Our structural biology programme at the crossroad of genetic diseases and drug discovery

The MOB group combines structural, biochemical, and chemical biology approaches to explore how genetic defects lead to disease at a protein molecular level. The group has determined to date > 60 crystal structures of human enzymes and complexes that are associated with Inborn Errors of Metabolism. We form a partnership network with 'front-line' geneticists, clinicians and drug developers in the field of rare diseases, aimed at deciphering the underlying genetic, biochemical and cellular disease mechanisms, as a first step towards developing novel disease-transforming therapeutics.

Our key areas of research interest include:

Structural characterization of metabolic enzyme complexes

Many metabolic enzymes performing essential cellular roles do not exist as individual entities, but instead function in concert with other proteins in the cellular compartment. These partner proteins within a macromolecular complex could be ‘functional neighbours’ performing the upstream/ downstream chemical reactions within a metabolic pathway, or accessory subunits responsible for the structural integrity and functional modulation of the target enzyme. As part of our rare disease research programme, we have a vested interest in studying metabolic enzyme complexes that are linked with genetic diseases. We adopt the co-expression approach to generate metabolic enzyme complexes for structural, biochemical and biophysical experiments aimed at characterizing the functional and disease-causing mechanisms.

Our recent structure of the molybdenum synthase complex MOCS2A-MOCS2B

Glycogen biosynthesis and storage disorders

In eukaryotes, glycogen biosynthesis involves the priming enzyme glycogenin (GYG1/2), the elongation enzyme glycogen synthase (GYS1/2), and the branching enzyme (GBE1). We have captured crystallographic snapshots of the human glycogenin dimer along its reaction cycle, revealing a dynamic conformational switch between ground and active states mediated by the sugar donor UDP-glucose. This work provides a new look into how glucose units are attached covalently to glycogenin during the initial step of glycogen synthesis. 

Mutations on the GBE1 gene lead to an extremely heterogeneous form of glycogen storage disorder type IV, including an allelic variant, adult polyglucosan body disease, a late-onset neurological disorder with a prevalent missense mutation p.Y329S. We have obtained soluble, recombinant GBE1 in wild-type and mutant forms, and determined its 3D crystal structure. Our long-term goal is to establish a molecular basis for disease-causing mutations (e.g. p.Y329S) and develop ‘pharmacological chaperones’ as novel therapeutics.

 Visit the webpage of Adult Polyglucosan Body Disease Research Foundation (APBDRF), where Wyatt Yue contributes as member of its Scientific Advisory Board.

Galactose metabolism, Lenoir pathway, and Galactosemia

Galactose-1-phosphate uridylyltransferase (GALT) is an essential enzyme in the Leloir pathway of galactose metabolism where it reversibly transfers a uridine monophosphate (UMP) group between galactose-1-phosphate and uridine diphosphate glucose, to generate glucose-1-phosphate. Mutations of the GALT gene lead to type I or classical galactosemia, with the most prevalent allele Q188R known to abolish GALT activity completely. We determined the 1.8 Å structure of human GALT ternary complex that contains a covalent uridylylated intermediate and glucose-1-phosphate in the active site. The structure provides a molecular template to understand the role of Gln188, and rationalizes the range of missense mutations associated with type I galactosemia, including Q188R

Read Wyatt Yue's article 'Conference First-timer reflects on Atlanta' on the Galactosemia Foundation newsletter (Winter 2016)

Human Vitamin B12 Metabolism

While Vitamin B­12 serves as the cofactor for only two human enzymes (mitochondrial methylmalonyl-CoA mutase and cytosolic methionine synthase), an intracellular pathway of seven known proteins has evolved for the uptake, processing and delivery of the appropriate cofactor form to the two enzymes. The essentiality of this ‘B12 trafficking pathway’ is underscored by inherited defects reported in all seven proteins, giving rise to the metabolic disorders methylmalonic aciduria and homocystinuria. Despite the well-defined genetic makeup of the B12 pathway, the biochemical function and interplay of the seven proteins, as well as the molecular basis of their genetic defects, remain poorly understood. Since 2010, the Structural Genomics Consortium has adopted a family-based approach in the study of the B12 pathway, with the structure determination of six member proteins (PDB codes: MUT 2XIQ, MMAA 2WWW, MCEE 3RMU, MMACHC 3SOM, MTR 4CCZ, MMADHC 5A4R), resulting in new lessons for the B12 pathway.





