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1.
Res Sq ; 2024 Apr 03.
Article in English | MEDLINE | ID: mdl-38645031

ABSTRACT

The intricate protein-chaperone network is vital for cellular function. Recent discoveries have unveiled the existence of specialized chaperone complexes called epichaperomes, protein assemblies orchestrating the reconfiguration of protein-protein interaction networks, enhancing cellular adaptability and proliferation. This study delves into the structural and regulatory aspects of epichaperomes, with a particular emphasis on the significance of post-translational modifications in shaping their formation and function. A central finding of this investigation is the identification of specific PTMs on HSP90, particularly at residues Ser226 and Ser255 situated within an intrinsically disordered region, as critical determinants in epichaperome assembly. Our data demonstrate that the phosphorylation of these serine residues enhances HSP90's interaction with other chaperones and co-chaperones, creating a microenvironment conducive to epichaperome formation. Furthermore, this study establishes a direct link between epichaperome function and cellular physiology, especially in contexts where robust proliferation and adaptive behavior are essential, such as cancer and stem cell maintenance. These findings not only provide mechanistic insights but also hold promise for the development of novel therapeutic strategies targeting chaperone complexes in diseases characterized by epichaperome dysregulation, bridging the gap between fundamental research and precision medicine.

2.
Environ Sci Technol ; 58(10): 4594-4605, 2024 Mar 12.
Article in English | MEDLINE | ID: mdl-38408303

ABSTRACT

Aerosol acts as ice-nucleating particles (INPs) by catalyzing the formation of ice crystals in clouds at temperatures above the homogeneous nucleation threshold (-38 °C). In this study, we show that the immersion mode ice nucleation efficiency of the environmentally relevant protein, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), occurs at temperatures between -6.8 and -31.6 °C. Further, we suggest that this range is controlled by the RuBisCO concentration and protein aggregation. The warmest median nucleation temperature (-7.9 ± 0.8 °C) was associated with the highest concentration of RuBisCO (2 × 10-1 mg mL-1) and large aggregates with a hydrodynamic diameter of ∼103 nm. We investigated four additional chemically and structurally diverse proteins, plus the tripeptide glutathione, and found that each of them was a less effective INP than RuBisCO. Ice nucleation efficiency of the proteins was independent of the size (molecular weight) for the five proteins investigated in this study. In contrast to previous work, increasing the concentration and degree of aggregation did not universally increase ice nucleation efficiency. RuBisCO was the exception to this generalization, although the underlying molecular mechanism determining why aggregated RuBisCO is such an effective INP remains elusive.


