{"id":283,"date":"2017-01-18T12:51:59","date_gmt":"2017-01-18T11:51:59","guid":{"rendered":"http:\/\/lbti.cnrs.fr\/?page_id=283"},"modified":"2022-03-18T18:21:12","modified_gmt":"2022-03-18T17:21:12","slug":"test-2-2","status":"publish","type":"page","link":"https:\/\/lbti.ibcp.fr\/?page_id=283","title":{"rendered":"Publications"},"content":{"rendered":"59 publications trouv\u00e9es.

2024<\/a>
59.<\/b><\/font>\u00a0\u00a0Mono- and Bi-specific Nanobodies Targeting the CUB Domains of PCPE-1 Reduce the Proteolytic Processing of Fibrillar Procollagens.<\/b><\/font>\u00a0
Lagoutte P, Bourhis Jm, Mariano N, Gueguen-chaignon V, Vandroux D, Moali C, Vadon-le Goff S
(2024)\u00a0J Mol Biol<\/b>\u00a0436<\/u> :168667-168667\u00a0\u00a0\"Icon<\/a>

58.<\/b><\/font>\u00a0\u00a0PCPE-2 (procollagen C-proteinase enhancer-2): The non-identical twin of PCPE-1.<\/b><\/font>\u00a0
Napoli M, Bauer J, Bonod C, Vadon-le Goff S, Moali C
(2024)\u00a0Matrix Biol<\/b>\u00a0134<\/u> :59-78\u00a0\u00a0\"Icon<\/a>

2023<\/a>
57.<\/b><\/font>\u00a0\u00a0Designed Ankyrin Repeat Proteins provide insights into the structure and function of CagI and are potent inhibitors of CagA translocation by the Helicobacter pylori type IV secretion system.<\/b><\/font>\u00a0
Blanc M, Lettl C, Gu\u00e9rin J, Vieille A, Furler S, Briand-schumacher S, Dreier B, Berg\u00e9 C, Pl\u00fcckthun A, Vadon-le Goff S, Fronzes R, Rousselle P, Fischer W, Terradot L
(2023)\u00a0Plos Pathog<\/b>\u00a019<\/u> :e1011368-e1011368\u00a0\u00a0\"Icon<\/a>

56.<\/b><\/font>\u00a0\u00a0Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1\/tolloid-like proteinases.<\/b><\/font>\u00a0
Vadon-le Goff S, Tessier A, Napoli M, Dieryckx C, Bauer J, Dussoyer M, Lagoutte P, Peyronnel C, Essayan L, Kleiser S, Tueni N, Bettler E, Mariano N, Errazuriz-cerda E, Fruchart Gaillard C, Ruggiero F, Becker-pauly C, Allain Jm, Bruckner-tuderman L, Nystr\u00f6m A, Moali C
(2023)\u00a0Nat Commun<\/b>\u00a014<\/u> :8020-8020\u00a0\u00a0\"Icon<\/a>

2022<\/a>
55.<\/b><\/font>\u00a0\u00a0Comparison of extracellular matrix enrichment protocols for the improved characterization of the skin matrisome by mass spectrometry.<\/b><\/font>\u00a0
Dussoyer M, Page A, Delolme F, Rousselle P, Nystr\u00f6m A, Moali C
(2022)\u00a0J Proteomics<\/b>\u00a0251<\/u> :104397-104397\u00a0\u00a0\"Icon<\/a>

54.<\/b><\/font>\u00a0\u00a0Dynamics of the secreted frizzled related protein Sizzled and potential implications for binding to bone morphogenetic protein-1 (BMP-1).<\/b><\/font>\u00a0
Sharma U, Vadon-le Goff S, Harlos K, Zhao Y, Mariano N, Bijakowski C, Bourhis Jm, Moali C, Hulmes Djs, Aghajari N
(2022)\u00a0Sci Rep<\/b>\u00a012<\/u> :14850-14850\u00a0\u00a0\"Icon<\/a>

2021<\/a>
53.<\/b><\/font>\u00a0\u00a0A 9-kDa matricellular SPARC fragment released by cathepsin D exhibits pro-tumor activity in the triple-negative breast cancer microenvironment.<\/b><\/font>\u00a0
Alcaraz Lb, Mallavialle A, David T, Derocq D, Delolme F, Dieryckx C, Mollevi C, Boissi\u00e8re-michot F, Simony-lafontaine J, Du Manoir S, Huesgen Pf, Overall Cm, Tartare-deckert S, Jacot W, Chard\u00e8s T, Guiu S, Roger P, Reinheckel T, Moali C, Liaudet-coopman E
(2021)\u00a0Theranostics<\/b>\u00a011<\/u> :6173-6192\u00a0\u00a0\"Icon<\/a>

