Publications scientifiques d’Anne-Marie Yim, Ph.D.

1-Publications en Chimie des Amino-Acides, Peptides et Protéines

Institut des Biomolécules Max Mousseron, Montpellier, FRANCE:

I had the privilege to do my thesis under the guidance and supervision of Dr Yves Vidal, Pr Philippe Viallefont as well as Pr Jean Martinez who presided my thesis jury, Founder of the IBMM Institute and Recipient of the Silver Medal of CNRS as well as Knight of Academic palms.

http://ibmmpeptide.com/jean-martinez

JEAN Martinez
Professor, Faculty of Pharmacy, University OF MONTPELLIER

Jean Martinez received both his PhD in 1972 from the University of Montpellier 2, at the National School of Chemistry and his Dr Sciences Degree in 1976 from the same University, under the supervision of Professor F. Winternitz. The same year, he joined Dr E. Bricas group at Orsay, University of Paris Sud, as a post-doctorate fellow and in 1977 the laboratory of Professor M. Bodanszky at Case Western Reserve University in Cleveland, Ohio, USA, where he stayed till mid 1979.

Jean Martinez is a Full Professor at the University of Montpellier. In 2007, he created the « Institut des Biomolécules Max Mousseron » (IBMM), which he has been the Director until December 2014. He is actually Head of the department of Amino Acids, Peptides and Proteins at IBMM.

He served the University of Montpellier 1 as a Member of the Scientific Council for 8 years, and as Vice-President for 6 years (2009-2014).

Prof. Martinez is recognized for his important contributions, at the interface of chemistry and biology, to the development of methodology in organic and peptide synthesis, design and synthesis of various potent and selective neuropeptide analogues, and biomaterials containing biomolecules.

He has published over 900 original papers, 50 patents, numerous review articles, and he has been editor of several books. In 2012, he was accepted into the « Académie Nationale de Pharmacie », France, and in 2014 into the « Real Academia Nacional de Farmacia », Spain. In 2015, he has been nominated Docteur Honoris causa of the Jagellonian University of Kracow, Poland. He has received various prizes including the Leonidas Zervas Award (Barcelona, Spain 1990), the Silver Medal CNRS (Paris, France 1996), The Labbe Award (Paris, France 1996), The Mentzer Award (Caen, France 1998), the Max Bergmann Medal (Munster, Germany 2004), the Cathay Award (Shanghai, China 2006), the Akabori Award (Tokohama, Japan 2006), the Ehrlich Award (Lyon, France 2011), the Roche « Johannes Meinhofer Award » (Boulder Co, USA 2011), the Léon Velluz Award (Paris, France 2015), the Rudinger Award (Leipzig, Germany 2016). He is « Chevalier dans l’Ordre des Palmes Académiques » (2010), and Chevalier dans l’Ordre de la Légion d’Honneur (2011).

Jean Martinez served the European Peptide Society as French Representative, Member of the Executive Committee (1991-1998), Scientific Officer (1998-2001), and President (2001-2010).

https://www.researchgate.net/scientific-contributions/2011842969-Anne-Marie-Yim
Regioselective Epoxyde Ring-opening to the Enantiomeriocally Pure Alpha-hydroxy Analogue of S-tert-butyl Cysteine, Cavelier F. and Yim A.M., Org. Prep. Proced. Int., 1998, 30(1), 103-106.
Abstract

Our interest in alpha-hydroxy acids arose in connection with other work in which we required 2-hydroxy-3 mercapto propanoic acid in an optically active form. One usual method to prepare alpha hydroxy acids is to convert alpha-amino acids by nitrous acid deamination. However when initiated from cysteine, this reaction occured with thiiran formation and beta-elimination, while with cystine, it yielded to many unwanted sulfur containing compounds, resulting from oxidation side-reactions. Since it is known that thiolates open epoxides, we decided to investigate the reaction of potassiumglycidate with ter-butyl thiol to lead tona S-protected hydroxy analogue of cysteine.

Solid-Phase Synthesis of Alpha-Amino Acids by Radical Addition to a Dehydroalanine Derivative, Anne-Marie Yim*, Yves Vidal*, Philippe Viallefont, Jean Martinez, Tetrahedron Lett., 1999, 40, 4535-4538.
Abstract

The first synthesis of N-acetyl-alpha-amino acids by radical addition on solid support to commercialy available 2-acetamidoacrylic acid using the mercury method is described The reaction proceeds in acceptable chemical efficiency (49-60%) depending on the nature of the mercury halide agent. Cleavage by mild acid treatment released the product from the solid support in excellent purity. © 1999 Elsevier Science Ltd. All rights reserved. Keywords: dehydroamina acids – solid phase – mercury method – radical addition – N-acetyl-a-amino acids.

Diastereoselective radical addition to dehydroalanine derivativesof pantolactone, Anne-Marie Yim, Yves Vidal,* Philippe Viallefont and Jean Martinez, Tetrahedron: Asymmetry, 2002, 503-510.

