P A KarplusSummaryAffiliation: Cornell University Country: USA Publications
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Publications
Experimentally observed conformation-dependent geometry and hidden strain in proteinsP A Karplus
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA
Protein Sci 5:1406-20. 1996....
Hydrophobicity regainedP A Karplus
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA
Protein Sci 6:1302-7. 1997....
The insect immune protein scolexin is a novel serine proteinase homologC M Finnerty
Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, New York 14853, USA
Protein Sci 8:242-8. 1999..Most remarkable is the absence of a canonical activation peptide cleavage site. This suggests that the regulation of scolexin activity will involve a novel activation mechanism...
Crystal structure of the catalytic domain of a thermophilic endocellulaseM Spezio
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853
Biochemistry 32:9906-16. 1993....
Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutantsE Jabri
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA
Biochemistry 35:10616-26. 1996....
Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraoseJ Sakon
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA
Biochemistry 35:10648-60. 1996....
Structure and mechanism of endo/exocellulase E4 from Thermomonospora fuscaJ Sakon
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA
Nat Struct Biol 4:810-8. 1997..We also provide evidence that E4 has two novel characteristics: first it combines exo- and endo-activities and second, when it functions as an exo-cellulase, it cleaves off cellotetraose units...
Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factorK Diederichs
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853
Science 254:1779-82. 1991..Residues implicated in receptor recognition, which are distant in the primary sequence, are on adjacent alpha helices in the folded protein. A working model for the receptor binding site is presented...
The crystal structure of urease from Klebsiella aerogenesE Jabri
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853, USA
Science 268:998-1004. 1995..A surprisingly high structural similarity between the urease catalytic domain and that of the zinc-dependent adenosine deaminase reveals a remarkable example of active site divergence...
Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domainM A Pearson
Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA
Cell 101:259-70. 2000..This extended binding mode suggests a novel mechanism for how different signals could produce varying levels of activation. Sequence conservation suggests a similar regulation of the tumor suppressor merlin...