52.<\/b><\/font>\u00a0\u00a0Latent TGF-\u03b2 Activation Is a Hallmark of the Tenascin Family.<\/b><\/font>\u00a0
Aubert A, Mercier-gouy P, Aguero S, Berthier L, Liot S, Prigent L, Alcaraz Lb, Verrier B, Terreux R, Moali C, Lambert E, Valcourt U
(2021)\u00a0Front Immunol<\/b>\u00a012<\/u> :613438-613438\u00a0\u00a0\"Icon<\/a>

51.<\/b><\/font>\u00a0\u00a0Targeting Ovarian Carcinoma with TSP-1:CD47 Antagonist TAX2 Activates Anti-Tumor Immunity.<\/b><\/font>\u00a0
Jeanne A, Sarazin T, Charl\u00e9 M, Moali C, Fichel C, Boulagnon-rombi C, Callewaert M, Andry Mc, Diesis E, Delolme F, Rioult D, Dedieu S
(2021)\u00a0Cancers (basel)<\/b>\u00a013<\/u> :\u00a0\u00a0\"Icon<\/a>

50.<\/b><\/font>\u00a0\u00a0Procollagen C-proteinase enhancer-1 (PCPE-1), a potential biomarker and therapeutic target for fibrosis.<\/b><\/font>\u00a0
Lagoutte P, Bettler E, Vadon-le Goff S, Moali C
(2021)\u00a0Matrix Biol Plus<\/b>\u00a011<\/u> :100062-100062\u00a0\u00a0\"Icon<\/a>

2020<\/a>
49.<\/b><\/font>\u00a0\u00a0BMP-1 disrupts cell adhesion and enhances TGF-\u03b2 activation through cleavage of the matricellular protein thrombospondin-1.<\/b><\/font>\u00a0
Anastasi C, Rousselle P, Talantikite M, Tessier A, Cluzel C, Bachmann A, Mariano N, Dussoyer M, Alcaraz Lb, Fortin L, Aubert A, Delolme F, El Kholti N, Armengaud J, Fourni\u00e9 P, Auxenfans C, Valcourt U, Goff Sv, Moali C
(2020)\u00a0Sci Signal<\/b>\u00a013<\/u> :\u00a0\u00a0\"Icon<\/a>

48.<\/b><\/font>\u00a0\u00a0Degradome of soluble ADAM10 and ADAM17 metalloproteases.<\/b><\/font>\u00a0
Scharfenberg F, Helbig A, Sammel M, Benzel J, Schlomann U, Peters F, Wichert R, Bettendorff M, Schmidt-arras D, Rose-john S, Moali C, Lichtenthaler Sf, Pietrzik Cu, Bartsch Jw, Tholey A, Becker-pauly C
(2020)\u00a0Cell Mol Life Sci<\/b>\u00a077<\/u> :331-350\u00a0\u00a0\"Icon<\/a>

2019<\/a>
47.<\/b><\/font>\u00a0\u00a0COL1A1 C-propeptide mutations cause ER mislocalization of procollagen and impair C-terminal procollagen processing.<\/b><\/font>\u00a0
Barnes Am, Ashok A, Makareeva En, Brusel M, Cabral Wa, Weis M, Moali C, Bettler E, Eyre Dr, Cassella Jp, Leikin S, Hulmes Djs, Kessler E, Marini Jc
(2019)\u00a0Biochim Biophys Acta Mol Basis Dis<\/b>\u00a0<\/u> :\u00a0\u00a0\"Icon<\/a>

46.<\/b><\/font>\u00a0\u00a0A scaffold- and serum-free method to mimic human stable cartilage validated by secretome.<\/b><\/font>\u00a0
Cortes I, Matsui Ram, Azevedo Ms, Beatrici A, Souza Kla, Launay G, Delolme F, Granjeiro Jm, Moali C, Baptista Ls
(2019)\u00a0Tissue Eng Part A<\/b>\u00a0<\/u> :\u00a0\u00a0\"Icon<\/a>

