneously heat, water and useful electrical power [J.M. Andujar, F. Segura, Renew. Sust. Energy Rev. 13 , 2309 (2009)], [J. Larminie, A. Dicks, Fuel Cell Systems Explained , 2nd edn. (John Wiley & Sons, 2003)]. As a matter of fact, the voltage generated by a fuel cell strongly depends on both the load power demand and the operating conditions. Besides, as a result of many design aspects, fuel cells are low voltage and high current electric generators. On the contrary, electric loads are commonly designed for small voltage swing and a high V/I ratio in order to minimize Joule losses. Therefore, electric loads supplied by fuel cells are typically fed by means of an intermediate power voltage regulator. The specifications of such a power converter are to be able to step up the input voltage with a high ratio (a ratio of 10 is a classic situation) and also to work with an excellent efficiency (in order to minimize its size, its weight and its losses) [A. Shahin, B. Huang, J.P. Martin, S. Pierfederici, B. Davat, Energy Conv. Manag. 51 , 56 (2010)]. This paper deals with the design of this essential ancillary device. It intends to bring out the best structure for fulfilling this function. Several dc-dc converters with large voltage step-up ratios are introduced. A topology based on a coupled inductor or tapped inductor is closely studied. A detailed modelling is performed with the purpose of providing designing rules. This model is validated with both simulation and implementation. The experimental prototype is based on the following specifications: the fuel cell output voltage ranges from a 50 V open-voltage to a 25 V rated voltage while the load requires a constant 250 V voltage. The studied coupled inductor converter is compared with a classic boost converter commonly used in this voltage elevating application. Even though the voltage regulator faces severe FC specifications, the measured efficiency reaches 96% at the rated power whereas conventional boost efficiency barely achieves 91.5% in the same operating conditions.

Pavelka Michal - One of the best experts on this subject based on the ideXlab platform.

  • Termodynamická analýza procesů v polymerní elektrolytické membráně palivového článku
    Univerzita Karlova Matematicko-fyzikální fakulta, 2012
    Co-Authors: Pavelka Michal
    Abstract:

    Termodynamická analýza procesů v polymerní elektrolytické membráně palivového článku Michal Pavelka April 12, 2012 Abstract Vodíkové palivové články1 se mohou stát klíčovou technologií 21. století, a proto je důležité umět popsat jejich chování. V této práci se zaměřujeme na vodíkové palivové články s polymerní elektrolytickou membránou. Pro membránu využíváme již existující model2 . Model zasazujeme do teorie směsí, kterou budujeme podobně jako se děje v klasické učebnici od Mazura a de Groota3 a kterou doplňujeme o tak zvané vniřní potenciální energie. Vnitřní potenciální energie nám pak umožňují popsat makroskopické důsledky vnitřních sil mezi vodou a polymerem v membráně a zahrnout tak do modelu membrány vliv gra- dientu povrchového napětí vody v membráně. Model řešíme numericky v 1D aproximaci. Následně určujeme vliv membrány a jednotlivých procesů v ní na účinnost palivového článku. 1 viz. například Larminie, J. and A. Dicks. Fuel Cell Systems Explained. 2nd edition. John Wiley & Sons Ltd., 2003. ISBN 0-470-84857-X. 2 Weber, A. Z. and J. Newman. Transport in Polymer-Electrolyte Membranes I, II, III. J. Electrochem. Soc., 150 (7), A1008-A1015, 2003; 151 (2), A1311-A1325, 2004.; 151 (2), A1326-A1339, 2004 3...Thermodynamic analysis of processes in electrolytic fuel cell membrane Michal Pavelka April 12, 2012 Abstract Hydrogen fuel cells1 may become a key technology of 21st century, and it is important to be able to describe their behavior, therefore. In this work we focus on hydrogen fuel cells with a polymer-electrolyte membrane. For the membrane we adopt an existing model2 . We for- mulate the model in the framework of the mixture theory which we develop similarly as has been done in the classical textbook of Mazur and de Groot3 . However, refining the concept of potential energy of a material point, we introduce new terms called internal potential ener- gies which enable us to describe macroscopic consequences of internal forces between water and polymer in the membrane and to describe the influence of gradient of surface tension of water in the membrane. We solve the model in 1D approximation. Consequently, we calculate the influence processes in the membrane have on efficiency of the fuel cell. 1 see for example Larminie, J. and A. Dicks. Fuel Cell Systems Explained. 2nd edition. John Wiley & Sons Ltd., 2003. ISBN 0-470-84857-X. 2 Weber, A. Z. and J. Newman. Transport in Polymer-Electrolyte Membranes I, II, III. J. Electrochem. Soc., 150 (7), A1008-A1015, 2003; 151 (2), A1311-A1325, 2004.; 151 (2), A1326-A1339,...Mathematical Institute of Charles UniversityMatematický ústav UKFaculty of Mathematics and PhysicsMatematicko-fyzikální fakult

  • Termodynamická analýza procesů v polymerní elektrolytické membráně palivového článku
    2012
    Co-Authors: Pavelka Michal
    Abstract:

    Thermodynamic analysis of processes in electrolytic fuel cell membrane Michal Pavelka April 12, 2012 Abstract Hydrogen fuel cells1 may become a key technology of 21st century, and it is important to be able to describe their behavior, therefore. In this work we focus on hydrogen fuel cells with a polymer-electrolyte membrane. For the membrane we adopt an existing model2 . We for- mulate the model in the framework of the mixture theory which we develop similarly as has been done in the classical textbook of Mazur and de Groot3 . However, refining the concept of potential energy of a material point, we introduce new terms called internal potential ener- gies which enable us to describe macroscopic consequences of internal forces between water and polymer in the membrane and to describe the influence of gradient of surface tension of water in the membrane. We solve the model in 1D approximation. Consequently, we calculate the influence processes in the membrane have on efficiency of the fuel cell. 1 see for example Larminie, J. and A. Dicks. Fuel Cell Systems Explained. 2nd edition. John Wiley & Sons Ltd., 2003. ISBN 0-470-84857-X. 2 Weber, A. Z. and J. Newman. Transport in Polymer-Electrolyte Membranes I, II, III. J. Electrochem. Soc., 150 (7), A1008-A1015, 2003; 151 (2), A1311-A1325, 2004.; 151 (2), A1326-A1339,..