Merck Sharp + Dohme Corp.

Merck + Co., Inc.

Indiana University

Istituto Di Ricerche Di Biologia Molecolare P. Angeletti Spa

Msd Italia S.r.l.

Istituto Di Ricerche Di Biologia Molecolare P. Angeletti S.r.l.

Istituto Di Ricerche Di Biologia Molecolare P. Angeletti

Donald J Marsh

Elisabetta Bianchi

Antonello Pessi

Paolo Ingallinella

Ranabir Sinha Roy

George J Eiermann

Yun-Ping Zhou

Yingjun Mu

Richard Dennis DiMarchi

Joseph M Metzger

Alessia Santoprete

Paul E Carrington

Brian P Ward

Elena Capito

Alessandro Pocai

Su Qian

George Eiermann

Richard Dimarchi

Antonella Pessi

Yin-Ping Zhou

Andrea M Peier

Maria A Bednarek

Peptide analogs of oxyntomodulin (OXM, glucagon-37), which have been modified to be resistant to cleavage and inactivation by dipeptidyl peptidase IV (DPP-IV) and to increase in vivo half-life of the peptide analog while enabling the peptide analog to act as a dual GLP-1/glucagon receptor (GCGR) agonist are described. The peptide analogs are useful for treatment of metabolic disorders such as diabetes and obesity.

Oxyntomodulin analogs

Modified oxyntomodulin derivatives. Such derivatives can be used for the treatment of metabolic diseases such as diabetes and obesity.

Pharmaceutical composition comprising oxyntomodulin derivatives and a method for reducing body weight using the composition

The present invention features viable MCH1R deficient mice. MCH1R deficient mice contain an alteration in one or both MCH1R alleles that substantially reduces expression of a functional MCH1R from the altered allele. Preferably, MCH1R deficient mice are MCH1R &#x2212;/&#x2212; knockout mice.

MCH1R deficient mice

The present invention features melanin concentrating hormone receptor (MCH-R) chimeric and fusion proteins. MCH-R chimeric proteins comprise an MCH-R polypeptide region made up of at least two or more polypeptide regions characteristic of MCH-R found in different species. MCH-R fusion proteins comprise an MCH-R polypeptide region and a fluorescent protein region.

Melanin concentrating hormone receptor chimeric and fusion proteins

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Hillsborough, NJ, United States of America

Donald J Marsh