Výsledky vyhledávání - "Marco Verzini"

The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments

Autor: Anna Lisa Agneletti, Rosario Donato, Ileana Giambanco, Marco Verzini, Guglielmo Sorci, Roberta Bianchi, Marisa Garbuglia

Publikováno v: Brazilian Journal of Medical and Biological Research v.32 n.10 1999
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
Scopus-Elsevier
Brazilian Journal of Medical and Biological Research, Volume: 32, Issue: 10, Pages: 1177-1185, Published: OCT 1999
Brazilian Journal of Medical and Biological Research, Vol 32, Iss 10, Pp 1177-1185 (1999)

The Ca2+-modulated, dimeric proteins of the EF-hand (helix-loop-helix) type, S100A1 and S100B, that have been shown to inhibit microtubule (MT) protein assembly and to promote MT disassembly, interact with the type III intermediate filament (IF) subu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5c5b391d3c32e6586729362c0483303
https://doi.org/10.1590/s0100-879x1999001000001

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Characterization of type III intermediate filament regulatory protein target epitopes: S-100 (β and/or α) binds the N-terminal head domain; annexin II2-p112 binds the rod domain

Autor: Marisa Garbuglia, Rosario Donato, Gordon A. Jamieson, Ruth V.W. Dimlich, Marco Verzini

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1313(3):268-276

We have investigated the interaction of S-100 proteins (beta and/or alpha) and annexin II2-p11(2) with glial fibrillary acidic protein (GFAP) and desmin to have further information on the mechanisms whereby S-100 proteins and annexin II2-p11(2) affec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f6ad03c65fb93a2df227eefc7c14b0b

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S-100 Protein and Annexin II2-p112 (Calpactin I) Act in Concert to Regulate the State of Assembly of GFAP Intermediate Filaments in Vitro

Autor: Rosario Donato, Ileana Giambanco, Marco Verzini, Roberta Bianchi, Marisa Garbuglia, Antonio Spreca

Publikováno v: Biochemical and Biophysical Research Communications. 208:910-918

S-100 protein and annexin II 2 -p11 2 were reported to inhibit and to stimulate the assembly of glial fibrillary acidic protein (GFAP), respectively, in a Ca 2+ -dependent manner. Here we show by a number of experimental approaches that S-100 protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89aa24c445ad05f70ddc041f24bbb524
https://doi.org/10.1006/bbrc.1995.1421

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Mechanism of S100 protein-dependent inhibition of glial fibrillary acidic protein (GFAP) polymerization

Autor: Marisa Garbuglia, Rosario Donato, Marco Verzini, Ileana Giambanco, Roberta Bianchi

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1223:354-360

S100 protein, a subfamily of Ca 2+ -binding proteins of the EF-hand type, was recently shown to bind to and to inhibit the polymerization of the glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, in the p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6d56295c8c8bbc61fa4fad8d344d73f
https://doi.org/10.1016/0167-4889(94)90095-7

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Calpactin I binds to the glial fibrillary acidic protein (GFAP) and cosediments with glial filaments in a Ca2+-dependent manner: Implications for concerted regulatory effects of calpactin I and S100 protein on glial filaments

Autor: Marco Verzini, Marisa Garbuglia, Rosario Donato, Ileana Giambanco, Roberta Bianchi

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1223:361-367

Calpactin I, a heterotetrameric, cytoskeletal protein complex composed of two copies of annexin II cross-linked by two copies of p11, an S100-like protein, binds to the glial fibrillary acidic protein (GFAP) and cosediments with glial filaments (GF)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bca0829396a4c8d1db675a86dd8ea671
https://doi.org/10.1016/0167-4889(94)90096-5

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Annexin V and Annexin VI in Rat Tissues during Postnatal Development: Immunochemical Measurements

Autor: Rosario Donato, Marco Verzini, Ileana Giambanco

Publikováno v: Biochemical and Biophysical Research Communications. 196:1221-1226

Annexins V and VI, two Ca2+-dependent phopsholipid- and membrane-binding proteins, were immunochemically measured in a number of rat organs and tissues during post-natal development. Annexin V proved much more abundant than annexin VI irrespective of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::74c075e338df361ac865b71c7a5250ee
https://doi.org/10.1006/bbrc.1993.2382

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S100A1 and S100B interactions with annexins

Autor: Marisa Garbuglia, Rosario Donato, Andreas Hofmann, Marco Verzini, Robert Huber

Publikováno v: Biochimica et biophysica acta. 1498(2-3)

Members of the annexin protein family interact with members of the S100 protein family thereby forming heterotetramers in which an S100 homodimer crossbridges two copies of the pertinent annexin. Previous work has shown that S100A1 and S100B bind ann

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df698e11c16ec9f11493b903e92302b3
https://pubmed.ncbi.nlm.nih.gov/11108963

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Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization

Autor: David J. Weber, Rosario Donato, Volker Gerke, Dirk Osterloh, Richard R. Rustandi, Marisa Garbuglia, Marco Verzini

Publikováno v: Biochemical and biophysical research communications. 254(1)

Whereas native and recombinant S100A1 inhibited GFAP assembly, a truncated S100A1 lacking the last six C-terminal residues (Phe88-Ser93) (S100A1Delta88-93) proved unable to do so. The inhibitory effects of native and recombinant S100A1 on GFAP assemb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67666c253bc45913e5317050fc7c43e9
https://pubmed.ncbi.nlm.nih.gov/9920729

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Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments

Autor: Marco Verzini, Marisa Garbuglia, Rosario Donato

Annexin VI, a member of a family of Ca(2+)-dependent phospholipid- and membrane-binding proteins, interacts with the Ca(2+)-regulated EF-hand proteins, S100A1 and S100B, and blocks the ability of these two proteins to inhibit the assembly of desmin a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d49ac973e2bd3201d38a07a107040fd
http://hdl.handle.net/11391/102854

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Annexin II2-p11(2) (calpactin I) stimulates the assembly of GFAP in a calcium- and pH-dependent manner

Autor: Rosario Donato, Marisa Garbuglia, Ileana Giambanco, Marco Verzini, Roberta Bianchi

Publikováno v: Biochemical and biophysical research communications. 208(3)

Annexin II 2 -p11 2 (calpactin I) was tested as a potential regulator of GFAP assembly into glial filaments (GF), following the observation that it interacts with GFAP and cosediments with GF in a sedimentation assay. Under conditions where GFAP asse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a298c1336f553f432579bd44e7b136b2
https://pubmed.ncbi.nlm.nih.gov/7702619

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