Group Members

Jolanta Kopec
Postdoc researcher
Nicholas Fox
Postdoc researcher
Elzbieta Rembeza
Research Technician
Hannah Brazier
DPhil Student
Sabrina MacKinnon
DPhil Student
Henry Bailey
DPhil Student
Jack Kelly
DPhil Student
Group Alumni
  • Stephanie Oerum (SGC DPhil 2012-2016, currently Postdoc at Université Paris Diderot)
  • Igor Ferreira (SGC visiting scientist 2012-2013 postdoc 2015-2016)
  • Thomas McCorvie (SGC postdoc 2012-2015, currently Research Associate at Imperial College)
  • Dipali Patel (SGC postdoc 2013-2015, currently Scientist at Relay Therapeutics)
  • Izabella Pena (SGC visiting scientist 2013-2014, currently postdoc at Children's Hospital at Eastern Ontario)
  • Fiona Fitzpatrick (SGC research technician 2013-2015, currently PhD student at University of Cambridge)
  • Sean Froese (SGC postdoc 2010-2013, currently Assistant Professor at Kinderspital Zurich)
  • Wasim Kiyani (SGC research technician 2011-2013, currently PhD student at Glasgow University)
  • Naeem Shafqat (SGC postdoc 2009-2011, currently Senior Assistant Professor, University Brunei Darussalam)
  • Ewelina Kryztofinska (SGC research technician 2009-2011, currently PhD student at King’s College London)


Group Publications


The origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats.
Pascoal, CC; Islam, Z; Adamoski, D; Ferreira, IM; Righetto, RD; Bettini, J; Portugal, RV; Yue, WW; Gonzalez, A; Dias, SMG; Ambrosio, ALB;
Journal of Biological Chemistry. 2017 :-. doi: 10.1074/jbc.M117.787291
PMID: 28526749

Protein destabilization and loss of protein-protein interaction are fundamental mechanisms in cblA-type methylmalonic aciduria.
Plessl, T; Bürer, C; Lutz, S; Yue, WW; Baumgartner, MR; Froese, DS;
Human Mutation. 2017 :-. doi: 10.1002/humu.23251
PMID: 28497574


Advantages and pitfalls of an extended gene panel for investigating complex neurometabolic phenotypes.
Reid, ES; Papandreou, A; Drury, S; Boustred, C; Yue, WW; Wedatilake, Y; Beesley, C; Jacques, TS; Anderson, G; Abulhoul, L; Broomfield, A; Cleary, M; Grunewald, S; Varadkar, SM; Lench, N; Rahman, S; Gissen, P; Clayton, PT; Mills, PB;
Brain: a journal of neurology. 2016 :-. doi:
PMID: 27604308

From structural biology to designing therapy for inborn errors of metabolism.
Y, W; u, W; e, ;
Journal of Inherited Metabolic Disease. 2016 39:489-498. doi:
PMID: 27240455

Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.
Patel, D; Kopec, J; Fitzpatrick, F; McCorvie, TJ; Yue, WW;
Scientific Reports. 2016 6:23748-. doi:
PMID: 27049649

Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase.
McCorvie, TJ; Kopec, J; Pey, AL; Fitzpatrick, F; Patel, D; Chalk, R; Streetha, L; Yue, WW;
Human Molecular Genetics. 2016 :-. doi:
PMID: 27005423

Expanding the Genotypic Spectrum of Perrault syndrome.
Demain, LA; Urquhart, JE; O'Sullivan, J; Williams, SG; Bhaskar, SS; Jenkinson, EM; Lourenco, CM; Heiberg, A; Pearce, SH; Shalev, SA; Yue, WW; Mackinnon, S; Munro, KJ; Newbury-Ecob, R; Becker, K; Kim, MJ; O' Keefe, RT; Newman, WG;
Clinical Genetics: an international journal of genetics and molecular medicine. 2016 :-. doi:
PMID: 26970254