45.<\/b><\/font>\u00a0\u00a0C-terminal proteolysis of the collagen VI \u03b13 chain by BMP-1 and proprotein convertase(s) releases endotrophin in fragments of different sizes.<\/b><\/font>\u00a0
Heumuller Se, Talantikite M, Napoli M, Armengaud J, Morgelin M, Hartmann U, Sengle G, Paulsson M, Moali C, Wagener R
(2019)\u00a0J Biol Chem<\/b>\u00a0294<\/u> :13769-13780\u00a0\u00a0\"Icon<\/a>

2018<\/a>
44.<\/b><\/font>\u00a0\u00a0Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1.<\/b><\/font>\u00a0
Pulido D, Sharma U, Vadon-le Goff S, Hussain Sa, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes Djs
(2018)\u00a0Structure<\/b>\u00a0<\/u> :\u00a0\u00a0\"Icon<\/a>

43.<\/b><\/font>\u00a0\u00a0Inhibitors of BMP-1\/tolloid-like proteinases: efficacy, selectivity and cellular toxicity.<\/b><\/font>\u00a0
Talantikite M, Lecorche P, Beau F, Damour O, Becker-pauly C, Ho Wb, Dive V, Vadon-le Goff S, Moali C
(2018)\u00a0Febs Open Bio<\/b>\u00a08<\/u> :2011-2021\u00a0\u00a0\"Icon<\/a>

2017<\/a>
42.<\/b><\/font>\u00a0\u00a0Deficiency of the DSPP-cleaving enzymes meprin ? and meprin ? does not result in dentin malformation in mice.<\/b><\/font>\u00a0
Arnold P, Koopmann L, Peters F, Birkenfeld F, Goff Sv, Damm T, Qin C, Moali C, Lucius R, Becker-pauly C
(2017)\u00a0Cell Tissue Res<\/b>\u00a0367<\/u> :351-358\u00a0\u00a0\"Icon<\/a>

41.<\/b><\/font>\u00a0\u00a0Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1\/Tolloid-like Proteinases.<\/b><\/font>\u00a0
Lacroix M, Tessier A, Dumestre-perard C, Vadon-le Goff S, Gout E, Bruckner-tuderman L, Kiritsi D, Nystrom A, Ricard-blum S, Moali C, Hulmes Djs, Thielens Nm
(2017)\u00a0Sci Rep<\/b>\u00a07<\/u> :16958-16958\u00a0\u00a0\"Icon<\/a>

40.<\/b><\/font>\u00a0\u00a0Structural basis of homo- and heterotrimerization of collagen I.<\/b><\/font>\u00a0
Sharma U, Carrique L, Vadon-le Goff S, Mariano N, Georges Rn, Delolme F, Koivunen P, Myllyharju J, Moali C, Aghajari N, Hulmes Dj
(2017)\u00a0Nat Commun<\/b>\u00a08<\/u> :14671-14671\u00a0\u00a0\"Icon<\/a>

2016<\/a>
39.<\/b><\/font>\u00a0\u00a0Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-? signaling as primary targets.<\/b><\/font>\u00a0
Bekhouche M, Leduc C, Dupont L, Janssen L, Delolme F, Vadon-le Goff S, Smargiasso N, Baiwir D, Mazzucchelli G, Zanella-cleon I, Dubail J, De Pauw E, Nusgens B, Hulmes Dj, Moali C, Colige A
(2016)\u00a0Faseb J<\/b>\u00a030<\/u> :1741-56\u00a0\u00a0\"Icon<\/a>

38.<\/b><\/font>\u00a0\u00a0Characterization of post-translational modifications in full-length human BMP-1 confirms the presence of a rare vicinal disulfide linkage in the catalytic domain and highlights novel features of the EGF domain.<\/b><\/font>\u00a0
Hung Cw, Koudelka T, Anastasi C, Becker A, Moali C, Tholey A
(2016)\u00a0J Proteomics<\/b>\u00a0138<\/u> :136-45\u00a0\u00a0\"Icon<\/a>

2015<\/a>
37.<\/b><\/font>\u00a0\u00a0Proteolytic control of TGF-? co-receptor activity by BMP-1\/tolloid-like proteases revealed by quantitative iTRAQ proteomics.<\/b><\/font>\u00a0
Delolme F, Anastasi C, Alcaraz Lb, Mendoza V, Vadon-le Goff S, Talantikite M, Capomaccio R, Mevaere J, Fortin L, Mazzocut D, Damour O, Zanella-cleon I, Hulmes Dj, Overall Cm, Valcourt U, Lopez-casillas F, Moali C
(2015)\u00a0Cell Mol Life Sci<\/b>\u00a072<\/u> :1009-27\u00a0\u00a0\"Icon<\/a>

