T.P. Ugarova, V.K. Lishko, N.P. Podolnikova, N. Okumura, S.M. Kerkulov, V.P. Yakubenko, V.C. Yee, S.T. Lord, and T.A. Haas. Sequence γ377-395(P2), but not γ190-202(P1), is the binding site for the αM I-domain of integrin αM β2 in the γC-domain of fibrinogen. Biochemistry 42: 9365-9373 (2003). [Medline]
P.R. Hall, Y.-F. Wang, R.E. Rivera-Hainaj, X. Zheng, M. Pustai-Carey, P.R. Carey, and V.C. Yee. Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. EMBO J., 22: 2334-2347 (2003).
[Medline]
V.K. Lishko, B. Kudryk, V.P. Yakubenko, V.C. Yee, and T.P. Ugarova. Regulated unmasking of the cryptic binding site for integrin αM β2 in the γC-domain of fibrinogen. Biochemistry 41:12942-12951 (2002).
[Medline]
X. Zheng, R.E. Rivera-Hainaj, Y. Zheng, M. Pusztai-Carey, P.R. Hall, V.C. Yee, & P.R. Carey. Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: Raman crystallographic evidence. Biochemistry 41:10741-10746 (2002).
[Medline]
K.J. Knaus, M. Morillas, W. Swietnicki, M. Malone, W.K. Surewicz, and V.C. Yee. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nature Struct. Biol. 8:770-774 (2001).
[Medline]
M. Souri, V.C. Yee, K. Kasai, T. Kaneshiro, K. Narasaki, G. Castaman, and A. Ichinose. Novel Y283C mutation of the A subunit for coagulation factor XIII: molecular modeling predicts its impaired protein folding and dimer formation. Br. J. Haematol. 113: 652-654 (2001).
[Medline]
V.P. Yakubenko, D.A. Solovjov, L. Zhang, V.C. Yee, E.F. Plow, and T.P. Ugarova. Identification of the binding site for fibrinogen recognition peptide γ383-395 within the αM I-domain of Integrin αM β2. J. Biol. Chem., 276: 13995-14003 (2001).
[Medline]
Y.-F. Wang, D.C. Hyatt, R.E. Rivera, P.R. Carey, and V.C. Yee. Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii. Acta Cryst., D57: 266-268 (2001).
[Medline]
A.G. Loewy, J. McDonagh, H. Mikkola, D.C. Teller, and V.C. Yee. Structure and function of Factor XIII, in “Hemostasis and Thrombosis” (Chapter 13, 4th edition, edited by R.W. Colman et al, 2001)
C. Sadasivan and V.C. Yee. Interaction of the factor XIII activation peptide with α-thrombin: Crystal structure of its enzyme-substrate analog complex. J. Biol. Chem., 47: 36942-36948 (2000).
[Medline]
F. van den Akker, X. Zhang, M. Miyagi, X. Huo, K.S. Misono, and V.C. Yee. Structure of the dimerized hormone binding domain of a guanylyl cyclase-coupled receptor. Nature 406: 101-104 (2000).
[Medline]
L. Muszbek, V.C. Yee, and Z. Hevessy. Blood coagulation factor XIII: Structure and function. Thromb. Res. 94: 271-305 (1999).
[Medline]
B.A. Fox, V.C. Yee, L.C. Pedersen, I. Le Trong, P.D. Bishop, R.E. Stenkamp, and D.C. Teller. Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by X-ray crystallography. J. Biol. Chem., 274: 4917-4923 (1999).
[Medline]
C.A. Behnke, V.C. Yee, I. Le Trong, L.C. Pedersen, R.E. Stenkamp, S.S. Kim, G.R. Reeck, and D.C. Teller. Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 Ĺ resolution. Biochemistry 37: 15277-15288 (1998).
[Medline]
T.P. Ugarova, D.A. Solovjov, L. Zhang, D.I. Loukinov, V.C. Yee, L.V. Medved, and E.F. Plow. Identification of a novel recognition sequence for integrin αM β2 within the γ-chain of fibrinogen. J. Biol. Chem., 273: 22519-22527 (1998).