Use of Methylmalonyl-CoA Epimerase in Enhancing Crotonase Stereoselectivity.
Hamed, RB; Gomez-Castellanos, JR; Sean Froese, D; Krysztofinska, E; Yue, WW; Schofield, CJ;
ChemBioChem: a European journal of chemical biology. 2016 17:471-473. doi:
PMID: 26716911

Role of reverse phenotyping in interpretation of next generation sequencing data and a review of INPP5E related disorders.
de Goede, C; Yue, WW; Yan, G; Ariyaratnam, S; Chandler, KE; Downes, L; Khan, N; Mohan, M; Lowe, M; Banka, S;
European Journal of Paediatric Neurology. 2016 20:286-295. doi:
PMID: 26748598

Crystal structure of Porphyromonas gingivalis peptidylarginine deiminase: implications for autoimmunity in rheumatoid arthritis.
Montgomery, AB; Kopec, J; Shrestha, L; Thezenas, ML; Burgess-Brown, NA; Fischer, R; Yue, WW; Venables, PJ;
Annals of the Rheumatic Diseases. 2016 75:1255-1261. doi:
PMID: 26209657


Structural Insights into the MMACHC-MMADHC Protein Complex Involved in Vitamin B12 Trafficking.
Froese, DS; Kopec, J; Fitzpatrick, F; Schuller, M; McCorvie, TJ; Chalk, R; Plessl, T; Fettelschoss, V; Fowler, B; Baumgartner, MR; Yue, WW;
Journal of Biological Chemistry. 2015 290:29167-29177. doi:
PMID: 26483544

Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation.
Colak, G; Pougovkina, O; Dai, L; Tan, M; Te Brinke, H; Huang, H; Cheng, Z; Park, J; Wan, X; Liu, X; Yue, WW; Wanders, RJ; Locasale, JW; Lombard, DB; de Boer, VC; Zhao, Y;
Molecular and Cellular Proteomics. 2015 14:3056-3071. doi:
PMID: 26320211

Structural basis of glycogen branching enzyme deficiency and pharmacologic rescue by rational peptide design.
Froese, DS; Michaeli, A; McCorvie, TJ; Krojer, T; Sasi, M; Melaev, E; Goldblum, A; Zatsepin, M; Lossos, A; Álvarez, R; Escribá, PV; Minassian, BA; von Delft, F; Kakhlon, O; Yue, WW;
Human Molecular Genetics. 2015 24:5667-5676. doi:
PMID: 26199317

Mutations in GMPPB cause congenital myasthenic syndrome and bridge myasthenic disorders with dystroglycanopathies.
Belaya, K; Rodríguez Cruz, PM; Liu, WW; Maxwell, S; McGowan, S; Farrugia, ME; Petty, R; Walls, TJ; Sedghi, M; Basiri, K; Yue, WW; Sarkozy, A; Bertoli, M; Pitt, M; Kennett, R; Schaefer, A; Bushby, K; Parton, M; Lochmüller, H; Palace, J; Muntoni, F; Beeson, D;
Brain: a journal of neurology. 2015 138:2493-2504. doi:
PMID: 26133662

Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation.
Riemersma, M; Froese, DS; van Tol, W; Engelke, UF; Kopec, J; van Scherpenzeel, M; Ashikov, A; Krojer, T; von Delft, F; Tessari, M; Buczkowska, A; Swiezewska, E; Jae, LT; Brummelkamp, TR; Manya, H; Endo, T; van Bokhoven, H; Yue, WW; Lefeber, DJ;
Chemistry and Biology. 2015 22:1643-1652. doi:
PMID: 26687144

Carnosine metabolism in diabetes is altered by reactive metabolites.
Peters, V; Lanthaler, B; Amberger, A; Fleming, T; Forsberg, E; Hecker, M; Wagner, AH; Yue, WW; Hoffmann, GF; Nawroth, P; Zschocke, J; Schmitt, CP;
Amino Acids. 2015 47:2367-2376. doi:
PMID: 26081982

Linking genotypes database with locus-specific database and genotype-phenotype correlation in phenylketonuria.
Wettstein, S; Underhaug, J; Perez, B; Marsden, BD; Yue, WW; Martinez, A; Blau, N;
European Journal of Human Genetics. 2015 23:302-309. doi:
PMID: 24939588