36.<\/b><\/font>\u00a0\u00a0BMP-1\/tolloid-like proteinases synchronize matrix assembly with growth factor activation to promote morphogenesis and tissue remodeling.<\/b><\/font>\u00a0
Vadon-le Goff S, Hulmes Dj, Moali C
(2015)\u00a0Matrix Biol<\/b>\u00a044-46<\/u> :14-23\u00a0\u00a0\"Icon<\/a>

2014<\/a>
35.<\/b><\/font>\u00a0\u00a0Upregulation of bone morphogenetic protein-1\/mammalian tolloid and procollagen C-proteinase enhancer-1 in corneal scarring.<\/b><\/font>\u00a0
Malecaze F, Massoudi D, Fournie P, Tricoire C, Cassagne M, Malbouyres M, Hulmes Dj, Moali C, Galiacy Sd
(2014)\u00a0Invest Ophthalmol Vis Sci<\/b>\u00a055<\/u> :6712-21\u00a0\u00a0\"Icon<\/a>

2013<\/a>
34.<\/b><\/font>\u00a0\u00a0Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.<\/b><\/font>\u00a0
Bourhis Jm, Vadon-le Goff S, Afrache H, Mariano N, Kronenberg D, Thielens N, Moali C, Hulmes Dj
(2013)\u00a0Proc Natl Acad Sci U S A<\/b>\u00a0110<\/u> :6394-9\u00a0\u00a0\"Icon<\/a>

33.<\/b><\/font>\u00a0\u00a0Metalloproteases meprin ? and meprin ? are C- and N-procollagen proteinases important for collagen assembly and tensile strength.<\/b><\/font>\u00a0
Broder C, Arnold P, Vadon-le Goff S, Konerding Ma, Bahr K, Muller S, Overall Cm, Bond Js, Koudelka T, Tholey A, Hulmes Dj, Moali C, Becker-pauly C
(2013)\u00a0Proc Natl Acad Sci U S A<\/b>\u00a0110<\/u> :14219-24\u00a0\u00a0\"Icon<\/a>

2012<\/a>
32.<\/b><\/font>\u00a0\u00a0Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)\/tolloid-like proteinases.<\/b><\/font>\u00a0
Bijakowski C, Vadon-le Goff S, Delolme F, Bourhis Jm, Lecorche P, Ruggiero F, Becker-pauly C, Yiallouros I, Stocker W, Dive V, Hulmes Dj, Moali C
(2012)\u00a0J Biol Chem<\/b>\u00a0287<\/u> :33581-93\u00a0\u00a0\"Icon<\/a>

31.<\/b><\/font>\u00a0\u00a0Structural basis of fibrillar collagen trimerization and related genetic disorders.<\/b><\/font>\u00a0
Bourhis Jm, Mariano N, Zhao Y, Harlos K, Exposito Jy, Jones Ey, Moali C, Aghajari N, Hulmes Dj
(2012)\u00a0Nat Struct Mol Biol<\/b>\u00a019<\/u> :1031-6\u00a0\u00a0\"Icon<\/a>

30.<\/b><\/font>\u00a0\u00a0Production and crystallization of the C-propeptide trimer from human procollagen III.<\/b><\/font>\u00a0
Bourhis Jm, Mariano N, Zhao Y, Walter Ts, El Omari K, Delolme F, Moali C, Hulmes Dj, Aghajari N
(2012)\u00a0Acta Crystallogr Sect F Struct Biol Cryst Commun<\/b>\u00a068<\/u> :1209-13\u00a0\u00a0\"Icon<\/a>

29.<\/b><\/font>\u00a0\u00a0Development of ex vivo organ culture models to mimic human corneal scarring.<\/b><\/font>\u00a0
Janin-manificat H, Rovere Mr, Galiacy Sd, Malecaze F, Hulmes Dj, Moali C, Damour O
(2012)\u00a0Mol Vis<\/b>\u00a018<\/u> :2896-908\u00a0\u00a0\"Icon<\/a>