[Medline]
O.V. Mitkevich, J.R. Shainoff, P.M. DiBello, V.C. Yee, D.C. Teller, G.B. Smejkal, P.D. Bishop, I.S. Kolotushkina, K. Fickenscher, and G.P. Samokhin. Coagulation factor XIIIa undergoes a conformational change evoked by glutamine substrate. Studies on kinetics of inhibition and binding of XIIIa by a cross-reacting anti-fibrinogen antibody. J. Biol. Chem., 273: 14387-14391 (1998).
[Medline]
E. Laiho, J. Ignatius, H. Mikkola, V.C. Yee, D.C. Teller, K-M. Niemi, U. Saarialho-Kere, J. Kere, and A. Palotie. Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis: Private and recurrent mutations in an isolated population. Am. J. Hum. Gen., 61: 529-538 (1997).[Medline]
S.E. Iismaa, L. Chung, M.-J. Wu, D.C. Teller, V.C. Yee, and R.M. Graham. The core domain of the tissue transglutaminase Gh hydrolyses GTP and ATP. Biochemistry, 36: 11655-11664 (1997).
[Medline]
M. Huber, V.C. Yee, N. Burri, Eva Vikerfors, Adriana P. M. Lavrijsen, Amy S. Paller, and D. Hohl. Novel Mutations in Keratinocyte Transglutaminase in Four Lamellar Ichthyosis Families. J. Biol. Chem., 272: 21018-21026 (1997)
[Medline]
S. Aslam, V.C. Yee, S. Narayanan, G. Duraisamy, and G.R. Standen. Structural analysis of a missense mutation (Val414Phe) in the catalytic core domain of the factor XIIIA subunit. Br. J. Haematol. 98: 346-352 (1997).
[Medline]
A. Inbal, V.C. Yee, N. Kornbrot, A. Zivelin, B. Brenner, and U. Seligsohn. Factor XIII deficiency due to a Leu660Pro mutation in the factor XIII subunit-a gene in three unrelated Palestinian Arab families. Thromb Hemost. 77: 1062-1067 (1997).
[Medline]
V.C. Yee, K.P. Pratt, H.C.F. Cote, I. Le Trong, D.W. Chung, E.W. Davie, R.E. Stenkamp, and D.C. Teller. Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen. Structure 5: 125-138 (1997).
[Medline]
V.C. Yee, I. Le Trong, P.D. Bishop, L.C. Pedersen, R.E. Stenkamp, and D.C. Teller. Structure and function studies of factor XIII A-subunit by X-ray crystallography. Sem. Thromb. Haemost, 22: 377-384 (1996).
H. Mikkola, V.C. Yee, M. Syrjala, R. Seitz, R. Egbring, P. Petrini, R. Ljung, D.C. Teller, L. Peltonen, and A. Palotie. Four novel mutations in deficiency of coagulation factor XIII: consequences to expression and structure of the A-subunit. Blood, 87: 141-151 (1996).[Medline]
S. Aslam, M-C. Poon, V. Yee, D.J. Bowen, G.R. Standen. Factor XIIIA Calgary: a candidate missense mutation (Leu667Pro) in the β barrel 2 domain of the factor XIIIA subunit. Br. J. Haematol., 91: 452-457 (1995).
[Medline]
V.C. Yee, L.C. Pedersen, P.D. Bishop, R.E. Stenkamp, D.C. Teller. Structural Evidence that the activation peptide is not released upon thrombin cleavage of Factor XIII. Throm. Res., 78: 389-397 (1995).[Medline]
I.V. Kurochkin, R. Procyk, P.D. Bishop, V.C. Yee, D.C. Teller, K.C. Ingham, and L.V. Medved. Domain structure, stability, and domain-domain interactions in recombinant Factor XIII. J. Mol. Biol., 248: 414-430 (1995).
[Medline]
P. Legzdins, E.C. Phillips, J. Trotter, and V.C. Yee. (η5-cyclopentadienyl)-oxo(peroxo-O, O')(trimethylsilylmethyl)tungsten and the related (η5-pentamethylcyclopentadienyl)-oxo(peroxo-O,O')(trimethylsilylmethyl)-tungsten-tetracyanoethylene(2/1) complex. Acta Cryst., C51: 2498-2501 (1995).