Leri's pleonosteosis, a congenital rheumatic disease, results from microduplication at 8q22.1 encompassing GDF6 and SDC2 and provides insight into systemic sclerosis pathogenesis.
Banka, S; Cain, SA; Carim, S; Daly, SB; Urquhart, JE; Erdem, G; Harris, J; Bottomley, M; Donnai, D; Kerr, B; Kingston, H; Superti-Furga, A; Unger, S; Ennis, H; Worthington, J; Herrick, AL; Merry, CL; Yue, WW; Kielty, CM; Newman, WG;
Annals of the Rheumatic Diseases. 2015 74:1249-1256. doi: 10.1136/annrheumdis-2013-204309
PMID: 24442880


Inter-domain communication of human cystathionine β-synthase: structural basis of S-adenosyl-L-methionine activation.
McCorvie, TJ; Kopec, J; Hyung, SJ; Fitzpatrick, F; Feng, X; Termine, D; Strain-Damerell, C; Vollmar, M; Fleming, J; Janz, JM; Bulawa, C; Yue, WW;
Journal of Biological Chemistry. 2014 289:36018-36030. doi:
PMID: 25336647

Expanding the clinical and molecular spectrum of thiamine pyrophosphokinase deficiency: a treatable neurological disorder caused by TPK1 mutations.
Banka, S; de Goede, C; Yue, WW; Morris, AA; von Bremen, B; Chandler, KE; Feichtinger, RG; Hart, C; Khan, N; Lunzer, V; Mataković, L; Marquardt, T; Makowski, C; Prokisch, H; Debus, O; Nosaka, K; Sonwalkar, H; Zimmermann, FA; Sperl, W; Mayr, JA;
Molecular Genetics and Metabolism. 2014 113:301-306. doi:
PMID: 25458521

Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ.
Wichelecki, DJ; Froese, DS; Kopec, J; Muniz, JR; Yue, WW; Gerlt, JA;
Biochemistry. 2014 53:2732-2738. doi:
PMID: 24697329

Functional characterization and categorization of missense mutations that cause methylmalonyl-CoA mutase (MUT) deficiency.
Forny, P; Froese, DS; Suormala, T; Yue, WW; Baumgartner, MR;
Human Mutation. 2014 35:1449-1458. doi:
PMID: 25125334

Mutation or knock-down of 17β-hydroxysteroid dehydrogenase type 10 cause loss of MRPP1 and impaired processing of mitochondrial heavy strand transcripts.
Deutschmann, AJ; Amberger, A; Zavadil, C; Steinbeisser, H; Mayr, JA; Feichtinger, RG; Oerum, S; Yue, WW; Zschocke, J;
Human Molecular Genetics. 2014 23:3618-3628. doi: 10.1093/hmg/ddu072
PMID: 24549042

The role of protein structural analysis in the next generation sequencing era.
Yue, WW; Froese, DS; Brennan, PE;
Topics in Current Chemistry. 2014 336:67-98. doi: 10.1007/128_2012_326
PMID: 22610134


5-Carboxy-8-hydroxyquinoline is a broad spectrum 2-oxoglutarate oxygenase inhibitor which causes iron translocation
Hopkinson, RJ; Tumber, A; Yapp, C; Chowdhury, R; Aik, W; Che, KH; Li, XS; Kristensen, JBL; King, ONF; Chan, MC; Yeoh, KK; Choi, H; Walport, LJ; Thinnes, CC; Bush, JT; Lejeune, C; Rydzik, AM; Rose, NR; Bagg, EA; McDonough, MA; Krojer, TJ; Yue, WW; Ng, SS; Olsen, L; Brennan, PE; Oppermann, U; Müller, S; Klose, RJ; Ratcliffe, PJ; Schofield, CJ; Kawamura, A;
Chemical Science. 2013 4:3110-3117. doi: 10.1039/c3sc51122g
PMID: 26682036

Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations.
Froese, DS; Forouhar, F; Tran, TH; Vollmar, M; Kim, YS; Lew, S; Neely, H; Seetharaman, J; Shen, Y; Xiao, R; Acton, TB; Everett, JK; Cannone, G; Puranik, S; Savitsky, P; Krojer, T; Pilka, ES; Kiyani, W; Lee, WH; Marsden, BD; von Delft, F; Allerston, CK; Spagnolo, L; Gileadi, O; Montelione, GT; Oppermann, U; Yue, WW; Tong, L;
Structure. 2013 21:1182-1192. doi: 10.1016/j.str.2013.05.001
PMID: 23791943

Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits.
Shafqat, N; Muniz, JR; Pilka, ES; Papagrigoriou, E; von Delft, F; Oppermann, U; Yue, WW;
Biochemical Journal. 2013 452:27-36. doi: 10.1042/BJ20121580
PMID: 23425511

A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency.
Shafqat, N; Kavanagh, KL; Sass, JO; Christensen, E; Fukao, T; Lee, WH; Oppermann, U; Yue, WW;
Journal of Inherited Metabolic Disease. 2013 36:983-987. doi: 10.1007/s10545-013-9589-z
PMID: 23420214

LRIG2 mutations cause urofacial syndrome.
Stuart, HM; Roberts, NA; Burgu, B; Daly, SB; Urquhart, JE; Bhaskar, S; Dickerson, JE; Mermerkaya, M; Silay, MS; Lewis, MA; Olondriz, MB; Gener, B; Beetz, C; Varga, RE; Gülpınar, O; Süer, E; Soygür, T; Ozçakar, ZB; Yalçınkaya, F; Kavaz, A; Bulum, B; Gücük, A; Yue, WW; Erdogan, F; Berry, A; Hanley, NA; McKenzie, EA; Hilton, EN; Woolf, AS; Newman, WG;
American Journal of Human Genetics. 2013 92:259-264. doi: 10.1016/j.ajhg.2012.12.002
PMID: 23313374


Forny, P; Froese, DS; Suormala, T; Yue, WW; Baumgartner, MR;
Journal of Inherited Metabolic Disease. 2012 35:S9-S9. doi:

Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
Chaikuad, A; Pilka, ES; De Riso, A; von Delft, F; Kavanagh, KL; Vénien-Bryan, C; Oppermann, U; Yue, WW;
BMC Structural Biology. 2012 12:14-. doi: 10.1186/1472-6807-12-14
PMID: 22720794

Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function.
Froese, DS; Krojer, T; Wu, X; Shrestha, R; Kiyani, W; von Delft, F; Gravel, RA; Oppermann, U; Yue, WW;
Biochemistry. 2012 51:5083-5090. doi: 10.1021/bi300150y
PMID: 22642810

3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical, enzymatic and molecular studies in 88 individuals.
Grünert, SC; Stucki, M; Morscher, RJ; Suormala, T; Bürer, C; Burda, P; Christensen, E; Ficicioglu, C; Herwig, J; Kölker, S; Möslinger, D; Pasquini, E; Santer, R; Schwab, KO; Wilcken, B; Fowler, B; Yue, WW; Baumgartner, MR;
Orphanet Journal of Rare Diseases. 2012 7:31-. doi: 10.1186/1750-1172-7-31
PMID: 22642865

Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.
Pilka, ES; Kochan, G; Oppermann, U; Yue, WW;
Biochemical and Biophysical Research Communications. 2012 419:485-489. doi: 10.1016/j.bbrc.2012.02.038
PMID: 22366092


Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis.
Chaikuad, A; Froese, DS; Berridge, G; von Delft, F; Oppermann, U; Yue, WW;
Proceedings of the National Academy of Sciences of USA. 2011 108:21028-21033. doi: 10.1073/pnas.1113921108
PMID: 22160680

Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family.
Hillringhaus, L; Yue, WW; Rose, NR; Ng, SS; Gileadi, C; Loenarz, C; Bello, SH; Bray, JE; Schofield, CJ; Oppermann, U;
Journal of Biological Chemistry. 2011 286:41616-41625. doi: 10.1074/jbc.M111.283689
PMID: 21914792

Interactive JIMD articles using the iSee concept: turning a new page on structural biology data
Lee, WH; Yue, WW; Raush, E; Totrov, M; Abagyan, R; Oppermann, U; Marsden, BD;
Journal of Inherited Metabolic Disease. 2011 :1-3. doi: 10.1007/s10545-011-9334-4
PMID: 21509537

