scholarly journals Characterization of Growth, Glomerular Number, and Tubular Proteins in the Developing Rhesus Monkey Kidney

2013 ◽  
Vol 296 (11) ◽  
pp. 1747-1757 ◽  
Author(s):  
Cynthia A. Batchelder ◽  
Jennifer L. Keyser ◽  
C. Chang I. Lee ◽  
Alice F. Tarantal
Keyword(s):  
Rhesus Monkey ◽  
Monkey Kidney ◽  
Glomerular Number ◽  
Tubular Proteins

Characterization of a cDNA for Rhesus Monkey Protein C Inhibitor – Evidence for N-Terminal Involvement in Heparin Stimulation

1995 ◽  
Vol 74 (04) ◽  
pp. 1079-1087 ◽  
Author(s):  
Klaus-P Radtke ◽  
José A Fernández ◽  
Bruno O Villoutreix ◽  
Judith S Greengard ◽  
John H Griffin
Keyword(s):  
Rhesus Monkey ◽  
Protein C ◽  
Activated Protein C ◽  
Pcr Amplification ◽  
Amino Acid Sequences ◽  
Heparin Binding ◽  
Reactive Center ◽  
Protein C Inhibitor ◽  
Polymerase Chain

SummarycDNAs for protein C inhibitor (PCI) were cloned from human and rhesus monkey 1 liver RNAs by reverse transcription and polymerase chain reaction (PCR) amplification. Sequencing showed that rhesus monkey and human PCI cDNAs were 93% identical. Predicted amino acid sequences differed at 26 of 387 residues. Pour of these differences (T352M, N359S, R362K, L3631) were in the reactive center loop that is important for inhibitory specificity, and two were in the N-terminal helix (M8T, E13K) that is implicated in glycosaminoglycan binding. PCI in human or rhesus monkey plasma showed comparable inhibitory activity towards human activated protein C in the presence of 10 U/ml heparin. However, maximal acceleration of the inhibition of activated protein C required 5-fold lower heparin concentration for rhesus monkey than for human plasma, consistent with the interpretation that the additional positive charge (E13K) in a putative-heparin binding region increased the affinity for heparin.

Cloning and characterization of rhesus monkey MCH-R1 and MCH-R2

Peptides ◽  
2002 ◽  
Vol 23 (8) ◽  
pp. 1401-1408 ◽  
Author(s):  
Steven Fried ◽  
Kim O’Neill ◽  
Brian E Hawes
Keyword(s):  
Rhesus Monkey

scholarly journals Enterovirus 70 Receptor Utilization Is Controlled by Capsid Residues That Also Regulate Host Range and Cytopathogenicity

2007 ◽  
Vol 81 (16) ◽  
pp. 8648-8655 ◽  
Author(s):  
Melissa Stewart Kim ◽  
Vincent R. Racaniello
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rhesus Monkey ◽  
Host Range ◽  
Hela Cells ◽  
Lytic Replication ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
Cytopathic Effects ◽  
Axis Of Symmetry

ABSTRACT Enterovirus type 70, an etiologic agent of acute hemorrhagic conjunctivitis, may bind different cellular receptors depending on cell type. To understand how EV70-receptor interaction is controlled, we studied two variants of the virus with distinct receptor utilization. EV70-Rmk, derived by passage in rhesus monkey kidney cells, replicates poorly in HeLa cells and does not cause cytopathic effects. Decay accelerating factor (DAF) is not a cell receptor for EV70-Rmk. Passage of EV70-Rmk in HeLa cells lead to isolation of EV70-Dne, which does not replicate in rhesus monkey kidney cells but grows to high titers in HeLa cells and causes cytopathic effects. DAF is sufficient for cell entry of EV70-Dne. EV70-Rmk replicates in human eye and brain-derived cell lines, whereas the Dne strain replicates only in HeLa cells and in conjunctiva-derived 15C4 cells. The two EV70 strains differ by five amino acid changes in the viral capsid. Single substitution of four of the five EV70-Rmk amino acids with the residue from EV70-Dne leads to lytic replication in HeLa cells. Conversely, substitution of any of the five EV70-Dne amino acids with the EV70-Rmk amino acid does not alter replication in HeLa cells. Three of these capsid amino acids are predicted to be located in the canyon encircling the fivefold axis of symmetry, one amino acid is found at the fivefold axis of symmetry, and one is located the interior of the capsid. The five EV70 residues define a region of the capsid that controls viral host range, DAF utilization, and cytopathogenicity.

Molecular characterization of rhesus monkey Mhc-DR region: full length cDRA/cDRB analysis

2003 ◽  
Vol 64 (10) ◽  
pp. S164
Author(s):  
Nanine de Groot ◽  
Gaby G.M. Doxiadis ◽  
Natasja G. de Groot ◽  
Nel Otting ◽  
Corrine M.C. Heijmans ◽  
...  
Keyword(s):  
Rhesus Monkey ◽  
Molecular Characterization ◽  
Full Length

Characterization of Latent Transforming Growth Factor-β2 from Monkey Kidney Cells

Endocrinology ◽  
1991 ◽  
Vol 128 (5) ◽  
pp. 2291-2296 ◽  
Author(s):  
MARIO N. LIOUBIN ◽  
LINDA MADISEN ◽  
RICHARD A. ROTH ◽  
A. F. PURCHIO
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
Transforming Growth Factor Β2

scholarly journals Pharmacological characterization of the rhesus monkey TRPA1 channel

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Bruce R Bianchi ◽  
Xu-Feng Zhang ◽  
Regina M Reilly ◽  
Philip R Kym ◽  
Betty B Yao ◽  
...  
Keyword(s):  
Rhesus Monkey ◽  
Pharmacological Characterization

scholarly journals Characterization of the Neuroanatomical Distribution of Agouti-Related Protein Immunoreactivity in the Rhesus Monkey and the Rat*

Endocrinology ◽  
1999 ◽  
Vol 140 (3) ◽  
pp. 1408-1415 ◽  
Author(s):  
Carrie Haskell-Luevano ◽  
Peilin Chen ◽  
Chien Li ◽  
Kang Chang ◽  
M. Susan Smith ◽  
...  
Keyword(s):  
Rhesus Monkey ◽  
Related Protein ◽  
Protein Immunoreactivity ◽  
Agouti Related Protein
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