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Genzyme Corporation is an American biotechnology company based in Cambridge, Massachusetts. Since its acquisition in 2011 it's been a fully owned subsidiary of Sanofi. In 2010 Genzyme was the world’s third-largest biotechnology company, employing more than 11,000 people around the world. As a subsidiary of Sanofi, Genzyme has a presence in approximately 65 countries, including 17 manufacturing facilities and 9 genetic-testing laboratories, its products are sold in 90 countries. In 2007, Genzyme generated $3.8 billion in revenues with more than 25 products in the market. In 2006 and 2007 Genzyme was named one of Fortune Magazine’s “100 Best Companies to Work for”. The company donated $83 million worth of products worldwide; in 2006, it made $11 million in cash donations. In 2005, Genzyme was awarded the National Medal of Technology, the highest level of honor awarded by the president of the United States to America’s leading innovators. Wikipedia.

Tambuyzer E.,Genzyme
Nature Reviews Drug Discovery | Year: 2010

Sustained advocacy efforts driven by patients' organizations to make rare diseases a health priority have led to regulatory and economic incentives for industry to develop drugs for these diseases, known as orphan drugs. These incentives, enacted in regulations first introduced in the United States in 1983 and later in Japan, Europe and elsewhere, have resulted in substantial improvements in the treatment for patients with a range of rare diseases. However, the advent of orphan drug development has also triggered several questions, from the definition of rarity to the pricing of orphan drugs and their impact on health-care systems. This article provides an industry perspective on some of the common questions and misconceptions related to orphan drug development and its regulation, with the aim of facilitating future progress in the field. © 2010 Macmillan Publishers Limited. All rights reserved. Source

Dharanipragada R.,Genzyme
Future Medicinal Chemistry | Year: 2013

There has been a resurgence of interest in peptide pharmaceuticals as they have an advantage of potency, selectivity and less toxicity compared with small-molecule therapeutics. The main draw back of peptides is lack of stability to biological media. Constraining a peptide has been one of the approaches to improving in vivo stability of the peptides. Several new modalities in constraining peptides have been developed over recent years and this review highlights some of the new developments. The newer cyclization strategies have rendered, in some cases, oral activity, cell permeability, improved potency at the target receptor, selectivity against receptor subtypes and improved stability to enzymes. As chemists further understand the rules governing cell permeability, oral absorption and enhancing stability of peptides, we can expect to see more peptides entering clinic for many unmet medical needs. © 2013 Future Science Ltd. Source

Fricker S.P.,Genzyme
Transfusion Medicine and Hemotherapy | Year: 2013

Autologous hematopoietic stem cell (HSC) transplantation is an important therapeutic option for patients with non-Hodgkin's lymphoma and multiple myeloma. The primary source of HSC is from the peripheral blood which requires mobilization from the bone marrow. Current mobilization regimens include cytokines such as G-CSF and/or chemotherapy. However not all patients mobilize enough HSC to proceed to transplant. The chemokine receptor CXCR4 and its ligand CXCL12 are an integral part of the mechanism of HSC retention in the bone marrow niche. The discovery of plerixafor, a selective inhibitor of CXCR4, has provided a new additional means of mobilizing HSC for autologous transplantation. Plerixafor consists of two cyclam rings with a phenylenebis(methylene) linker. It inhibits CXCL12 binding to CXCR4 and subsequent downstream events including chemotaxis. The molecular interactions of plerixafor have been defined indicating a unique binding mode to CXCR4. Plerixafor rapidly mobilizes HSC within hours compared with the multi-day treatment required by G-CSF in mouse, dog and non-human primate. The mobilized cells once transplanted are capable of timely and endurable engraftment. Additionally CXCR4 has been implicated in the pathology of HIV, inflammatory disease and cancer and the pharmacology of plerixafor in various disease models is described. © 2013 S. Karger GmbH, Freiburg. Source

Fricker S.P.,Genzyme
Metallomics | Year: 2010

The discovery of the platinum anticancer drug cisplatin provided a major stimulus for research into metal-based drugs. The molecular target for the platinum agents is DNA; however recent developments in inorganic medicinal chemistry have identified several alternative novel targets for metal-based drugs. Biological molecules with essential thiol groups are attractive targets. Thiol-containing molecular targets include the redox enzymes thioredoxin reductase and glutathione reductase, transcription factors, and cysteine proteases such as caspases and cathepsins. Inorganic chemistry offers many opportunities for medicinal chemistry, and alternative targets for metal-based drugs are reviewed, with a focus on cysteine proteases. The cathepsin cysteine proteases have numerous physiological functions, and have been implicated in diseases including cancer, autoimmune and inflammatory, and parasitic diseases. The catalytic mechanism of these enzymes is dependent upon a cysteine at the active site. We postulate that metal complexes can inhibit these enzymes via a ligand substitution with the thiol of the active site cysteine. We have investigated several classes of metal complexes including cyclometalated organo gold(iii) and Pd(ii) complexes, and a series of rhenium(v) mixed ligand oxorhenium complexes as inhibitors of cathepsin cysteine proteases. Mechanistic studies were conducted on the latter supporting the hypothesis of active site-directed inhibition. These data are reviewed below and discussed in the context of possible therapeutic applications including cancer and parasitic disease. © 2010 The Royal Society of Chemistry. Source

The hemitartrate salt of a compound represented by the following structural formula: (Formula I Hemitartrate), which may be used in pharmaceutical applications, are disclosed. Particular single crystalline forms of the Formula (I) Hemitartrate are characterized by a variety of properties and physical measurements. As well, methods of producing crystalline Formula (I) Hemitartrate, and using it to inhibit glucosylceramide synthase or lowering glycosphingolipid concentrations in subjects to treat a number of diseases, are also discussed. Pharmaceutical compositions are also described.

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