Depósito Digital de Documentos de la UAB Encontrados 6 registros  La búsqueda tardó 0.00 segundos. 
1.
10 p, 912.2 KB Pharmacokinetic analysis of omomyc shows lasting structural integrity and long terminal half-Life in tumor tissue / Beaulieu, Marie-Eve (Peptomyc SL) ; Martínez-Martín, Sandra (Peptomyc SL) ; Kaur, Jastrinjan (Vall d'Hebron Institut d'Oncologia) ; Castillo Cano, Virginia (Peptomyc SL) ; Massó Vallés, Daniel (Peptomyc SL) ; Foradada Felip, Laia (Peptomyc SL) ; López-Estévez, Sergio (Peptomyc SL) ; Serrano del Pozo, Erika (Vall d'Hebron Institut d'Oncologia) ; Thabussot, Hugo (Peptomyc SL) ; Soucek, Laura (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
MYC is an oncoprotein causally involved in the majority of human cancers and a most wanted target for cancer treatment. Omomyc is the best-characterized MYC dominant negative to date. In the last years, it has been developed into a therapeutic miniprotein for solid tumor treatment and recently reached clinical stage. [...]
2023 - 10.3390/cancers15030826
Cancers, Vol. 15, Issue 3 (February 2023) , art. 826  
2.
21 p, 11.5 MB MYC Inhibition Halts Metastatic Breast Cancer Progression by Blocking Growth, Invasion, and Seeding / Massó Vallés, Daniel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Beaulieu, Marie-Eve (Hospital Universitari Vall d'Hebron) ; Jauset González, Toni (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Giuntini, Fabio (Vall d'Hebron Institut d'Oncologia) ; Zacarías-Fluck, Mariano F (Vall d'Hebron Institut d'Oncologia) ; Foradada Felip, Laia (Hospital Universitari Vall d'Hebron) ; Martínez-Martín, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Serrano, Erika (Vall d'Hebron Institut d'Oncologia) ; Martín-Fernández, Génesis (Vall d'Hebron Institut d'Oncologia) ; Casacuberta-Serra, Sílvia (Hospital Universitari Vall d'Hebron) ; Castillo Cano, Virginia (Hospital Universitari Vall d'Hebron) ; Kaur, Jastrinjan (Vall d'Hebron Institut d'Oncologia) ; López-Estévez, Sergio (Hospital Universitari Vall d'Hebron) ; Morcillo, Miguel Ángel (Centro de Investigaciones Energéticas, Medioambientales y Tecnológicas (Espanya)) ; Alzrigat, Mohammad (Karolinska Institutet (Suècia). Department of Microbiology, Tumor and Cell Biology) ; Mahmoud, Loay (Karolinska Institutet (Suècia). Department of Microbiology, Tumor and Cell Biology) ; Luque-García, Antonio (Vall d'Hebron Institut d'Oncologia) ; Escorihuela, Marta (Vall d'Hebron Institut d'Oncologia) ; Guzman, Marta (Vall d'Hebron Institut d'Oncologia) ; Arribas, Joaquín V (Institució Catalana de Recerca i Estudis Avançats) ; Serra, Violeta (Vall d'Hebron Institut d'Oncologia) ; Larsson, Lars-Gunnar (Karolinska Institutet (Suècia). Department of Microbiology, Tumor and Cell Biology) ; Whitfield, Jonathan R. (Vall d'Hebron Institut d'Oncologia) ; Soucek, Laura (Institució Catalana de Recerca i Estudis Avançats)
While MYC role in metastasis has been long controversial, this manuscript demonstrates that MYC inhibition by either transgenic expression or pharmacologic use of the recombinantly produced Omomyc miniprotein exerts antitumor and antimetastatic activity in breast cancer models in vitro and in vivo, suggesting its clinical applicability.
2022 - 10.1158/2767-9764.CRC-21-0103
Cancer Research Communications, Vol. 2 (february 2022) , p. 110-130  
3.
15 p, 1.9 MB The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain / Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Chiti, Fabrizio (Università di Firenze. Dipartimento di Scienze Biochimiche) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: Protein aggregation is linked to the onset of an increasing number of human nonneuropathic (either localized or systemic) and neurodegenerative disorders. In particular, misfolding of native α-helical structures and their self-assembly into nonnative intermolecular β-sheets has been proposed to trigger amyloid fibril formation in Alzheimer's and Parkinson's diseases. [...]
2013 - 10.1371/journal.pone.0058297
PloS one, Vol. 8 issue 3 (2013) , art. e58297  
4.
15 p, 1.8 MB Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain / Marinelli, Patrizia ; Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Amyloid fibril formation is implicated in different human diseases. The transition between native α-helices and nonnative intermolecular β-sheets has been suggested to be a trigger of fibrillation in different conformational diseases. [...]
2013 - 10.3390/ijms140917830
International journal of molecular sciences, Vol. 14 Núm. 9 (August 2013) , p. 17830-17844  
5.
205 p, 4.2 MB Using small globular proteins to study folding stability and aggregation / Castillo Cano, Virginia ; Ventura, Salvador, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular ; Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
El propòsit d'aquesta tesis que porta com a títol "Estudi de l'estabilitat de plegament i l'agregació mitjançant l'ús de proteïnes globulars petites" és el de contribuir al coneixement de com les proteïnes globulars adquireixen la seva estructura nativa i funcional o, alternativament, despleguen i agreguen donant lloc a assemblatges tòxics. [...]
The purpose of the thesis entitled "Using small globular proteins to study folding stability and aggregation" is to contribute to understand how globular proteins fold into their native, functional structures or, alternatively, misfold and aggregate into toxic assemblies. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2013  
6.
16 p, 1.6 MB Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases / Castillo Cano, Virginia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Protein aggregation underlies a wide range of human disorders. The polypeptides involved in these pathologies might be intrinsically unstructured or display a defined 3D-structure. Little is known about how globular proteins aggregate into toxic assemblies under physiological conditions, where they display an initially folded conformation. [...]
2009 - 10.1371/journal.pcbi.1000476
PLOS Computational Biology, Vol. 5, Issue 8 (August 2009) , p. e1000476  

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