Results 71 to 80 of about 234,539 (335)

Novel mutations associated with pyruvate kinase deficiency in Brazil

Hematology, Transfusion and Cell Therapy, 2018
Background: Pyruvate kinase deficiency is a hereditary disease that affects the glycolytic pathway of the red blood cell, causing nonspherocytic hemolytic anemia.
Maria Carolina Costa Melo Svidnicki, Andrey Santos, Jhonathan Angel Araujo Fernandez, Ana Paula Hitomi Yokoyama, Isis Quezado Magalhães, Vitoria Regia Pereira Pinheiro, Silvia Regina Brandalise, Paulo Augusto Achucarro Silveira, Fernando Ferreira Costa, Sara Teresinha Olalla Saad   +9 more
doaj   +1 more source

Pyruvate Kinase M2 Protects Heart from Pressure Overload‐Induced Heart Failure by Phosphorylating RAC1

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2022
Background Heart failure, caused by sustained pressure overload, remains a major public health problem. PKM (pyruvate kinase M) acts as a rate‐limiting enzyme of glycolysis. PKM2 (pyruvate kinase M2), an alternative splicing product of PKM, plays complex
Le Ni, Bowen Lin, Lingjie Hu, Ruoyu Zhang, Fengmei Fu, Meiting Shen, Jian Yang, Dan Shi   +7 more
doaj   +1 more source

A fluorometric method for the assay of protein kinase activity [PDF]

, 2018
Protein kinases constitute one of the largest protein families in nature. Current methods to assay their activity involve the use of radioactive ATP or very expensive reagents.
Figueroa, Carlos Maria, Iglesias, Alberto Alvaro, Rojas, Bruno Ezequiel, Santin, Franco, Ulloa, Rita Maria   +4 more
core   +1 more source

Establishment and optimization of the two‐step induction system for generating primordial germ cell‐like cells from chicken embryonic stem cells

FEBS Open Bio, EarlyView.
This study optimizes a two‐step induction system to generate PGCLCs from chicken ESCs. The induced cells express germline markers and migrate to gonads in ovo, offering a novel approach for avian genetic resource conservation. Primordial germ cells (PGCs) are the progenitor cells of sperm and eggs.
Zeyu Li, XianShuai Xu, GuangZheng Liu, XiaoQian Lv, JiuZhou Song, HongYan Sun, YingJie Niu, QiSheng Zuo, Wei Han, BiChun Li, Kai Jin   +10 more
wiley   +1 more source

A simple and reliable method for determination of optimum pH in coupled enzyme assays

BioTechniques, 2020
Determination of the optimum pH in a coupled enzyme assay poses significant challenges because altering the pH of the reaction mixture can affect the performance of both enzymes.
Lee Bowman, Rachael Motamed, Paul Lee, Kadijah Aleem, Astha S Berawala, Katherine L Hayden, David J Bzik, Debasish Chattopadhyay   +7 more
doaj   +1 more source

Stable isotope metabolomics of pulmonary artery smooth muscle and endothelial cells in pulmonary hypertension and with TGF-beta treatment. [PDF]

, 2020
Altered metabolism in pulmonary artery smooth muscle cells (PASMCs) and endothelial cells (PAECs) contributes to the pathology of pulmonary hypertension (PH), but changes in substrate uptake and how substrates are utilized have not been fully ...
D' Alessandro, Angelo, Freeman, Scott, Graham, Brian B, Gu, Sue, Hernandez-Saavedra, Daniel, Kassa, Biruk, Kumar, Rahul, Lee, Michael H, Mickael, Claudia, Reisz, Julie A, Sanders, Linda, Stenmark, Kurt R, Tuder, Rubin M   +12 more
core   +1 more source

Metabolism within the tumor microenvironment and its implication on cancer progression: an ongoing therapeutic target [PDF]

