» Authors » J H Till

J H Till

Explore the profile of J H Till including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 10
Citations 761
Followers 0
Related Specialties
Top 10 Co-Authors
Published In
Affiliations
Soon will be listed here.
Recent Articles
1.
Rix U, Remsing Rix L, Terker A, Fernbach N, Hantschel O, Planyavsky M, et al.
Leukemia . 2009 Nov; 24(1):44-50. PMID: 19890374
Resistance to the BCR-ABL tyrosine kinase inhibitor imatinib poses a pressing challenge in treating chronic myeloid leukemia (CML). This resistance is often caused by point mutations in the ABL kinase...
2.
Remsing Rix L, Rix U, Colinge J, Hantschel O, Bennett K, Stranzl T, et al.
Leukemia . 2008 Nov; 23(3):477-85. PMID: 19039322
The detailed molecular mechanism of action of second-generation BCR-ABL tyrosine kinase inhibitors, including perturbed targets and pathways, should contribute to rationalized therapy in chronic myeloid leukemia (CML) or in other...
3.
Favelyukis S, Till J, Hubbard S, Miller W
Nat Struct Biol . 2001 Nov; 8(12):1058-63. PMID: 11694888
The insulin-like growth factor 1 (IGF1) receptor is closely related to the insulin receptor. However, the unique biological functions of IGF1 receptor make it a target for therapeutic intervention in...
4.
Parang K, Till J, Ablooglu A, Kohanski R, Hubbard S, Cole P
Nat Struct Biol . 2001 Jan; 8(1):37-41. PMID: 11135668
Protein kinase inhibitors have applications as anticancer therapeutic agents and biological tools in cell signaling. Based on a phosphoryl transfer mechanism involving a dissociative transition state, a potent and selective...
5.
Till J, Ablooglu A, Frankel M, Bishop S, Kohanski R, Hubbard S
J Biol Chem . 2001 Jan; 276(13):10049-55. PMID: 11124964
The tyrosine kinase domain of the insulin receptor is subject to autoinhibition in the unphosphorylated basal state via steric interactions involving the activation loop. A mutation in the activation loop...
6.
Hubbard S, Till J
Annu Rev Biochem . 2000 Aug; 69:373-98. PMID: 10966463
Tyrosine phosphorylation is one of the key covalent modifications that occurs in multicellular organisms as a result of intercellular communication during embryogenesis and maintenance of adult tissues. The enzymes that...
7.
Ablooglu A, Till J, Kim K, Parang K, Cole P, Hubbard S, et al.
J Biol Chem . 2000 Jun; 275(39):30394-8. PMID: 10869355
The interaction of a synthetic tetrafluorotyrosyl peptide substrate with the activated tyrosine kinase domain of the insulin receptor was studied by steady-state kinetics and x-ray crystallography. The pH-rate profiles indicate...
8.
Till J, Chan P, Miller W
J Biol Chem . 1999 Feb; 274(8):4995-5003. PMID: 9988744
c-Abl is a non-receptor tyrosine kinase that is involved in a variety of signaling pathways. Activated forms of c-Abl are associated with some forms of human leukemia. Presently, no high...
9.
Lee T, Till J, Lawrence D, Miller W
J Biol Chem . 1995 Nov; 270(45):27022-6. PMID: 7592951
The active site substrate specificities of v-Abl and c-Src are compared and contrasted. Both enzymes catalyze the phosphorylation of a broad assortment of peptide-bound aliphatic and aromatic alcohols, such as...
10.
Till J, Annan R, Carr S, Miller W
J Biol Chem . 1994 Mar; 269(10):7423-8. PMID: 8125961
To search for peptides which serve as substrates for protein kinases, an approach based on peptide libraries has been developed. These peptide libraries are chemically synthesized by a modified "divide-couple-recombine"...