N. Brunet, P. Legzdins, J. Trotter, and V.C. Yee. Structure of a tungsten complex. Acta Cryst., C51: 193-195 (1995).
V.C. Yee, L.C. Pedersen, I. Le Trong, P.D. Bishop, R.E. Stenkamp, and D.C. Teller. Three dimensional structure of a transglutaminase: Human blood coagulation Factor XIII. PNAS USA, 91: 7296-300 (1994). [Medline]
L.C. Pedersen, V.C. Yee, P.D. Bishop, I. Le Trong, D.C. Teller, and R.E. Stenkamp. Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Protein Science, 3: 1131-1135 (1994). [Medline]
L.C. Pedersen, V.C. Yee, G. von Dassow, M. Hazeghazam, G.R. Reeck, R.E. Stenkamp, and D.C. Teller. The corn inhibitor of blood coagulation Factor XIIa: Crystallization and preliminary crystallographic analysis. J. Mol. Biol., 236: 385-387 (1994). [Medline]
N.J. Christensen, P. Legzdins, J. Trotter, and V.C. Yee. Structure of Di-μ-chloro-bis(cyclopentadienyl)nitrosyl molybdenum. Acta Cryst., C50: 1558-1559 (1994).
S.V. Evans, V.C. Yee, M. Garcia-Garibay, and J. Trotter. Structure of a Mixed Crystal of α- and β-Pipitzol (1:1), C15H20O3.C15H20O3. Acta Cryst., C50:278-281 (1994).
T-P. Wu, V.C. Yee, A. Tulinsky, R.A. Crusciel, H. Nakanishi, R. Schen, C. Priebe, and M. Kahn. The structure of a designed peptidomimetic inhibitor complex of α-thrombin. Prot. Eng., 6: 471-478 (1993).
J. Trotter and V.C. Yee. Structure of dimethyl-9-chloro-9,10-dihydro-9,10-ethenoanthracene-11,12-
dicarboxylate. Acta Cryst., C49: 846-848 (1993).
N. Brunet, J.D. Debad, P. Legzdins, J. Trotter, J.E. Veltheer, and V.C. Yee. Novel route to the unsymmetrical dialkyl complex CpW(NO)(CH2SiMe2)(CH2CPh3) and formation of metallacycles by thermolysis of CpW(NO)(CH2SiMe2)(CH2CR2Ph) (R=Me,Ph). Organometallics, 12: 4572-4579 (1993).
P. Legzdins, E.C. Phillips, S.J. Rettig, J. Trotter, J.E. Veltheer, and V.C. Yee. Reactivity of Cp*W(O)2 (CH2SiMe2) toward p-tolyl isocyanate: Cycloaddition reactions of tungsten-oxo and -imido linkages. Organometallics, 11: 3104-3110 (1992).
T.T. Chin, P. Legzdins, J. Trotter, and V.C. Yee. New organometallic nitrosyl cations containing the group 6 Elements. Organometallics, 11: 913-922 (1992).
N.J. Christensen, P. Legzdins, J. Trotter, and V.C. Yee. Reactivities of representative cyclopentadienyl(η4 -trans-diene)-nitrosyl complexes of molybdenum toward acetone. Organometallics, 10: 4021-4030 (1991).
N.H. Dryden, P. Legzdins, J. Trotter, and V.C. Yee. Synthesis and Characterization of Chiral Molybdenum and Tungsten Neutral Complexes Containing η²-Benzyl Ligands. Organometallics, 10: 2857-2870 (1991).
P. Legzdins, R.H. Jones, E.C. Phillips, V.C. Yee, J. Trotter, and F.W.B. Einstein. Synthesis, characterization, and physical properties of unusual cyclopentadienyl bis(benzyl) nitrosyl complexes of molybdenum and tungsten. Organometallics, 10: 986-1002 (1991).
N.H. Dryden, P. Legzdins, E.C. Phillips, J. Trotter, and V.C. Yee. Unambiguous Example of an η²-benzyl group functioning as a formal three-electron ligand: Solid-state molecular structure of Cp*Mo(NO)(CH2SiMe2)(η²-CH2C6 H5). Organometallics, 9: 882-884 (1990).
P. Legzdins, E.C. Phillips, S.J. Rettig, L. Sanchez, J. Trotter, and V.C. Yee. Remarkably inert metal-alkyl linkages in alkyl dioxo complexes of molybdenum and tungsten. Organometallics, 7: 1877-1878 (1988).
S.V. Evans, J. Trotter, and V.C. Yee. Structure of bis [(-)-menthyl] acetylenedicarboxylate. Acta Cryst., C44: 878-880 (1988).