Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Mary E. Shuck"'
Autor:
Beverly A. Reitz, Joseph W. Leone, Michael J. Bienkowski, Daniel F. Curran, Karl J. Mathis, Thomas L. Emmons, Jacqueline E. Day, Mary E. Shuck, Mark C. Walker, Alfredo G. Tomasselli, H. David Fischer
Publikováno v:
Protein Expression and Purification. 65:133-139
Soluble guanylate cyclase (sGC) has been purified from 100 L cell culture infected by baculovirus using the newer and highly effective titerless infected-cells preservation and scale-up (TIPS) method. Successive passage of the enzyme through DEAE, Ni
Autor:
Ismail Kola, Weiqun Liu, Kjell A. Svensson, Mary E. Shuck, Hartmut Tintrup, Sarah Wright, John A. Wijsman, Karen S. Chen, Lisa McConlogue, Thomas T. Kawabe, John P. Anderson, Kang Hu, Guriqbal Basi, Michael Power, Steven L. Roberds, Karl Kappenman, Dale Schenk, Stephen B. Freedman, Michael Schoor, Normand Frigon, David W. Robertson, Ralf Kuehn, Dora Kate Games, Sukanto Sinha, George Shopp, Kelly Johnson-Wood, Nanette F. Nichols, Michael Jerome Bienkowski, Mike Lee, Gwen Tatsuno, Ruth Motter, Daniel G. Branstetter
Publikováno v:
Human Molecular Genetics. 10:1317-1324
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by accumulation of amyloid plaques and neurofibrillary tangles in the brain. The major components of plaque, beta-amyloid peptides (Abetas), are produced from amyloid precursor pr
Autor:
Mary E. Shuck, Donald B. Carter, John R. Brashler, Mark E. Gurney, Alfredo G. Tomasselli, Luis A. Parodi, Riqiang Yan, Michael Jerome Bienkowski, Monica C. Tory, Allen E. Buhl, Nancy C. Stratman, Adele M. Pauley, Robert L. Heinrikson, W. Rodney Mathews, Huiyi Miao
Publikováno v:
Nature. 402:533-537
Mutations in the gene encoding the amyloid protein precursor (APP) cause autosomal dominant Alzheimer's disease. Cleavage of APP by unidentified proteases, referred to as beta- and gamma-secretases, generates the amyloid beta-peptide, the main compon
Autor:
Jeffery H. Bock, Jerry L. Slightom, Michael Jerome Bienkowski, Mary E. Shuck, Timothy Piser, Kai S. Lee
Publikováno v:
Journal of Biological Chemistry. 272:586-593
The DNA sequence encoding the rat brain inward rectifier-10 K+ channel was amplified from rat brain RNA using reverse transcription-polymerase chain reaction and used to clone the human homolog. Low stringency screening of a human kidney cDNA library
Autor:
C. W. Benjamin, Jerry L. Slightom, Jeffery H. Bock, K. S. Lee, Mary E. Shuck, Michael J. Bienkowski, Ti-Dao Tsai
Publikováno v:
Journal of Biological Chemistry. 269:24261-24270
The rat kidney ROM-K1 potassium channel cDNA was used to clone the homolog from human kidney using a combination of cDNA cloning, reverse transcriptase-polymerase chain reaction (RT-PCR), and primer extension cloning methods. In addition to the human
Publikováno v:
The Journal of biological chemistry. 276(36)
BACE1 and BACE2 define a new subfamily of membrane-anchored aspartyl proteases. Both endoproteases share similar structural organization including a prodomain, a catalytic domain formed via DTG and DSG active site motifs, a single transmembrane domai
Autor:
Jeffrey H. Bock, Mea Chee, Christopher W. Benjamin, Michael J. Bienkowski, Mary E. Shuck, Jerry L. Slightom
Publikováno v:
Gene. 188(1)
Detailed analyses of transcripts encoding various isoforms of the human potassium (K+, inward rectifying) channel ROM-K (also referred to as Kir1.1) revealed the existence of at least five distinct transcripts [Shuck et al., J. Biol. Chem. 269 (1994)
Publikováno v:
Gene. 137(2)
A third member of the human 5 HT ID gene family has been identified using a combination of homology cloning and DNA sequence analysis. This human gene is most related to the 5 HT 1 D α subtype (77% shared identity) and is a pseudogene, based on the
Publikováno v:
European journal of immunology. 21(11)
A cDNA coding for the human interleukin 1 receptor antagonist protein (IL 1Ra) was used to clone the corresponding murine cDNA. The nucleotide sequence of the open reading frame coding for the processed form of mIL 1Ra predicted a 152-residue protein