, 2018
Since reprogramming energy metabolism is considered a new hallmark of cancer, tumor metabolism is again in the spotlight of cancer research. Many studies have been carried out and many possible therapies have been developed in the last years.
Abdel-Aziz, Ahmadzadeh, Al-Zhoughbi, Albina, Alkan, Allard, Allen, Altman, Alves-Filho, Amelio, Araújo, Argilés, Arora, Arts, Aslanian, Astaldi, Attieh, Augsten, Auvinen, Babbar, Baker, Balasubramanian, Baltazar, Bauer, Bello-Fernandez, Beloribi-Djefaflia, Berchner-Pfannschmidt, Berge, Berrone, Birendra, Bloch-Frankenthal, Bock, Bock, Bonuccelli, Boros, Boudreau, Boukalova, Britten, Brooks, Broome, Bueno, Buqué, Burnet, Cadamuro, Cahlin, Cantelmo, Cao, Carito, Carmeliet, Carmeliet, Caro, Carrascosa, Casazza, Caspani, Catane, Cavalcante, Chakravarty, Chakravarty, Chakravarty, Chang, Chang, Chang, Chappell, Chaudhary, Chen, Chen, Chen, Chiarini, Chittezhath, Choi, Choi, Clark, Clem, Clem, Cohen, Colegio, Collins, Commisso, Covarrubias, Covarrubias, Dang, Dang, Das, Dasgupta, Daurkin, DeBerardinis, DeBerardinis, Delgoffe, Delgoffe, Dell’ Antone, Desai, DiNapoli, Dirat, Dobrina, Doherty, Dong, Draoui, Dufour, Eason, Eelen, El Sayed, Elia, Elwood, Eminel, Fallarino, Farabegoli, Farber, Feun, Fields, Figueras, Filipp, Fischer, Flaig, Flint, Floor, Floridi, Folkman, Folkman, Franklin, Gacche, Ganeshan, Garber, García-Caballero, García-Faroldi, García-Faroldi, Gatenby, Gazi, Geiger, Gentric, Gerner, Gershtein, Ghashghaeinia, Gonen, Goveia, Granchi, Grieninger, Grivennikov, Gross, Gunnink, Guo, Guo, Guppy, Guth, Halestrap, Han, Hanahan, Hanahan, Hanai, Harjes, Harjes, Haskell, Hatzivassiliou, Hayakawa, Hessini, Hitosugi, Ho, Ho, Hoff, Holm, Hosono, Huang, Hubler, Hui, Häusler, Hée, Ignatenko, Ioannesyants, Ip, Jiménez-Valerio, Jiménez-Valerio, Jochems, Johansen, Jones, Kabat, Kafkewitz, Kamphorst, Kamphorst, Kamphorst, Kannan, Karpel-Massler, Katt, Kawasaki, Kelly, Kim, Klimp, Ko, Koliaraki, Kouidhi, Koukourakis, Kridel, Krishna, Kroemer, Krützfeldt, Kubatka, Kucharzewska, la Cueva, Labow, Laing, Lampropoulou, Le, Lechowski, Lee, Lee, Leek, Leighton, Leopold, LePage, Lerma Barbaro, Li, Lin, Liu, Liu, Liu, Liu, Liu, Liu, Liu, Lopes-Coelho, Lu, Lucca, Lukey, Lunt, Luo, López-Lázaro, Löb, Ma, Madaan, Maity, Marchiq, Martinez-Outschoorn, Martinez-Outschoorn, Maráz, Mashima, Masri, Matusewicz, McCann, McKee, McLaughlin, Medina, Medina, Merchan, Meyer, Mider, Missiaen, Mitra, Mockler, Moreno-Sánchez, Morrison, Mu, Murray-Stewart, Márquez, Márquez, Nacev, Nancolas, Newsholme, Nieman, Nisoli, Noman, Norrby, Noy, Nurjhan, Nyberg, Ocaña, Ohmura, Oka, Opitz, Orimo, Pallangyo, Palm, Panda, Papandreou, Parra-Bonilla, Parry, Pascual, Pasquier, Patsoukis, Pavlides, Pavlova, Pelicano, Pellerin, Pennisi, Penny, Peters, Pisarsky, Pizer, Polanski, Polet, Pollard, Polyak, Possemato, Potente, Potente, Prager, Prager, Pushkina, Pérez-Escuredo, Quatromoni, Quesada, Quesada, Rabold, Ramjiawan, Rashid, Rattigan, Reihill, Reitzer, Ribatti, Ribatti, Ribeiro, Richard, Rider, Roberts, Rodríguez-González, Rodríguez-Prados, Rohle, Romero, Romero-García, Roy, Roy, Ruan, Ruiz-Pérez, Russell, Ryu, Saez, Salimian Rizi, Salimian Rizi, Samal, Samudio, Santos, Sanuphan, Sasaki, Saulnier Sholler, Scherz-Shouval, Schoors, Schulze, Segura, Sekar, Selak, Seltzer, Serafini, Shapot, Shapot, Shapot, Sharkia, Shime, Shin, Shurbaji, Sieber, Siu, Skelton, Song, Sonveaux, Sonveaux, Souba, Sousa, Spahr, Spinelli, Spolarics, Stacpoole, Stern, Stuart, Stumvoll, Su, Sukumar, Sánchez-López, Tachibana, Takigawa, Talekar, Tanese, Tang, Tannahill, Tebbe, Thomas, Thomas, Thornburg, Tisdale, Torosian, Torres, Trudeau, Ullah, Uray, Urdiales, Vander Heiden, Vander Heiden, Varricchi, Vasudevan, Velaei, Vera, Vornovitskaya, Végran, Wagner, Wakil, Wang, Wang, Wang, Wang, Warburg, Warburg, Wen, Whitaker-Menezes, Williams-Ashman, Wilson, Wood, Woodward, Woster, Wu, Wu, Xie, Yamanishi, Yang, Yang, Yau, Yen, Yoshida, Yoshizaki, Yu, Yuan, Yuan, Yuan, Yun, Zabala-Letona, Zahalka, Zhan, Zhang, Zhang, Zhang, Zhang, Zhang, Zhao, Zheng, Zhou, Zhu, Ziegler   +431 more
core   +2 more sources

