About: Mathias Ziegler

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researcher (ORCID 0000-0001-6961-2396), University of Bergen

Attributes	Values
rdf:type	Item
description	forskare (sv) ikertzailea (eu) 연구원 (ko) গবেষক (bn) 研究者 (ja) ഗവേഷകൻ (ml) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq) researcher (ORCID 0000-0001-6961-2396), University of Bergen (en)
rdfs:label	Mathias Ziegler (en) Mathias Ziegler (es) Mathias Ziegler (nl) Mathias Ziegler (ast) Mathias Ziegler (de) Mathias Ziegler (sl) ماثياس زيغلر (ar)
skos:prefLabel	Mathias Ziegler (en) Mathias Ziegler (es) Mathias Ziegler (nl) Mathias Ziegler (ast) Mathias Ziegler (de) Mathias Ziegler (sl) ماثياس زيغلر (ar)
name	Mathias Ziegler (en) Mathias Ziegler (es) Mathias Ziegler (nl) Mathias Ziegler (ast) Mathias Ziegler (de) Mathias Ziegler (sl) ماثياس زيغلر (ar)
Scopus author ID	wds:Q42723114-ED7759FF-F602-4021-83DC-6DE5FBDC8735
Scopus author ID	7202530401
given name	wds:Q42723114-FF188CBE-3838-40AE-822C-057A7D08B342
given name	Mathias
instance of	wds:Q42723114-46385107-42C4-4C06-80F3-11C8AC2F51AC
instance of	Homo sapiens
occupation	wds:Q42723114-43C05323-B70C-4362-B70A-D64A12A0BAA2
employer	wds:Q42723114-46C2052A-AFAD-44B5-B3E9-483F9CED0474
sex or gender	wds:Q42723114-1706FD47-CEB6-40DA-9FB8-951B5DF145A0
VIAF ID	wds:Q42723114-772cc050-afe1-4364-ba93-c55ed7345e70
IdRef ID	wds:Q42723114-F4B04AE0-9AD0-436B-B101-569C899BC4C5
family name	wds:Q42723114-554BED03-725F-4C51-B1D3-FABAE75F3502
VIAF ID	http://viaf.org/viaf/309153409726641580387
IdRef ID	http://www.idref.fr/228494176/id
occupation	researcher
employer	University of Bergen
sex or gender	male
VIAF ID	309153409726641580387
IdRef ID	228494176
family name	Ziegler
ORCID iD	wds:Q42723114-2A7F0ED9-486F-4DEF-B888-6DC6967FD579
ORCID iD	https://orcid.org/0000-0001-6961-2396
ORCID iD	0000-0001-6961-2396
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42723114
is author of	Regulation of RNA polymerase II-dependent transcription by poly(ADP-ribosyl)ation of transcription factors An organellar nα-acetyltransferase, naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms The power to reduce: pyridine nucleotides--small molecules with a multitude of functions The new life of a centenarian: signalling functions of NAD(P). Application of a coupled enzyme assay to characterize nicotinamide riboside kinases Structural and functional characterization of human NAD kinase The human NAD metabolome: Functions, metabolism and compartmentalization Stimulation of the catalytic activity of poly(ADP-ribosyl) transferase by transcription factor Yin Yang 1. Pathophysiological relevance of mitochondria in NAD(+) metabolism. Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation. Separating NADH and NADPH fluorescence in live cells and tissues using FLIM Protein-protein interaction of the human poly(ADP-ribosyl)transferase depends on the functional state of the enzyme. Time sensing by NAADP receptors. Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-acetyltransferase activity Poly(ADP-ribosylation) and genomic stability Generation, Release, and Uptake of the NAD Precursor Nicotinic Acid Riboside by Human Cells Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis Regulation of glutamate dehydrogenase by reversible ADP-ribosylation in mitochondria New functions of a long-known molecule Refinement of a radioreceptor binding assay for nicotinic acid adenine dinucleotide phosphate NAD kinase levels control the NADPH concentration in human cells ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). Compartmentation of NAD+-dependent signalling. Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1 Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN Progress in the function and regulation of ADP-Ribosylation. Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform Insect immune activation by apolipophorin III is correlated with the lipid-binding properties of this protein. Carbohydrate metabolism during vertebrate appendage regeneration: what is its role? How is it regulated?: A postulation that regenerating vertebrate appendages facilitate glycolytic and pentose phosphate pathways to fuel macromolecule biosynthesis NAD+ analogs substituted in the purine base as substrates for poly(ADP-ribosyl) transferase. Emerging roles of NAD+ and its metabolites in cell signaling. Pathway analysis of NAD+metabolism Visualization of subcellular NAD pools and intra-organellar protein localization by poly-ADP-ribose formation NAD+biosynthesis and salvage - a phylogenetic perspective The NMN/NaMN adenylyltransferase (NMNAT) protein family. ATP-dependent selection between single nucleotide and long patch base excision repair. Insect immune activation by recombinant Galleria mellonella apolipophorin III(1). The phosphate makes a difference: cellular functions of NADP.

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