About: Adrian Goldman

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researcher ORCID ID = 0000-0001-8032-9700

Attributes	Values
rdf:type	Item
description	forskare (sv) ikertzailea (eu) araştırmacı (tr) эрдэмтэн (mn) वैज्ञानिक (hi) باحت (ary) изилдөөчү (ky) 研究者 (zh) onderzoeker (nl) researcher ORCID ID = 0000-0001-8032-9700 (en)
rdfs:label	Adrian Goldman (en) Adrian Goldman (es) Adrian Goldman (nl) Adrian Goldman (ast)
skos:prefLabel	Adrian Goldman (en) Adrian Goldman (es) Adrian Goldman (nl) Adrian Goldman (ast)
name	Adrian Goldman (en) Adrian Goldman (es) Adrian Goldman (nl) Adrian Goldman (ast)
affiliation	wds:Q61785066-a01cf15d-44ec-67c8-fce3-d928d0b83e3d
affiliation	School of Biomedical Sciences
given name	wds:Q61785066-219089c8-4298-5627-d4c8-e2d77e1cc681 wds:Q61785066-51C7E126-A090-4937-8FDE-E40E3B2E6B77
given name	Jack Adrian
instance of	wds:Q61785066-B72A9A84-263E-4463-A0A9-B7DE6E415935
instance of	Homo sapiens
occupation	wds:Q61785066-313bcc7d-4b35-cada-6b79-79f27c55f0d6
employer	wds:Q61785066-079d402a-4443-f773-052c-c3fa20d574d0 wds:Q61785066-45adc541-40a9-14c5-365b-de337acd7907 wds:Q61785066-4BBC305B-8414-4189-BF82-1AD391183D9B wds:Q61785066-75B80381-43C1-4EEB-86F9-E1C1E5A2DC2F wds:Q61785066-8D3C2CA2-7FF4-426A-8B00-5691955A50D6 wds:Q61785066-E6DFAB82-96DA-40DF-8D21-41478CD721C7 wds:Q61785066-a902d8a8-40c0-2d12-09b0-529324288aa6
participant in	wds:Q61785066-DE3D7401-74EA-43D3-9E5C-CF11499D4BA1
sex or gender	wds:Q61785066-a0e8b394-4bd9-779e-f00e-ba777097eb6c
educated at	wds:Q61785066-D3E3E9CB-0243-4299-94C8-C07BC117EFF7 wds:Q61785066-FEC2F739-59EC-4EBD-B372-A896348399DD
family name	wds:Q61785066-5F9FF0F6-90D3-49E2-BADA-8ECE1C718685 wds:Q61785066-9A6567A3-E65F-4065-8F25-C922CE6CBB86
official website	wds:Q61785066-6CE9ABB8-A63A-47A6-9FE4-29AD20ED0002
occupation	researcher
employer	Nankai University University of Leeds University of Helsinki Helsinki Institute of Physics Faculty of Biological Sciences
participant in	Exploiting the structure of integral membrane pyrophosphatases
sex or gender	male
educated at	University of Leeds Helsinki Institute of Physics
family name	Goldman Wright
official website	https://researchportal.helsinki.fi/en/persons/994b51b5-3f68-4fa1-b8ce-97193fac623f
ORCID iD	wds:Q61785066-67EEB554-E45A-4E15-934D-BBDCB8E91367 wds:Q61785066-BDA4182D-FE6E-4C09-A907-AB35E2343B06
ORCID iD	https://orcid.org/0000-0001-8032-9700 https://orcid.org/0000-0002-1847-9027
ORCID iD	0000-0001-8032-9700 0000-0002-1847-9027
is owl:sameAs of	Adrian Goldman
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q61785066
is author of	The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll Obesity risk gene TMEM18 encodes a sequence-specific DNA-binding protein A Trimetal Site and Substrate Distortion in a Family II Inorganic Pyrophosphatase Electrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90: COMPUTATIONAL ANALYSIS AND PROTEIN ENGINEERING Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide Structure of Streptococcus agalactiae serine/threonine phosphatase Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi The Structure of the Glial Cell Line-derived Neurotrophic Factor-Coreceptor Complex: INSIGHTS INTO RET SIGNALING AND HEPARIN BINDING Zebrafish GDNF and its co-receptor GFRα1 activate the human RET receptor and promote the survival of dopaminergic neurons in vitro The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease. Structure and biology of trimeric autotransporter adhesins. The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Yersinia infection tools-characterization of structure and function of adhesins The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement A method for detergent-free isolation of membrane proteins in their local lipid environment. First analysis of a bacterial collagen-binding protein with collagen Toolkits: promiscuous binding of YadA to collagens may explain how YadA interferes with host processes Unusual twinning in an acetyl coenzyme A synthetase (ADP-forming) fromPyrococcus furiosus A complete structural description of the catalytic cycle of yeast pyrophosphatase The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site Proton/sodium pumping pyrophosphatases: the last of the primary ion pumps. The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2 Human UDP-glucuronosyltransferase expression in insect cells: ratio of active to inactive recombinant proteins and the effects of a C-terminal his-tag on glucuronidation kinetics. The first aspartic acid of the DQxD motif for human UDP-glucuronosyltransferase 1A10 interacts with UDP-glucuronic acid during catalysis. Mutation analysis in UGT1A9 suggests a relationship between substrate and catalytic residues in UDP-glucuronosyltransferases. Artificial membranes for membrane protein purification, functionality and structure studies Correction: Microbes Bind Complement Inhibitor Factor H via a Common Site G protein-coupled receptors show unusual patterns of intrinsic unfolding Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure. Crystal structure of a tripartite complex between C3dg, C-terminal domains of factor H and OspE of Borrelia burgdorferi. Comparison of GFL–GFRα complexes: further evidence relating GFL bend angle to RET signalling [Pyrophosphate in medicine].

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