About: Ying Li

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

researcher, University of Louisville, ORCID ID = 0000-0001-7678-9405

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) 연구원 (ko) 研究者 (ja) araştırmacı (tr) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) researcher (ORCID ID = 0000-0001-7678-9405) (en-gb) researcher, University of Louisville, ORCID ID = 0000-0001-7678-9405 (en)
rdfs:label	Ying Li (en) Ying Li (nl) Ying Li (ast) Ying Li (es) Ying Li (nb) Ying Li (de) Ying Li (da) Ying Li (fo) Ying Li (fr) Ying Li (is) Ying Li (kl) Ying Li (nn) Ying Li (sv) Ying Li (en-gb) Ying Li (sl)
skos:prefLabel	Ying Li (en) Ying Li (nl) Ying Li (ast) Ying Li (es) Ying Li (nb) Ying Li (de) Ying Li (da) Ying Li (fo) Ying Li (fr) Ying Li (is) Ying Li (kl) Ying Li (nn) Ying Li (sv) Ying Li (en-gb) Ying Li (sl)
name	Ying Li (en) Ying Li (nl) Ying Li (ast) Ying Li (es) Ying Li (nb) Ying Li (de) Ying Li (da) Ying Li (fo) Ying Li (fr) Ying Li (is) Ying Li (kl) Ying Li (nn) Ying Li (sv) Ying Li (en-gb) Ying Li (sl)
given name	wds:Q43119564-1AFFECD2-1563-453F-AA59-A6179BAF3D5F
given name	Ying
instance of	wds:Q43119564-A83DD55A-763D-496F-A694-9B87A858E494
instance of	Homo sapiens
occupation	wds:Q43119564-97F10351-A44C-4BE7-A9D1-7FD35196227F
employer	wds:Q43119564-6AA56542-F409-4B9B-884D-E03B8EA3BE80 wds:Q43119564-B128F24B-2117-437A-990D-97FBB4655C71
sex or gender	wds:Q43119564-E22C6E72-4DDB-4F60-BDCC-9CB6B9BA382F
date of birth	wds:Q43119564-EB320E55-692C-4CE2-84E5-FD2C9D00944E
educated at	wds:Q43119564-23147DDB-73EE-4435-B6DB-19F61B5BC6A8 wds:Q43119564-3BB76757-7256-4169-A888-F1356E641B18
occupation	researcher
employer	Columbia University University of Louisville
sex or gender	female organism
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
educated at	University of Illinois at Urbana–Champaign Nanjing University
ORCID iD	wds:Q43119564-03C394A9-7CFA-41CE-9098-FA1A0EB287DA
ORCID iD	https://orcid.org/0000-0001-7678-9405
ORCID iD	0000-0001-7678-9405
ResearcherID	wds:Q43119564-46C619F2-E80D-4187-860B-BC17AD6F23B6
Publons author ID	wds:Q43119564-7f379e4d-3257-4da3-983c-eb1175d3a793
ResearcherID	D-1758-2011
Publons author ID	1539242
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q43119564
is author of	TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy. Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy. Temperature-dependent sensitivity enhancement of solid-state NMR spectra of alpha-synuclein fibrils Reduction of RF-induced sample heating with a scroll coil resonator structure for solid-state NMR probes. Narrowing of protein NMR spectral lines broadened by chemical exchange Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4. Crystal structure of chemically synthesized vMIP-II Crystal structure and structural mechanism of a novel anti-human immunodeficiency virus and D-amino acid-containing chemokine Selective refocusing pulses in magic-angle spinning NMR: characterization and applications to multi-dimensional protein spectroscopy. Partial (13)C and (15)N chemical-shift assignments of the disulfide-bond-forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion Backbone H, C, and N resonance assignments of deubiquitinase A in non-phosphorylated and phosphorylated forms Conformational flexibility in the binding surface of the potassium channel blocker ShK. Rotation operator propagators for time-varying radiofrequency pulses in NMR spectroscopy: applications to shaped pulses and pulse trains Modulation of conformational equilibrium by phosphorylation underlies the activation of deubiquitinase A Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant. Conformational Dynamics of Deubiquitinase A and Functional Implications

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