Short‐term actions of epigalocatechin‐3‐gallate in the liver: a mechanistic insight into hypoglycemic and potential toxic effects

FEBS Open Bio, EarlyView.
Epigallocatechin‐3‐gallate (EGCG) acutely inhibited gluconeogenesis and enhanced glycolysis, glycogenolysis, and fatty acid oxidation in perfused rat livers. Mechanistic assays revealed mitochondrial uncoupling, inhibition of pyruvate carboxylation and glucose‐6‐phosphatase, shift of NADH/NAD+ ratios toward oxidation, and loss of membrane integrity ...
Carla Indianara Bonetti, Bruna Lopes Correia, Francielle Cristina Nakamura Manicardi, Nairana Mithieli de Queiroz Eskuarek Melo, Vanesa de Oliveira Pateis, Jurandir Fernando Comar, Anacharis Babeto de Sá‐Nakanishi, Adelar Bracht, Lívia Bracht   +8 more
wiley   +1 more source

Pyruvate kinase M2 at a glance [PDF]

Journal of Cell Science, 2015
Reprogrammed metabolism is a key feature of cancer cells. The pyruvate kinase M2 (PKM2) isoform, which is commonly upregulated in many human cancers, has been recently shown to play a crucial role in metabolism reprogramming, gene transcription and cell cycle progression.
Weiwei Yang, Zhimin Lu, Zhimin Lu
openaire   +3 more sources

Mitochondria‐associated membranes (MAMs): molecular organization, cellular functions, and their role in health and disease

FEBS Open Bio, EarlyView.
Mitochondria‐associated membranes (MAMs) are contact sites between the endoplasmic reticulum and mitochondria that regulate calcium signaling, lipid metabolism, autophagy, and stress responses. This review outlines their molecular organization, roles in cellular homeostasis, and how dysfunction drives neurodegeneration, metabolic disease, cancer, and ...
Viet Bui, Maryline Santerre, Natalia Shcherbik, Bassel E Sawaya   +3 more
wiley   +1 more source