295 lesions were detected: PET alone, 178 lesions; diagnostic CT, 22 1 lesions; PET/CT (low-close CT), 272 lesions; PET/ check details CT (diagnostic CT). 295 lesions. Two thirds of the lesions, were located ill the bone: one third ill the prostate. lymph nodes, periprostatic tissue and soft tissue (lung, liver). The use of diagnostic CT did not result ill a statistically significant difference with respect to lesion The use of diagnostic localization certainly and lesion characterization (P=.063, P=.063), PET-negative bill PET/CT-positive lesions were mostly localized in the bone (78%, 91/117) as were PET-positive and CT-negative lesions (72%, 53/74). Of the latter, 91% (48/53) represented

bone marrow and 9% (5/53) cortical involvement,

Conclusions: Staging and restaging with [C-11]Choline PET/CT in patients with advanced prostate cancer improve the assessment of local and regional recurrent as well as metastatic disease including Tideglusib skeletal manifestations. [C-11]Choline PET/CT (with a low-dose CT) results in improved localiziation and

lesion characterization. [C-11]Choline PET/CT provides ill added value for skeletal manifestations. [C-11]Choline PET/CT changed disease management in 11 (24%) of 45 patients with advanced Prostate cancer. (C) 2008 Elsevier Inc. All rights reserved.”
“It is believed that a novel coronavirus, severe acute respiratory syndrome coronavirus (SARS-CoV), was passed from palm civets to humans and caused the epidemic of SARS in 2002 to 2003. The major species barriers between humans and civets for SARS-CoV infections are the specific interactions between a defined receptor-binding domain (RBD) on a viral spike protein and its host receptor, angiotensin-converting enzyme 2 (ACE2). In this study a chimeric ACE2 bearing the critical N-terminal helix from civet and the remaining peptidase domain from human was constructed, and it was shown that this construct has the same receptor activity as civet ACE2. In addition, crystal structures of the chimeric

ACE2 complexed with RBDs from various human and civet SARS-CoV strains were determined. These structures, combined with a previously determined structure of human ACE2 complexed with the RBD from a human to SARS-CoV strain, have revealed a structural basis for understanding the major species barriers between humans and civets for SARS-CoV infections. They show that the major species barriers are determined by interactions between four ACE2 residues (residues 31, 35, 38, and 353) and two RBD residues (residues 479 and 487), that early civet SARS-CoV isolates were prevented from infecting human cells due to imbalanced salt bridges at the hydrophobic virus/receptor interface, and that SARS-CoV has evolved to gain sustained infectivity for human cells by eliminating unfavorable free charges at the interface through stepwise mutations at positions 479 and 487.