Wei Ge

发表

A human protein hydroxylase that accepts D-residues

Hwangseo Park, C. Schofield, T. Leissing, 2020, Communications Chemistry.

Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor.

C. Schofield, J. McCullagh, R. Chowdhury, 2013, Angewandte Chemie.

OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation

Rachelle S. Singleton, P. Ratcliffe, M. Coleman, 2014, Proceedings of the National Academy of Sciences.

Ribosomal Oxygenases are Structurally Conserved from Prokaryotes to Humans

K. Kavanagh, F. von Delft, U. Oppermann, 2014, Nature.

Crystal structure of the PHF8 Jumonji domain, an N ε‐methyl lysine demethylase

K. Kavanagh, W. Yue, U. Oppermann, 2010, FEBS letters.

Engineered Escherichia coli Nissle 1917 with urate oxidase and an oxygen-recycling system for hyperuricemia treatment

Mingyu Wang, Huaiwei Liu, Yongzhen Xia, 2022, Gut microbes.

Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor.

A. Conejo-García, C. Schofield, K. Hewitson, 2010, Bioorganic & medicinal chemistry letters.

Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation

C. Schofield, J. Paps, G. Preston, 2014, Proceedings of the National Academy of Sciences.

Assembly, Core Microbiota, and Function of the Rhizosphere Soil and Bark Microbiota in Eucommia ulmoides

Wei Ge, YAN-FENG Han, Qi-Yu Shao, 2022, Frontiers in Microbiology.

Optimal Translational Termination Requires C4 Lysyl Hydroxylation of eRF1

L. Frolova, E. Alkalaeva, P. Ratcliffe, 2014, Molecular cell.

The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site

P. Rutledge, I. Clifton, J. Baldwin, 2013, FEBS letters.

Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases.

U. Oppermann, B. Marsden, K. Che, 2012, Angewandte Chemie.

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans.

C. Robinson, P. Ratcliffe, M. Coleman, 2012, Nature chemical biology.

Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy

P. Ratcliffe, M. Mackeen, B. Kessler, 2014, Proceedings of the National Academy of Sciences.

PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an N-dimethyl lysine demethylase

R. Klose, P. Ratcliffe, M. Coleman, 2009 .

Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

I. Landrieu, P. Ratcliffe, C. Domene, 2016, Nature Communications.

New perspective: Symbiotic pattern and assembly mechanism of Cantharellus cibarius-associated bacteria

S. Deshmukh, Wei Ge, Zhaoying He, 2023, Frontiers in Microbiology.

The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases

Weston B. Struwe, Simon Davis, Christopher J. Schofield, 2018, Nature Chemical Biology.

Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth

P. Ratcliffe, C. Schofield, M. Melani, 2014, Proceedings of the National Academy of Sciences.

Asparagine and Aspartate Hydroxylation of the Cytoskeletal Ankyrin Family Is Catalyzed by Factor-inhibiting Hypoxia-inducible Factor

Christopher J. Schofield, Wei Ge, Timothy D. W. Claridge, 2010, The Journal of Biological Chemistry.

Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases

C. Schofield, M. McDonough, W. Aik, 2015, Structure.

Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases

C. Schofield, R. Chowdhury, A. Kawamura, 2016, Nature Communications.

The crystal structure of isopenicillin N synthase with δ-((L)-α-aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination to iron.

P. Rutledge, I. Clifton, J. Baldwin, 2011, Archives of biochemistry and biophysics.

Isopenicillin N Synthase Binds δ‐(L‐α‐Aminoadipoyl)‐L‐Cysteinyl‐D‐Thia‐allo‐Isoleucine through both Sulfur Atoms

P. Rutledge, I. Clifton, J. Baldwin, 2011, Chembiochem : a European journal of chemical biology.

Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase.

Jeanette E. Stok, P. Rutledge, I. Clifton, 2010, Biochemical and biophysical research communications.

The crystal structure of an LLL-configured depsipeptide substrate analogue bound to isopenicillin N synthase.

Jeanette E. Stok, P. Rutledge, I. Clifton, 2010, Organic & biomolecular chemistry.

Structural Studies on the Reaction of Isopenicillin N Synthase with a Sterically Demanding Depsipeptide Substrate Analogue

P. Rutledge, I. Clifton, J. Baldwin, 2009, Chembiochem : a European journal of chemical biology.

JMJD5 is a human arginyl C-3 hydroxylase

C. Schofield, R. Chowdhury, R. Hopkinson, 2018, Nature Communications.

Specialist species of fungi and bacteria are more important than the intermediate and generalist species in near-urban agricultural soils

Wei Ge, C. Dong, Yulian Ren, 2023, Applied Soil Ecology.

Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains

P. Ratcliffe, B. Kessler, C. Schofield, 2011, The FEBS journal.

Mitochondria immobilized fluorescent probe for dual-emissive monitoring mitophagy based on aggregation/monomer principle

Wei Ge, Minggang Tian, Juan Li, 2023, Sensors and Actuators B: Chemical.

Deciphering Protein O-GalNAcylation: Method Development and Disease Implication

Shuang-Fen Yue, Shuang Yang, Wei Ge, 2023, ACS omega.

The Tet2–Upf1 complex modulates mRNA stability under stress conditions

Wei Ge, Z. Miao, Bo Wan, 2023, Frontiers in Genetics.

Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a depsipeptide substrate analogue: implications for oxygen binding and a link to nitrile hydratase?

P. Rutledge, I. Clifton, J. Baldwin, 2008, Journal of the American Chemical Society.