About: Birgit Habenstein

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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) 研究者 (ja) wetenschapper (nl) дослідниця (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy)
rdfs:label	Birgit Habenstein (en) Birgit Habenstein (es) Birgit Habenstein (nl) Birgit Habenstein (ast)
skos:prefLabel	Birgit Habenstein (en) Birgit Habenstein (es) Birgit Habenstein (nl) Birgit Habenstein (ast)
name	Birgit Habenstein (en) Birgit Habenstein (es) Birgit Habenstein (nl) Birgit Habenstein (ast)
given name	wds:Q57019911-EA5AE6FF-83CF-45B0-8F8B-3621B0F16E4D
given name	Birgit
instance of	wds:Q57019911-0FBE46AB-A697-4FB8-861D-7EA4924D1932
instance of	Homo sapiens
doctoral advisor	wds:Q57019911-2A9AC02A-1EDF-431E-BC43-D838410AEFC0
doctoral advisor	Anja Böckmann
occupation	wds:Q57019911-7238D29E-149A-46D8-A573-AF9E5F4A6061
sex or gender	wds:Q57019911-e19bb8cf-8e56-4996-8b57-543ab8df05b6
VIAF ID	wds:Q57019911-5AC85CC1-04C8-43DC-B826-0C760787C9C8
IdRef ID	wds:Q57019911-9F89F3D5-7217-4A2A-B660-9896B1A7E223
date of birth	wds:Q57019911-0CF9C2EB-3A38-4C67-9046-7456014C8304
VIAF ID	http://viaf.org/viaf/306486195
IdRef ID	http://www.idref.fr/176350586/id
occupation	researcher
sex or gender	female organism
VIAF ID	306486195
IdRef ID	176350586
date of birth	1981-01-01 00:00:00Z (xsd:dateTime)
ORCID iD	wds:Q57019911-D44D100D-6E21-4831-B372-DDC713C5B5DC
ORCID iD	https://orcid.org/0000-0003-3723-9552
ORCID iD	0000-0003-3723-9552
ResearcherID	wds:Q57019911-82D83C05-B956-4E20-AB1B-3A0FBA2D74B2
Publons author ID	wds:Q57019911-636c0776-4ec1-6a45-415a-a6f6eb677fe2
ResearcherID	E-4425-2013
Publons author ID	2649458
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57019911
is author of	Structural and functional characterization of two alpha-synuclein strains Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion Protocols for the Sequential Solid-State NMR Spectroscopic Assignment of a Uniformly Labeled 25 kDa Protein: HET-s(1-227) The conformation of the prion domain of Sup35p in isolation and in the full-length protein Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity BSH-CP based 3D solid-state NMR experiments for protein resonance assignment β-Sheet core of tau paired helical filaments revealed by solid-state NMR. High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils. [Structure of a bacterial nanomachine: the type 3 secretion system needle]. Solid-state NMR sequential assignments of the amyloid core of Sup35pNM. Solid-state NMR sequential assignments of α-synuclein. Yet another polymorph of α-synuclein: solid-state sequential assignments A Two-Component Adhesive: Tau Fibrils Arise from a Combination of a Well-Defined Motif and Conformationally Flexible Interactions. Lipid Internal Dynamics Probed in Nanodiscs. Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene. The extracellular matrix protects Bacillus subtilis colonies from Pseudomonas invasion and modulates plant co-colonization Molecular architecture of bacterial amyloids in Bacillus biofilms Novel self-replicating α-synuclein polymorphs that escape ThT monitoring can spontaneously emerge and acutely spread in neurons Bacterial Filamentous Appendages Investigated by Solid-State NMR Spectroscopy Detection of side-chain proton resonances of fully protonated biosolids in nano-litre volumes by magic angle spinning solid-state NMR. 3D structure determination of amyloid fibrils using solid-state NMR spectroscopy. Structural and Functional Characterization of the Type Three Secretion System (T3SS) Needle of Coiled-coil oligomerization controls localization of the plasma membrane REMORINs. REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment Automated solid-state NMR resonance assignment of protein microcrystals and amyloids Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR Structural dissection of amyloid aggregates of TDP-43 and its C-terminal fragments TDP-35 and TDP-16 Molecular mechanisms for the destabilization of model membranes by islet amyloid polypeptide Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein Mechanisms governing subcompartmentalization of biological membranes A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.
is author of	wds:Q41189772-020F2D6E-352F-45C2-992F-A7D38A72F1AB wds:Q51316365-41885312-2DAD-486A-A14A-74FE637F33C7 wds:Q100427007-47F8D8AE-C6D5-46D6-9B40-4DDC832E5593 wds:Q40151205-E77ADDCD-9594-40AA-94A2-A90B2179A7BC wds:Q44220930-E8489125-0536-4A41-9460-39164EBFE78A wds:Q45877820-CC0D3F23-4174-4B31-ADE0-56BA60F25F2F wds:Q45307267-D1B6B13B-B196-494B-BAD6-1C6F9C926854 wds:Q46950940-C29D2535-FAAC-46C9-A468-6F1051092A87 wds:Q52675503-4CEE178D-8DC7-4975-990A-40D725AD5EC2

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