Subject(s)
Ice , Ribulose-Bisphosphate Carboxylase , Freezing , Temperature
3.
Nagy‐Reis, Mariana B.; Oshima, Júlia Emi de Faria; Kanda, Claudia Zukeran; Palmeira, Francesca Belem Lopes; Melo, Fabiano Rodrigues de; Morato, Ronaldo Gonçalves; Bonjorne, Lilian; Magioli, Marcelo; Leuchtenberger, Caroline; Rohe, Fabio; Lemos, Frederico Gemesio; Martello, Felipe; Alves‐Eigenheer, Milene; Silva, Rafaela Aparecida da; Santos, Juliana Silveira dos; Priante, Camila Fátima; Bernardo, Rodrigo; Rogeri, Patricia; Assis, Julia Camara; Gaspar, Lucas Pacciullio; Tonetti, Vinicius Rodrigues; Trinca, Cristiano Trapé; Ribeiro, Adauto de Souza; Bocchiglieri, Adriana; Hass, Adriani; Canteri, Adriano; Chiarello, Adriano Garcia; Paglia, Adriano Pereira; Pereira, Adriele Aparecida; Souza, Agnis Cristiane de; Gatica, Ailin; Medeiro, Akyllam Zoppi; Eriksson, Alan; Costa, Alan Nilo; González‐Gallina, Alberto; Yanosky, Alberto A; Cruz, Alejandro Jesus de la; Bertassoni, Alessandra; Bager, Alex; Bovo, Alex Augusto Abreu; Mol, Alexandra Cravino; Bezerra, Alexandra Maria Ramos; Percequillo, Alexandre; Vogliotti, Alexandre; Lopes, Alexandre Martins Costa; Keuroghlian, Alexine; Hartley, Alfonso Christopher Zúñiga; Devlin, Allison L.; Paula, Almir de; García‐Olaechea, Alvaro; Sánchez, Amadeo; Aquino, Ana Carla Medeiros Morato; Srbek‐Araujo, Ana Carolina; Ochoa, Ana Cecilia; Tomazzoni, Ana Cristina; Lacerda, Ana Cristyna Reis; Bacellar, Ana Elisa de Faria; Campelo, Ana Kellen Nogueira; Victoria, Ana María Herrera; Paschoal, Ana Maria de Oliveira; Potrich, Ana Paula; Gomes, Ana Paula Nascimento; Olímpio, Ana Priscila Medeiros; Costa, Ana Raissa Cunha; Jácomo, Anah Tereza de Almeida; Calaça, Analice Maria; Jesus, Anamélia Souza; Barban, Ananda de Barros; Feijó, Anderson; Pagoto, Anderson; Rolim, Anderson Claudino; Hermann, Andiara Paula; Souza, Andiara Silos Moraes de Castro e; Alonso, André Chein; Monteiro, André; Mendonça, André Faria; Luza, André Luís; Moura, André Luis Botelho; Silva, André Luiz Ferreira da; Lanna, Andre Monnerat; Antunes, Andre Pinassi; Nunes, André Valle; Dechner, Andrea; Carvalho, Andrea Siqueira; Novaro, Andres Jose; Scabin, Andressa Barbara; Gatti, Andressa; Nobre, Andrezza Bellotto; Montanarin, Anelise; Deffaci, Ângela Camila; Albuquerque, Anna Carolina Figueiredo de; Mangione, Antonio Marcelo; Pinto, Antonio Millas Silva; Pontes, Antonio Rossano Mendes; Bertoldi, Ariane Teixeira; Calouro, Armando Muniz; Fernandes, Arthur; Ferreira, Arystene Nicodemo; Ferreguetti, Atilla Colombo; Rosa, Augusto Lisboa Martins; Banhos, Aureo; Francisco, Beatriz da Silva de Souza; Cezila, Beatriz Azevedo; Beisiegel, Beatriz de Mello; Thoisy, Benoit de; Ingberman, Bianca; Neves, Bianca dos Santos; Pereira‐Silva, Brenda; Camargo, Bruna Bertagni de; Andrade, Bruna da Silva; Santos, Bruna Silva; Leles, Bruno; Campos, Bruno Augusto Torres Parahyba; Kubiak, Bruno Busnello; França, Bruno Rodrigo de Albuquerque; Saranholi, Bruno Henrique; Mendes, Calebe Pereira; Devids, Camila Cantagallo; Pianca, Camila; Rodrigues, Camila; Islas, Camila Alvez; Lima, Camilla Angélica de; Lima, Camilo Ribeiro de; Gestich, Carla Cristina; Tedesco, Carla Denise; Angelo, Carlos De; Fonseca, Carlos; Hass, Carlos; Peres, Carlos A.; Kasper, Carlos Benhur; Durigan, Carlos Cesar; Fragoso, Carlos Eduardo; Verona, Carlos Eduardo; Rocha, Carlos Frederico Duarte; Salvador, Carlos Henrique; Vieira, Carlos Leonardo; Ruiz, Carmen Elena Barragán; Cheida, Carolina Carvalho; Sartor, Caroline Charão; Espinosa, Caroline da Costa; Fieker, Carolline Zatta; Braga, Caryne; Sánchez‐Lalinde, Catalina; Machado, Cauanne Iglesias Campos; Cronemberger, Cecilia; Luna, Cecília Licarião; Vechio, Christine Del; Bernardo, Christine Steiner S.; Hurtado, Cindy Meliza; Lopes, Cíntia M.; Rosa, Clarissa Alves da; Cinta, Claudia Cristina; Costa, Claudia Guimaraes; Zárate‐Castañeda, Claudia Paola; Novaes, Claudio Leite; Jenkins, Clinton N.; Seixas, Cristiana Simão; Martin, Cristiane; Zaniratto, Cristiane Patrícia; López‐Fuerte, Cristina Fabiola; Cunha, Cristina Jaques da; Brito De‐Carvalho, Crizanto; Chávez, Cuauhtémoc; Santos, Cyntia Cavalcante; Polli, Daiana Jeronimo; Buscariol, Daiane; Carreira, Daiane Cristina; Galiano, Daniel; Thornton, Daniel; Ferraz, Daniel da Silva; Lamattina, Daniela; Moreno, Daniele Janina; Moreira, Danielle Oliveira; Farias, Danilo Augusto; Barros‐Battesti, Darci Moraes; Tavares, Davi Castro; Braga, David Costa; Gaspar, Denise Alemar; Friedeberg, Diana; Astúa, Diego; Silva, Diego Afonso; Viana, Diego Carvalho; Lizcano, Diego J.; Varela, Diego M.; Jacinavicius, Fernando de Castro; Andrade, Gabrielle Ribeiro de; Almeida, Maria Cristina Ferreira do Rosário; Onofrio, Valeria Castilho.
Ecology, v. 101, n. 11, e03128, nov. 2020
Article in English | Sec. Est. Saúde SP, SESSP-IBPROD, Sec. Est. Saúde SP | ID: bud-3174

ABSTRACT

Mammalian carnivores are considered a key group in maintaining ecological health and can indicate potential ecological integrity in landscapes where they occur. Carnivores also hold high conservation value and their habitat requirements can guide management and conservation plans. The order Carnivora has 84 species from 8 families in the Neotropical region: Canidae; Felidae; Mephitidae; Mustelidae; Otariidae; Phocidae; Procyonidae; and Ursidae. Herein, we include published and unpublished data on native terrestrial Neotropical carnivores (Canidae; Felidae; Mephitidae; Mustelidae; Procyonidae; and Ursidae). NEOTROPICAL CARNIVORES is a publicly available data set that includes 99,605 data entries from 35,511 unique georeferenced coordinates. Detection/non‐detection and quantitative data were obtained from 1818 to 2018 by researchers, governmental agencies, non‐governmental organizations, and private consultants. Data were collected using several methods including camera trapping, museum collections, roadkill, line transect, and opportunistic records. Literature (peerreviewed and grey literature) from Portuguese, Spanish and English were incorporated in this compilation. Most of the data set consists of detection data entries (n = 79,343; 79.7%) but also includes non‐detection data (n = 20,262; 20.3%). Of those, 43.3% also include count data (n = 43,151). The information available in NEOTROPICAL CARNIVORES will contribute to macroecological, ecological, and conservation questions in multiple spatio‐temporal perspectives. As carnivores play key roles in trophic interactions, a better understanding of their distribution and habitat requirements are essential to establish conservation management plans and safeguard the future ecological health of Neotropical ecosystems. Our data paper, combined with other largescale data sets, has great potential to clarify species distribution and related ecological processes within the Neotropics. There are no copyright restrictions and no restriction for using data from this data paper, as long as the data paper is cited as the source of the information used. We also request that users inform us of how they intend to use the data.

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