Výsledky vyhledávání - "Mauricio P Sica"

Akademický článek

Protein-protein interactions in crystals of the human receptor-type protein tyrosine phosphatase ICA512 ectodomain.

Autor: María E Primo, Jean Jakoncic, Martín E Noguera, Valeria A Risso, Laura Sosa, Mauricio P Sica, Michele Solimena, Edgardo Poskus, Mario R Ermácora

Publikováno v: PLoS ONE, Vol 6, Iss 9, p e24191 (2011)

ICA512 (or IA-2) is a transmembrane protein-tyrosine phosphatase located in secretory granules of neuroendocrine cells. Initially, it was identified as one of the main antigens of autoimmune diabetes. Later, it was found that during insulin secretion

Externí odkaz: https://doaj.org/article/3ffe97e4e932437994247768ba03fcd4

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Akademický článek

Protocol to study the oligomeric organization of single-span transmembrane peptides using molecular dynamics simulations

Autor: Mauricio P. Sica, Micaela V. Kortsarz, Angelines A. Morillas, Cristian R. Smulski

Publikováno v: STAR Protocols, Vol 3, Iss 3, Pp 101636- (2022)

Summary: Herein, you will find detailed information for the preparation of a coarse-grained array of peptides embedded in a lipid membrane. It contains all the steps to set up and run a molecular dynamic simulation using a coarse-grained approach. We

Externí odkaz: https://doaj.org/article/d62e154fa2884475bc7b3b7f41da6b0b

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Akademický článek

Coarse Grained Molecular Dynamic Simulations for the Study of TNF Receptor Family Members' Transmembrane Organization

Autor: Mauricio P. Sica, Cristian R. Smulski

Publikováno v: Frontiers in Cell and Developmental Biology, Vol 8 (2021)

The Tumor Necrosis Factor (TNF) and the TNF receptor (TNFR) superfamilies are composed of 19 ligands and 30 receptors, respectively. The oligomeric properties of ligands, both membrane bound and soluble, has been studied most. However, less is known

Externí odkaz: https://doaj.org/article/9decc9626a4b4f02890ac0e89071a9e0

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Differential trafficking of ligands trogocytosed via CD28 versus CTLA4 promotes collective cellular control of co-stimulation

Autor: Simon Zenke, Mauricio P. Sica, Florian Steinberg, Julia Braun, Alicia Zink, Alina Gavrilov, Alexander Hilger, Aditya Arra, Monika Brunner-Weinzierl, Roland Elling, Niklas Beyersdorf, Tim Lämmermann, Cristian R. Smulski, Jan C. Rohr

Publikováno v: Nature Communications

Intercellular communication is crucial for collective regulation of cellular behaviors. While clustering T cells have been shown to mutually control the production of key communication signals, it is unclear whether they also jointly regulate their a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33b0543764ca6eda93e9171a26dba251
https://pubmed.ncbi.nlm.nih.gov/36309492

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Ligand-independent oligomerization of TACI is controlled by the transmembrane domain and regulates proliferation of activated B cells

Autor: Cristian R. Smulski, Luyao Zhang, Malte Burek, Ariadna Teixidó Rubio, Jana-Susann Briem, Mauricio P. Sica, Eirini Sevdali, Michele Vigolo, Laure Willen, Patricia Odermatt, Duygu Istanbullu, Stephanie Herr, Marco Cavallari, Henry Hess, Marta Rizzi, Hermann Eibel, Pascal Schneider

Publikováno v: Cell reports, vol. 38, no. 13, pp. 110583

In mature B cells, TACI controls class-switch recombination and differentiation into plasma cells during T cell-independent antibody responses. TACI binds the ligands BAFF and APRIL. Approximately 10% of patients with common variable immunodeficiency

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2645ba5913a8d25cf852dcd7f715418
https://pubmed.ncbi.nlm.nih.gov/35354034

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Modulation of Plasma Membrane Ca2+-ATPase by Neutral Phospholipids

Autor: F. Luis González-Flecha, Irene C. Mangialavori, Juan Pablo F.C. Rossi, Mauricio P. Sica, María Florencia Pignataro, Martin M. Dodes-Traian

Publikováno v: Journal of Biological Chemistry. 290:6179-6190

The effects of lipids on membrane proteins are likely to be complex and unique for each membrane protein. Here we studied different detergent/phosphatidylcholine reconstitution media and tested their effects on plasma membrane Ca2+ pump (PMCA). We fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::49791d204f80a432c1d138dc506bea16
https://doi.org/10.1074/jbc.m114.585828

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Recognition between a short unstructured peptide and a partially folded fragment leads to the thioredoxin fold sharing native-like dynamics

Autor: Mauricio P. Sica, Javier Santos, Andres Binolfi, José M. Delfino, Claudio O. Fernández

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 80:1448-1464

Thioredoxins (TRXs) constitute attractive α/β scaffolds for investigating molecular recognition. The interaction between the recombinant fragment spanning the sequence 1–93 of full-length TRX (TRX1-93) and the synthetic peptide comprising residue

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::87eae0bf7dc8fd9d653e73090344cf7a
https://doi.org/10.1002/prot.24043

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Frequency Of Pancreatic Beta-Cell Autoimmunity Markers In Patients With Autoimmune Thyroid Disease Frecuencia de marcadores de autoinmunidad beta pancreática en pacientes con enfermedad tiroidea autoinmune

Autor: María E. Primo, Hugo Niepomniszcze, Edgardo Poskus, Mónica S. Sala, Silvia S. Guaita, Mauricio P. Sica, Anabel Villalba, Alejandro Cardoso, Oscar D. Bruno

Publikováno v: Medicina (Buenos Aires), Vol 68, Iss 1, Pp 37-42 (2008)

A total of 305 ambulatory patients recruited at the Division of Endocrinology, Hospital de Clínicas, University of Buenos Aires, with autoimmune thyroid disease (AITD) were studied to search for associations between autoimmune thyroid disease and pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doajarticles::0fdff81f6b03989c6b3874ea6f159046
http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0025-76802008000100006

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Effects of Serine-to-Cysteine Mutations on β-Lactamase Folding

Autor: Valeria A. Risso, Mario R. Ermácora, Javier Santos, Mauricio P. Sica

Publikováno v: Biophysical Journal. 93(5):1707-1718

B. licheniformis exo-small β-lactamase (ESBL) has two nonsequential domains and a complex architecture. We replaced ESBL serine residues 126 and 265 with cysteine to probe the conformation of buried regions in each domain. Spectroscopic, hydrodynami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c093a0109273e3117973cb914ae56015

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