Abstract

The diastereoselective synthesis of-amino acids by radical addition to dehydroalanine derivatives of pantolactoneusing the stannane method both in the presence and absence of Lewis acid catalysts is reported. The absolute configuration of thenewly-generated stereogenic center is highly dependent on the nature of the added radical. Acid hydrolysis afforded the aminoacids with excellent yields and without racemization. This approach constitutes a novel method for the asymmetric synthesis of-amino acids by a radical pathway. © 2002 Elsevier Science Ltd. All rights reserved

2-Publications en Biotechnologies/Protéomique

University of Michigan, United States
Pubmed

An immune response manifested by thecommon occurrence of annexins I and IIautoantibodies and high circulatinglevels of IL-6 in lung cancer, Franck M. Brichory*, David E. Misek*, Anne-Marie Yim*, Melissa C. Krause*, Thomas J. Giordano†, David G. Beer‡,and Samir M. Hanash*, Proc. Natl. Acad. Sci. U.S.A, 2001, 98(17), 9824-9829.

An immune response manifested by thecommon occurrence of annexins I and IIautoantibodies and high circulatinglevels of IL-6 in lung cancer,
Abstract

An immune response manifested by thecommon occurrence of annexins I and IIautoantibodies and high circulatinglevels of IL-6 in lung cancerFranck M. Brichory*, David E. Misek*, Anne-Marie Yim*, Melissa C. Krause*, Thomas J. Giordano†, David G. Beer‡,and Samir M. Hanash*§Departments of *Pediatrics,†Pathology, and‡Surgery, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, MI 48109Communicated by Lewis T. Williams, Chiron Technologies, Emeryville, CA, June 25, 2001 (received for review March 26, 2001)The identification of circulating tumor antigens or their relatedautoantibodies provides a means for early cancer diagnosis as wellas leads for therapy. The purpose of this study was to identifyproteins that commonly induce a humoral response in lung cancerby using a proteomic approach and to investigate biologicalprocesses that may be associated with the development of auto-antibodies. Aliquots of solubilized proteins from a lung adenocar-cinoma cell line (A549) and from lung tumors were subjected totwo-dimensional PAGE, followed by Western blot analysis in whichindividual sera were tested for primary antibodies. Sera from 54newly diagnosed patients with lung cancer and 60 patients withother cancers and from 61 noncancer controls were analyzed. Serafrom 60% of patients with lung adenocarcinoma and 33% ofpatients with squamous cell lung carcinoma but none of thenoncancer controls exhibited IgG-based reactivity against proteinsidentified as glycosylated annexins I andyor II. Immunohistochem-ical analysis showed that annexin I was expressed diffusely inneoplastic cells in lung tumor tissues, whereas annexin II waspredominant at the cell surface. Interestingly, IL-6 levels weresignificantly higher in sera of antibody-positive lung cancer pa-tients compared with antibody-negative patients and controls. Weconclude that an immune response manifested by annexins I andII autoantibodies occurs commonly in lung cancer and is associatedwith high circulating levels of an inflammatory cytokine. Theproteomic approach we have implemented has utility for thedevelopment of serum-based assays for cancer diagnosis as wereport in this paper on the discovery of antiannexins I andyor II insera from patients with lung cance

Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function, Bong Kyung Shin  1 Hong WangAnne Marie YimFrancois Le NaourFranck BrichoryJun Ho JangRong ZhaoEric PuravsJohn TraClaire W MichaelDavid E MisekSamir M Hanash, J Biol Chem,. 2003 Feb 28;278(9):7607-16.

Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function
Abstract

There is currently limited data available pertaining to the global characterization of the cell surface proteome. We have implemented a strategy for the comprehensive profiling and identification of surface membrane proteins. This strategy has been applied to cancer cells, including the SH-SY5Y neuroblastoma, the A549 lung adenocarcinoma, the LoVo colon adenocarcinoma, and the Sup-B15 acute lymphoblastic leukemia (B cell) cell lines and ovarian tumor cells. Surface membrane proteins of viable, intact cells were subjected to biotinylation then affinity-captured and purified on monomeric avidin columns. The biotinylated proteins were eluted from the monomeric avidin columns as intact proteins and were subsequently separated by two-dimensional PAGE, transferred to polyvinylidene difluoride membranes, and visualized by hybridization with streptavidin-horseradish peroxidase. Highly reproducible, but distinct, two-dimensional patterns consisting of several hundred biotinylated proteins were obtained for the different cell populations analyzed. Identification of a subset of biotinylated proteins among the different cell populations analyzed using matrix-assisted laser desorption ionization and tandem mass spectrometry uncovered proteins with a restricted expression pattern in some cell line(s), such as CD87 and the activin receptor type IIB. We also identified more widely expressed proteins, such as CD98, and a sushi repeat-containing protein, a member of the selectin family. Remarkably, a set of proteins identified as chaperone proteins were found to be highly abundant on the cell surface, including GRP78, GRP75, HSP70, HSP60, HSP54, HSP27, and protein disulfide isomerase. Comprehensive profiling of the cell surface proteome provides an effective approach for the identification of commonly occurring proteins as well as proteins with restricted expression patterns in this compartment

%d blogueurs aiment cette page :