About: André Padilla

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) researcher (en) 연구원 (ko) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) 研究者 (zh) հետազոտող (hy)
rdfs:label	André Padilla (en) André Padilla (es) André Padilla (nl) André Padilla (sl) André Padilla (ast)
skos:prefLabel	André Padilla (en) André Padilla (es) André Padilla (nl) André Padilla (sl) André Padilla (ast)
name	André Padilla (en) André Padilla (es) André Padilla (nl) André Padilla (sl) André Padilla (ast)
given name	wds:Q56417154-46DD0B29-426F-4F62-9D04-C4529F3C40B9
given name	André
instance of	wds:Q56417154-E6C8809B-A696-4D42-90EE-BD889DC9FFEA
instance of	Homo sapiens
occupation	wds:Q56417154-56844977-BD71-4BC7-9856-8D5B6F2D2594
employer	wds:Q56417154-20461FBC-86E3-4D23-B4D1-450AA929E489 wds:Q56417154-896775D9-FB51-426B-81B4-A7798A5A5473
sex or gender	wds:Q56417154-CE20E064-8998-44BE-B854-6D6D6CCF28C9
ISNI	wds:Q56417154-1CD24987-82EB-440F-A8D5-3C8F50C63040
VIAF ID	wds:Q56417154-60182A6A-9FD1-44F8-B229-27A98BC2D737
Bibliothèque nationale de France ID	wds:Q56417154-2A6AC7A4-34F6-4E53-9871-FFFD50D39DC4
IdRef ID	wds:Q56417154-F2B4C2B6-B06F-46BA-88A4-CD8580C7ADD1
date of birth	wds:Q56417154-9A57054E-DED5-4F26-AC93-47E7DA1FA715
educated at	wds:Q56417154-C977BBC6-E913-491F-AB8D-780A263DD7D5
family name	wds:Q56417154-6B66BC59-1335-465D-A809-62BBBC1F4E96
VIAF ID	http://viaf.org/viaf/29635442
Bibliothèque nationale de France ID	http://data.bnf.fr/ark:/12148/cb12486764d#about
IdRef ID	http://www.idref.fr/034074635/id
occupation	researcher
employer	Institute of Human Genetics Délégation Languedoc Roussillon
sex or gender	male
ISNI	0000000001809224
VIAF ID	29635442
Bibliothèque nationale de France ID	12486764d
IdRef ID	034074635
date of birth	1957-01-01 00:00:00Z (xsd:dateTime)
educated at	Centre de Biologie Structurale
family name	Padilla
ORCID iD	wds:Q56417154-F87E8053-391C-4356-B071-9BDE4832C401
ORCID iD	https://orcid.org/0000-0001-9702-4612
ORCID iD	0000-0001-9702-4612
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56417154
is author of	Structural and biochemical characterization of the Cop9 signalosome CSN5/CSN6 heterodimer Crystal structure of p14TCL1, an oncogene product involved in T-cell prolymphocytic leukemia, reveals a novel beta-barrel topology Kinetics of interaction between ADP-ribosylation factor-1 (Arf1) and the Sec7 domain of Arno guanine nucleotide exchange factor, modulation by allosteric factors, and the uncompetitive inhibitor brefeldin A. Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein-protein complexes Probing the active site of the deoxynucleotide N-hydrolase Rcl encoded by the rat gene c6orf108. NMR solution structure of Mob1, a mitotic exit network protein and its interaction with an NDR kinase peptide. Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase Crystal structure of the coiled-coil dimerization motif of geminin: structural and functional insights on DNA replication regulation. Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi. HIV-1 Nef protein: purification, crystallizations, and preliminary X-ray diffraction studies. 6-(Hetero)Arylpurine nucleotides as inhibitors of the oncogenic target DNPH1: synthesis, structural studies and cytotoxic activities N (6)-substituted AMPs inhibit mammalian deoxynucleotide N-hydrolase DNPH1 Structure of the oncoprotein Rcl bound to three nucleotide analogues Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5. Crystallization and preliminary X-ray crystallographic analysis of human Geminin coiled-coil domain The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study. Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus. Assignment of 13C resonances and analysis of relaxation properties and internal dynamics of pike parvalbumin by 13C-NMR at natural abundance. Solution conformation of a synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: new structural alignment between the squash inhibitors and the potato carboxypeptidase inhibitor Aedesin: Structure and Antimicrobial Activity against Multidrug Resistant Bacterial Strains Fragment-based identification of a locus in the Sec7 domain of Arno for the design of protein-protein interaction inhibitors Two-dimensional 1H nuclear magnetic resonance study of pike pI 5.0 parvalbumin (Esox lucius). Sequential resonance assignments and folding of the polypeptide chain. Two well-defined motifs in the cAMP-dependent protein kinase inhibitor (PKIalpha) correlate with inhibitory and nuclear export function Correction: N6-Substituted AMPs Inhibit Mammalian Deoxynucleotide N-Hydrolase DNPH1. Kinetics of amide proton exchange in parvalbumin studied by 1H 2-D NMR. A comparison of the calcium and magnesium loaded forms Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins. Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors from <i>Magnaporthe oryzae</i> Resonance assignments and topology of the 15N, 13C labelled 23 kDa core domain of xenopus Mob1 Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics Statistical analysis of double NOE transfer pathways in proteins as measured in 3D NOE-NOE spectroscopy Removing the invariant salt bridge of parvalbumin increases flexibility in the AB-loop structure
is author of	wds:Q27687079-11F460CF-B663-415D-A09A-779FC0238ABC wds:Q45835697-66F116F5-A156-42A1-80EA-DB4A1F0C2C94 wds:Q47342500-42EBDB09-2DFB-466D-9D9A-BF9C184B7B2D wds:Q78649971-2EC99BE4-946C-4787-BB14-BC4E7CE19E10 wds:Q28542494-B4DFDE7E-5EE8-4E1E-9F82-46783BA9FA62 wds:Q112563268-FE825A6E-CF17-4E52-8D5F-852CB11F7E74 wds:Q24301864-1BC66034-04E7-4FE4-BCF2-2DCCDA4EBDD9 wds:Q30176337-4B8338AF-06BB-4B63-BB68-4FC4916337FE

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