2011<\/a>
28.<\/b><\/font>\u00a0\u00a0Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide region only.<\/b><\/font>\u00a0
Vadon-le Goff S, Kronenberg D, Bourhis Jm, Bijakowski C, Raynal N, Ruggiero F, Farndale Rw, Stocker W, Hulmes Dj, Moali C
(2011)\u00a0J Biol Chem<\/b>\u00a0286<\/u> :38932-8\u00a0\u00a0\"Icon<\/a>

2010<\/a>
27.<\/b><\/font>\u00a0\u00a0Role of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity.<\/b><\/font>\u00a0
Bekhouche M, Kronenberg D, Vadon-le Goff S, Bijakowski C, Lim Nh, Font B, Kessler E, Colige A, Nagase H, Murphy G, Hulmes Dj, Moali C
(2010)\u00a0J Biol Chem<\/b>\u00a0285<\/u> :15950-9\u00a0\u00a0\"Icon<\/a>

26.<\/b><\/font>\u00a0\u00a0Processing of procollagen III by meprins: new players in extracellular matrix assembly?<\/b><\/font>\u00a0
Kronenberg D, Bruns Bc, Moali C, Vadon-le Goff S, Sterchi Ee, Traupe H, Bohm M, Hulmes Dj, Stocker W, Becker-pauly C
(2010)\u00a0J Invest Dermatol<\/b>\u00a0130<\/u> :2727-35\u00a0\u00a0\"Icon<\/a>

2009<\/a>
25.<\/b><\/font>\u00a0\u00a0Strong cooperativity and loose geometry between CUB domains are the basis for procollagen c-proteinase enhancer activity.<\/b><\/font>\u00a0
Kronenberg D, Vadon-le Goff S, Bourhis Jm, Font B, Eichenberger D, Hulmes Dj, Moali C
(2009)\u00a0J Biol Chem<\/b>\u00a0284<\/u> :33437-46\u00a0\u00a0\"Icon<\/a>

24.<\/b><\/font>\u00a0\u00a0Extracellular and cell surface proteases in wound healing: new players are still emerging.<\/b><\/font>\u00a0
Moali C, Hulmes Dj
(2009)\u00a0Eur J Dermatol<\/b>\u00a019<\/u> :552-64\u00a0\u00a0\"Icon<\/a>

2007<\/a>
23.<\/b><\/font>\u00a0\u00a0Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity.<\/b><\/font>\u00a0
Blanc G, Font B, Eichenberger D, Moreau C, Ricard-blum S, Hulmes Dj, Moali C
(2007)\u00a0J Biol Chem<\/b>\u00a0282<\/u> :16924-33\u00a0\u00a0\"Icon<\/a>

2005<\/a>
22.<\/b><\/font>\u00a0\u00a0Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1.<\/b><\/font>\u00a0
Moali C, Font B, Ruggiero F, Eichenberger D, Rousselle P, Francois V, Oldberg A, Bruckner-tuderman L, Hulmes Dj
(2005)\u00a0J Biol Chem<\/b>\u00a0280<\/u> :24188-94\u00a0\u00a0\"Icon<\/a>

2003<\/a>
21.<\/b><\/font>\u00a0\u00a0Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis.<\/b><\/font>\u00a0
Moali C, Anne C, Lamotte-brasseur J, Groslambert S, Devreese B, Van Beeumen J, Galleni M, Frere Jm
(2003)\u00a0Chem Biol<\/b>\u00a010<\/u> :319-29\u00a0\u00a0\"Icon<\/a>

2002<\/a>
20.<\/b><\/font>\u00a0\u00a0Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1.<\/b><\/font>\u00a0
Ricard-blum S, Bernocco S, Font B, Moali C, Eichenberger D, Farjanel J, Burchardt Er, Van Der Rest M, Kessler E, Hulmes Dj
(2002)\u00a0J Biol Chem<\/b>\u00a0277<\/u> :33864-9\u00a0\u00a0\"Icon<\/a>

2001<\/a>
19.<\/b><\/font>\u00a0\u00a0CENTA as a chromogenic substrate for studying beta-lactamases.<\/b><\/font>\u00a0
Bebrone C, Moali C, Mahy F, Rival S, Docquier Jd, Rossolini Gm, Fastrez J, Pratt Rf, Frere Jm, Galleni M
(2001)\u00a0Antimicrob Agents Chemother<\/b>\u00a045<\/u> :1868-71\u00a0\u00a0\"Icon<\/a>

