Design of the Novel Protraction Mechanism of Insulin Degludec, an Ultra-long-Acting Basal Insulin

[1]  L Nosek,et al.  Ultra‐long‐acting insulin degludec has a flat and stable glucose‐lowering effect in type 2 diabetes , 2012, Diabetes, obesity & metabolism.

[2]  L Nosek,et al.  Insulin degludec: four times lower pharmacodynamic variability than insulin glargine under steady‐state conditions in type 1 diabetes , 2012, Diabetes, obesity & metabolism.

[3]  T. Heise,et al.  Insulin degludec has a two-fold longer half-life and a more consistent pharmacokinetic profile compared with insulin glargine , 2012 .

[4]  J. DeVries,et al.  The future of basal insulin supplementation. , 2011, Diabetes technology & therapeutics.

[5]  B. Zinman,et al.  Insulin degludec, an ultra-long-acting basal insulin, once a day or three times a week versus insulin glargine once a day in patients with type 2 diabetes: a 16-week, randomised, open-label, phase 2 trial , 2011, The Lancet.

[6]  R. Jorde,et al.  A New-Generation Ultra-Long-Acting Basal Insulin With a Bolus Boost Compared With Insulin Glargine in Insulin-Naïve People With Type 2 Diabetes , 2011, Diabetes Care.

[7]  J. DeVries,et al.  A randomized controlled trial of a new-generation ultra-long-acting insulin compared with insulin glargine , 2011 .

[8]  Christine J. Bryson,et al.  Immunogenicity of protein therapeutics: The key causes, consequences and challenges. , 2010, Self/nonself.

[9]  Patrick Garidel,et al.  Strategies for the Assessment of Protein Aggregates in Pharmaceutical Biotech Product Development , 2010, Pharmaceutical Research.

[10]  A. Rosenberg,et al.  Effects of protein aggregates: An immunologic perspective , 2006, The AAPS Journal.

[11]  T. Pieber,et al.  Towards peakless, reproducible and long‐acting insulins. An assessment of the basal analogues based on isoglycaemic clamp studies , 2007, Diabetes, obesity & metabolism.

[12]  T. Pieber,et al.  Refining basal insulin therapy: what have we learned in the age of analogues? , 2007, Diabetes/metabolism research and reviews.

[13]  T. Heise,et al.  Albumin‐bound basal insulin analogues (insulin detemir and NN344): comparable time‐action profiles but less variability than insulin glargine in type 2 diabetes , 2007, Diabetes, obesity & metabolism.

[14]  Svend Havelund,et al.  Biochemical and Physiological Properties of a Novel Series of Long-Acting Insulin Analogs Obtained by Acylation with Cholic Acid Derivatives , 2006, Pharmaceutical Research.

[15]  P. Kurtzhals How to achieve a predictable basal insulin? , 2005, Diabetes & metabolism.

[16]  U. Ribel,et al.  The Mechanism of Protraction of Insulin Detemir, a Long-Acting, Acylated Analog of Human Insulin , 2004, Pharmaceutical Research.

[17]  L. Heinemann,et al.  Lower within-subject variability of insulin detemir in comparison to NPH insulin and insulin glargine in people with type 1 diabetes. , 2004, Diabetes.

[18]  K. Jørgensen,et al.  Homogeneous mono-125I-insulins , 1980, Diabetologia.

[19]  A. Lindholm New insulins in the treatment of diabetes mellitus. , 2002, Best practice & research. Clinical gastroenterology.

[20]  R. Brown Refractive Increment Data-Book , 2001 .

[21]  N. Kaarsholm,et al.  Structural effects of protein lipidation as revealed by LysB29-myristoyl, des(B30) insulin. , 2000, Biochemistry.

[22]  T. Arakawa,et al.  Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. , 1996, Analytical biochemistry.

[23]  U. Ribel,et al.  Albumin binding of insulins acylated with fatty acids: characterization of the ligand-protein interaction and correlation between binding affinity and timing of the insulin effect in vivo. , 1995, The Biochemical journal.

[24]  U. Ribel,et al.  Action Profile of Cobalt(III)-Insulin: A Novel Principle of Protraction of Potential Use for Basal Insulin Delivery , 1995, Diabetes.

[25]  M. Dunn,et al.  The allosteric transition of the insulin hexamer is modulated by homotropic and heterotropic interactions. , 1993, Biochemistry.

[26]  P. Krüger,et al.  Cooperativity and intermediate states in the T----R-structural transformation of insulin. , 1990, Biological chemistry Hoppe-Seyler.

[27]  M. Dunn,et al.  Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin. , 1989, Biochemistry.

[28]  J. Brange,et al.  Monomeric insulins obtained by protein engineering and their medical implications , 1988, Nature.

[29]  W. Stockmayer,et al.  Information on Polydispersity and Branching from Combined Quasi-Elastic and Intergrated Scattering , 1980 .

[30]  K. Jørgensen,et al.  Homogeneous mono-(125)i-insulins. Preparation and characterization of mono-(125)i-(tyr a14)-and mono-(125)i-(tyr a19)-insulin. , 1980, Diabetologia.

[31]  T. Blundell,et al.  Three-Dimensional Atomic Structure of Insulin and Its Relationship to Activity , 1972, Diabetes.

[32]  P. Andrews Estimation of molecular size and molecular weights of biological compounds by gel filtration. , 1970, Methods of biochemical analysis.

[33]  L. G. Longsworth,et al.  The specific refractive increment of some purified proteins. , 1948, Journal of the American Chemical Society.