Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
Add more filters










Database
Language
Publication year range
1.
Radiographics ; 36(1): 7-18, 2016.
Article in English | MEDLINE | ID: mdl-26761528

ABSTRACT

Ultrasonography (US) of the breast and axilla is primarily used to evaluate a symptomatic patient or to further investigate findings identified with other imaging modalities. Breast imagers are generally familiar with US evaluation of level I, II, and III axillary lymph nodes in the diagnosis and staging of breast cancer. However, the axilla contains nonlymphatic tissue as well, including muscle, fat, and vascular and neurologic structures, and anatomically the breast lies on the chest wall. Therefore, lesions of nonmammary and non-lymph node origin in the axilla or chest wall are not infrequently encountered during US evaluation of the breast or axilla. In fact, such lesions may be the reason that the patient presents to the breast imaging department for evaluation. Understanding the anatomy of the chest wall and axilla and using a systematic US approach will help radiologists expedite accurate diagnosis, suggest optimal additional imaging, and streamline appropriate clinical referral. Key imaging features of nonmammary non-lymph node masses are highlighted, and case examples are provided to illustrate these features. Appropriate patient management is critical in these cases because referral to a breast surgeon may not be the best next step. Depending on institutional referral patterns, other subspecialty surgeons will be involved. Online supplemental material is available for this article.


Subject(s)
Image Enhancement/methods , Lymphatic Diseases/diagnostic imaging , Soft Tissue Infections/diagnostic imaging , Thoracic Diseases/diagnostic imaging , Ultrasonography, Mammary/methods , Vascular Diseases/diagnostic imaging , Axilla , Diagnosis, Differential , Female , Humans , Male
2.
J Clin Ultrasound ; 42(7): 423-6, 2014 Sep.
Article in English | MEDLINE | ID: mdl-24585495

ABSTRACT

PURPOSE: To assess the prevalence of testicular microlithiasis and its association with primary testicular neoplasm. METHODS: Evaluated were 6,002 patients undergoing scrotal ultrasound at our institution. Data recorded included age, ultrasound date, presence of microlithiasis, presence of testicular mass on ultrasound, and pathologic diagnosis for those who had subsequent orchiectomy. RESULTS: Four hundred fifty-six of 6,002 patients (7.6%) demonstrated testicular microlithiasis. The prevalence increased from 4.6% for those examined before 2001 to 9.02% for those examined since 2001 (p < 0.001). The prevalence of primary testicular neoplasm in patients without microlithiasis was 1.5% (84/5,546), whereas in those with microlithiasis it was 12% (53/456) (p < 0.001). The prevalence of pure seminoma was 39% (33/84) in the nonmicrolithiasis group with tumor versus 64% (34/53) in the microlithiasis group with tumor (p < 0.001). Germ cell tumors made up 98% of neoplasms in patients with microlithiasis, but only 85% in patients without microlithiasis (p = 0.009). CONCLUSIONS: Advances in ultrasound technology have led to an increased detection of testicular microlithiasis. We observed an eight-fold increased prevalence of primary testicular neoplasm in patients with microlithiasis than in those without as well as an increased prevalence of germ cell tumors, particularly pure seminoma. © 2014 Wiley Periodicals, Inc. J Clin Ultrasound 42:423-426, 2014.


Subject(s)
Calculi/diagnostic imaging , Testicular Diseases/diagnostic imaging , Testicular Neoplasms/diagnostic imaging , Adult , Calculi/epidemiology , Calculi/etiology , Diagnosis, Differential , Humans , Male , Prevalence , Retrospective Studies , Risk Factors , Testicular Diseases/epidemiology , Testicular Diseases/etiology , Testicular Neoplasms/complications , Testicular Neoplasms/epidemiology , Ultrasonography , United States/epidemiology
3.
Nat Chem Biol ; 5(9): 647-54, 2009 Sep.
Article in English | MEDLINE | ID: mdl-19648931

ABSTRACT

Biochemical combinatorial techniques such as phage display, RNA display and oligonucleotide aptamers have proven to be reliable methods for generation of ligands to protein targets. Adapting these techniques to small synthetic molecules has been a long-sought goal. We report the synthesis and interrogation of an 800-million-member DNA-encoded library in which small molecules are covalently attached to an encoding oligonucleotide. The library was assembled by a combination of chemical and enzymatic synthesis, and interrogated by affinity selection. We describe methods for the selection and deconvolution of the chemical display library, and the discovery of inhibitors for two enzymes: Aurora A kinase and p38 MAP kinase.


Subject(s)
DNA/chemistry , Drug Design , Protein Kinase Inhibitors/chemical synthesis , Small Molecule Libraries/chemical synthesis , Animals , Aurora Kinases , Combinatorial Chemistry Techniques , DNA/genetics , Models, Molecular , Protein Kinase Inhibitors/chemistry , Protein Kinase Inhibitors/pharmacology , Protein Serine-Threonine Kinases/antagonists & inhibitors , Small Molecule Libraries/chemistry , Small Molecule Libraries/pharmacology , p38 Mitogen-Activated Protein Kinases/antagonists & inhibitors
4.
Biophys J ; 95(1): 322-32, 2008 Jul.
Article in English | MEDLINE | ID: mdl-18339762

ABSTRACT

The unfolding and refolding reaction of myoglobin was examined in solution and within a porous silica sol-gel glass. The sol-gel pores constrain the protein to a volume that is the same size and shape as the folded native state accompanied by a few layers of water solvation. Denaturants such as low pH buffers can be diffused through the gel pores to the protein to initiate unfolding and refolding. Acid-induced unfolding was hindered by the steric constraints imposed by the gel pores such that more denaturing conditions were required within the gel than in solution to create the unfolded state. No new folding intermediates were observed. Refolding of myoglobin was not complete in millimolar pH 7 buffer alone. Addition of 25% glycerol to the pH 7 buffer resulted in nearly complete refolding, and the use of 1 M phosphate buffer resulted in complete refolding. The role of this cosolvent and salt in disrupting the ordered water surrounding the protein within the gel is discussed in light of the Hofmeister series and entropic trapping via a diminished hydrophobic effect within the gel. These results are consistent with the premises of folding models in which secondary and tertiary structures are considered to form within a compact conformation of the protein backbone.


Subject(s)
Glass/chemistry , Models, Chemical , Models, Molecular , Myoglobin/chemistry , Silicon Dioxide/chemistry , Computer Simulation , Phase Transition , Protein Conformation , Protein Folding
SELECTION OF CITATIONS
SEARCH DETAIL
...