18.<\/b><\/font>\u00a0\u00a0Oxidations of N(omega)-hydroxyarginine analogues and various N-hydroxyguanidines by NO synthase II: key role of tetrahydrobiopterin in the reaction mechanism and substrate selectivity.<\/b><\/font>\u00a0
Moali C, Boucher Jl, Renodon-corniere A, Stuehr Dj, Mansuy D
(2001)\u00a0Chem Res Toxicol<\/b>\u00a014<\/u> :202-10\u00a0\u00a0\"Icon<\/a>

17.<\/b><\/font>\u00a0\u00a0Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: kinetic and spectroscopic studies.<\/b><\/font>\u00a0
Mollard C, Moali C, Papamicael C, Damblon C, Vessilier S, Amicosante G, Schofield Cj, Galleni M, Frere Jm, Roberts Gc
(2001)\u00a0J Biol Chem<\/b>\u00a0276<\/u> :45015-23\u00a0\u00a0\"Icon<\/a>

16.<\/b><\/font>\u00a0\u00a0Coordination chemistry of the heme in cystathionine beta-synthase: formation of iron(II)-isonitrile complexes.<\/b><\/font>\u00a0
Vadon-le Goff S, Delaforge M, Boucher Jl, Janosik M, Kraus Jp, Mansuy D
(2001)\u00a0Biochem Biophys Res Commun<\/b>\u00a0283<\/u> :487-92\u00a0\u00a0\"Icon<\/a>

2000<\/a>
15.<\/b><\/font>\u00a0\u00a0Modulation of cholinergic airway reactivity and nitric oxide production by endogenous arginase activity.<\/b><\/font>\u00a0
Meurs H, Hamer Ma, Pethe S, Vadon-le Goff S, Boucher Jl, Zaagsma J
(2000)\u00a0Br J Pharmacol<\/b>\u00a0130<\/u> :1793-8\u00a0\u00a0\"Icon<\/a>

1999<\/a>
14.<\/b><\/font>\u00a0\u00a0Nitric oxide biosynthesis, nitric oxide synthase inhibitors and arginase competition for L-arginine utilization.<\/b><\/font>\u00a0
Boucher Jl, Moali C, Tenu Jp
(1999)\u00a0Cell Mol Life Sci<\/b>\u00a055<\/u> :1015-28\u00a0\u00a0\"Icon<\/a>

1998<\/a>
13.<\/b><\/font>\u00a0\u00a0Substrate specificity of NO synthases: detailed comparison of L-arginine, homo-L-arginine, their N omega-hydroxy derivatives, and N omega-hydroxynor-L-arginine.<\/b><\/font>\u00a0
Moali C, Boucher Jl, Sari Ma, Stuehr Dj, Mansuy D
(1998)\u00a0Biochemistry<\/b>\u00a037<\/u> :10453-60\u00a0\u00a0\"Icon<\/a>

12.<\/b><\/font>\u00a0\u00a0Detection of a nitric oxide synthase possibly involved in the regulation of the Rhodococcus sp R312 nitrile hydratase.<\/b><\/font>\u00a0
Sari Ma, Moali C, Boucher Jl, Jaouen M, Mansuy D
(1998)\u00a0Biochem Biophys Res Commun<\/b>\u00a0250<\/u> :364-8\u00a0\u00a0\"Icon<\/a>

11.<\/b><\/font>\u00a0\u00a0Biosynthesis of NO: mechanism, regulation and control<\/b><\/font>\u00a0
Sennequier N, Vadon-le Goff S
(1998)\u00a0M S-medecine Sciences<\/b>\u00a014<\/u> :1185-1195

1997<\/a>
10.<\/b><\/font>\u00a0\u00a0Highly efficient control of iron-containing nitrile hydratases by stoichiometric amounts of nitric oxide and light.<\/b><\/font>\u00a0
Bonnet D, Artaud I, Moali C, Petre D, Mansuy D
(1997)\u00a0Febs Lett<\/b>\u00a0409<\/u> :216-20\u00a0\u00a0\"Icon<\/a>

9.<\/b><\/font>\u00a0\u00a0N-omega-OH-D,L-indospicine, a potent and selective: Inhibitor of arginase in rat and rabbit alveolar macrophages (AM phi) can promote utilization of L-arginine by nitric oxide synthase (NOS)<\/b><\/font>\u00a0
Hey C, Boucher Jl, Vadon S, Ketterer G, Stichnote C, Wessler I, Racke K
(1997)\u00a0British Journal Of Pharmacology<\/b>\u00a0120<\/u> :P48-P48