Structural basis of fumarate hydratase deficiency.
Picaud, S; Kavanagh, KL; Yue, WW; Lee, WH; Muller-Knapp, S; Gileadi, O; Sacchettini, J; Oppermann, U;
Journal of Inherited Metabolic Disease. 2011 34:671-676. doi: 10.1007/s10545-011-9294-8
PMID: 21445611

Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS.
Chaikuad, A; Shafqat, N; Al-Mokhtar, R; Cameron, G; Clarke, AR; Brady, RL; Oppermann, U; Frayne, J; Yue, WW;
Biochemical Journal. 2011 435:401-409. doi: 10.1042/BJ20101442
PMID: 21269272

Froese, DS; Kochan, G; Muniz, JRC; Chaikuad, A; Wu, X; Gileadi, C; Ugochukwu, E; Krysztofinska, E; Gravel, RA; Oppermann, U; Yue, WW;
Journal of Inherited Metabolic Disease. 2011 34:S119-S119. doi:

Lee, WH; Raush, E; Totrov, M; Abagyan, R; Marsden, BD; Oppermann, U; Yue, WW;
Journal of Inherited Metabolic Disease. 2011 34:S240-S240. doi:

High-throughput structural biology of metabolic enzymes and its impact on human diseases.
Yue, WW; Oppermann, U;
Journal of Inherited Metabolic Disease. 2011 34:575-581. doi: 10.1007/s10545-011-9296-6
PMID: 21340633


Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation.
Froese, DS; Kochan, G; Muniz, JR; Wu, X; Gileadi, C; Ugochukwu, E; Krysztofinska, E; Gravel, RA; Oppermann, U; Yue, WW;
Journal of Biological Chemistry. 2010 285:38204-38213. doi: 10.1074/jbc.M110.177717
PMID: 20876572

Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment.
Healy, S; McDonald, MK; Wu, X; Yue, WW; Kochan, G; Oppermann, U; Gravel, RA;
Biochemistry. 2010 49:4687-4694. doi: 10.1021/bi901612y
PMID: 20443544

Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design.
Shafqat, N; Turnbull, A; Zschocke, J; Oppermann, U; Yue, WW;
Journal of Molecular Biology. 2010 398:497-506. doi: 10.1016/j.jmb.2010.03.034
PMID: 20346956

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase.
Yue, WW; Hozjan, V; Ge, W; Loenarz, C; Cooper, CD; Schofield, CJ; Kavanagh, KL; Oppermann, U; McDonough, MA;
FEBS Letters. 2010 584:825-830. doi: 10.1016/j.febslet.2009.12.055
PMID: 20067792


Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing.
Picaud, SS; Muniz, JR; Kramm, A; Pilka, ES; Kochan, G; Oppermann, U; Yue, WW;
Proteins: Structure, Function, and Bioinformatics. 2009 76:507-511. doi: 10.1002/prot.22411
PMID: 19360879

Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.
Kochan, G; Pilka, ES; von Delft, F; Oppermann, U; Yue, WW;
Journal of Molecular Biology. 2009 388:997-1008. doi: 10.1016/j.jmb.2009.03.064
PMID: 19345228

Dynamic protein methylation in chromatin biology.
Ng, SS; Yue, WW; Oppermann, U; Klose, RJ;
Cellular and Molecular Life Sciences. 2009 66:407-422. doi: 10.1007/s00018-008-8303-z
PMID: 18923809


Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture.
Hassler, M; Singh, S; Yue, WW; Luczynski, M; Lakbir, R; Sanchez-Sanchez, F; Bader, T; Pearl, LH; Mittnacht, S;
Molecular Cell. 2007 28:371-385. doi: 10.1016/j.molcel.2007.08.023
PMID: 17996702

Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase.
Yue, WW; Hassler, M; Roe, SM; Thompson-Vale, V; Pearl, LH;
The EMBO Journal. 2007 26:4402-4412. doi: 10.1038/sj.emboj.7601856
PMID: 17882261


Recognition of iron-free siderophores by TonB-dependent iron transporters.
Schalk, IJ; Yue, WW; Buchanan, SK;
Molecular Microbiology. 2004 54:14-22. doi: 10.1111/j.1365-2958.2004.04241.x
PMID: 15458401


Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA.
Yue, WW; Grizot, S; Buchanan, SK;
Journal of Molecular Biology. 2003 332:353-368. doi:
PMID: 12948487

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