About: Laura Cendron

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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	forskare (sv) ikertzailea (eu) researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) chercheuse (fr) investigadora (es) ഗവേഷക (ml) araştırmacı (tr) wetenschapper (nl) дослідниця (uk) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) researcher (en-ca) researcher (en-gb) researcher (en-us) hulumtuese (sq) investigadora (ca) investigadora (gl) investigadora (pt) investigadora (ast) ricercatrice italiana (1977-) (it)
rdfs:label	Laura Cendron (en) Laura Cendron (es) Laura Cendron (fr) Laura Cendron (it) Laura Cendron (nl) Laura Cendron (sl) Laura Cendron (ast)
skos:prefLabel	Laura Cendron (en) Laura Cendron (es) Laura Cendron (fr) Laura Cendron (it) Laura Cendron (nl) Laura Cendron (sl) Laura Cendron (ast)
name	Laura Cendron (en) Laura Cendron (es) Laura Cendron (fr) Laura Cendron (it) Laura Cendron (nl) Laura Cendron (sl) Laura Cendron (ast)
Scopus author ID	wds:Q28324177-1D2FED2A-4357-45E4-BC9E-D5751C4777B5
Scopus author ID	21741997900
given name	wds:Q28324177-BBB995E2-2213-487D-8181-00759D97BBCF
given name	Laura
instance of	wds:Q28324177-570648AB-7905-4D9F-8B01-EACD5D0F2536
instance of	Homo sapiens
occupation	wds:Q28324177-E8373B5E-E712-490F-9D3B-8A4A07D1EFE9
employer	wds:Q28324177-43CD6CE1-9B87-480B-9DEB-45915C2F3DCB
CONOR.SI ID	wds:Q28324177-4C952A87-43AB-49C7-8569-5F86F03ADAC4
NSK ID	wds:q28324177-fcf2de2c-4e70-d855-e1f2-f8ff77069412
sex or gender	wds:Q28324177-7F722F36-54C2-410D-8441-9B62BFA90C91
VIAF ID	wds:Q28324177-855D4FBE-DCB8-4733-B074-4140B75568C9
SBN author ID	wds:Q28324177-91F4FAE0-1E57-4763-B904-9E20F0D2D4AF
date of birth	wds:Q28324177-D3671696-87F1-4C84-A0B8-9ECF2F56B010
family name	wds:q28324177-246094be-49b2-df58-a188-033310841c81
WorldCat Identities ID (superseded)	wds:q28324177-de72c871-4baa-59c2-cb4f-d31785ca6184
VIAF ID	http://viaf.org/viaf/307345233
occupation	researcher
employer	University of Padua
CONOR.SI ID	132222563
NSK ID	000726354
sex or gender	female organism
VIAF ID	307345233
SBN author ID	CFIV275169
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
family name	Cendron
WorldCat Identities ID (superseded)	viaf-307345233
Springer Nature person ID	wds:Q28324177-36431713-928B-4DF8-8B8E-7089AB099923
ORCID iD	wds:Q28324177-C7E00DB1-0BC0-42B5-BEDC-3D7237DFCD2D
Dimensions author ID	wds:Q28324177-AC96E7D9-0E26-4986-ACD0-ABD47BE9B962
ORCID iD	https://orcid.org/0000-0002-0125-0461
Springer Nature person ID	0774345673.70
ORCID iD	0000-0002-0125-0461
Dimensions author ID	0774345673.70
Padua Research Archive author ID	wds:Q28324177-2F0CCF02-1670-49C1-8710-7134319F85C0
Padua Research Archive author ID	22606
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28324177
is author of	Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors DJ-1 is a copper chaperone acting on SOD1 activation The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation The EF-Hand Ca2+ Binding Protein MICU Choreographs Mitochondrial Ca2+ Dynamics in Arabidopsis Probing the evolution of hydroxyisourate hydrolase into transthyretin through active-site redesign. Crystal structure of truncated FlgD from the human pathogen Helicobacter pylori Acidic pH-induced conformational changes in amyloidogenic mutant transthyretin Amyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSES Helicobacter pylori acidic stress response factor HP1286 is a YceI homolog with new binding specificity Structure of the uncomplexedNeisseria meningitidisfactor H-binding protein fHbp (rLP2086) Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases The Structure of Helicobacter pylori HP0310 Reveals an Atypical Peptidoglycan Deacetylase Aluminum, copper, iron and zinc differentially alter amyloid-Aβ(1-42) aggregation and toxicity Multiple binding sites for substrates and modulators of semicarbazide-sensitive amine oxidases: kinetic consequences Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system

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