8.<\/b><\/font>\u00a0\u00a0Inhibition of arginase in rat and rabbit alveolar macrophages by N omega-hydroxy-D,L-indospicine, effects on L-arginine utilization by nitric oxide synthase.<\/b><\/font>\u00a0
Hey C, Boucher Jl, Vadon-le Goff S, Ketterer G, Wessler I, Racke K
(1997)\u00a0Br J Pharmacol<\/b>\u00a0121<\/u> :395-400\u00a0\u00a0\"Icon<\/a>

1996<\/a>
7.<\/b><\/font>\u00a0\u00a0Expression in yeast and purification of functional macrophage nitric oxide synthase. Evidence for cysteine-194 as iron proximal ligand.<\/b><\/font>\u00a0
Sari Ma, Booker S, Jaouen M, Vadon S, Boucher Ji, Pompon D, Mansuy D
(1996)\u00a0Biochemistry<\/b>\u00a035<\/u> :7204-13\u00a0\u00a0\"Icon<\/a>

6.<\/b><\/font>\u00a0\u00a0Synthesis and effects on arginase and nitric oxide synthase of two novel analogues of N omega-hydroxyarginine, N omega-hydroxyindospicine and p-hydroxyamidinophenylalanine<\/b><\/font>\u00a0
Vadon S, Custot J, Boucher Jl, Mansuy D
(1996)\u00a0Journal Of The Chemical Society-perkin Transactions 1<\/b>\u00a0<\/u> :645-648

1994<\/a>
5.<\/b><\/font>\u00a0\u00a0N omega-hydroxyl-L-arginine, an intermediate in the L-arginine to nitric oxide pathway, is a strong inhibitor of liver and macrophage arginase.<\/b><\/font>\u00a0
Boucher Jl, Custot J, Vadon S, Delaforge M, Lepoivre M, Tenu Jp, Yapo A, Mansuy D
(1994)\u00a0Biochem Biophys Res Commun<\/b>\u00a0203<\/u> :1614-21\u00a0\u00a0\"Icon<\/a>

4.<\/b><\/font>\u00a0\u00a0N-OMEGA-HYDROXY-L-ARGININE, AN INTERMEDIATE IN THE L-ARGININE TO NITRIC-OXIDE PATHWAY, IS A STRONG INHIBITOR OF LIVER AND MACROPHAGE ARGINASE<\/b><\/font>\u00a0
Boucher Jl, Custot J, Vadon S, Delaforge M, Lepoivre M, Tenu Jp, Yapo A, Mansuy D
(1994)\u00a0Biochemical And Biophysical Research Communications<\/b>\u00a0203<\/u> :1614-1621

1993<\/a>
3.<\/b><\/font>\u00a0\u00a0Particular ability of liver P450s3A to catalyze the oxidation of N omega-hydroxyarginine to citrulline and nitrogen oxides and occurrence in no synthases of a sequence very similar to the heme-binding sequence in P450s.<\/b><\/font>\u00a0
Renaud Jp, Boucher Jl, Vadon S, Delaforge M, Mansuy D
(1993)\u00a0Biochem Biophys Res Commun<\/b>\u00a0192<\/u> :53-60\u00a0\u00a0\"Icon<\/a>

1992<\/a>
2.<\/b><\/font>\u00a0\u00a0Cytochrome P450 catalyzes the oxidation of N omega-hydroxy-L-arginine by NADPH and O2 to nitric oxide and citrulline.<\/b><\/font>\u00a0
Boucher Jl, Genet A, Vadon S, Delaforge M, Henry Y, Mansuy D
(1992)\u00a0Biochem Biophys Res Commun<\/b>\u00a0187<\/u> :880-6\u00a0\u00a0\"Icon<\/a>

1.<\/b><\/font>\u00a0\u00a0Formation of nitrogen oxides and citrulline upon oxidation of N omega-hydroxy-L-arginine by hemeproteins.<\/b><\/font>\u00a0
Boucher Jl, Genet A, Vadon S, Delaforge M, Mansuy D
(1992)\u00a0Biochem Biophys Res Commun<\/b>\u00a0184<\/u> :1158-64\u00a0\u00a0\"Icon<\/a>

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