| Limestone Internal Medicine | |
|
710 W Hobbs St Athens AL 35611-1508 | |
| (256) 233-6311 | |
| Not Available |
| Full Name | Limestone Internal Medicine |
|---|---|
| Speciality | Internal Medicine |
| Location | 710 W Hobbs St, Athens, Alabama |
| Authorized Official Name and Position | James Russell Walker (PRESIDENT) |
| Authorized Official Contact | 2562336311 |
| Accepts Medicare Insurance | This clinic does not participate in Medicare Program. |
| Mailing Address | Practice Location Address |
|---|---|
| Limestone Internal Medicine 710 West Hobbs Street Athens AL 35611-1508 Ph: (256) 233-6311 | Limestone Internal Medicine 710 W Hobbs St Athens AL 35611-1508 Ph: (256) 233-6311 |
| NPI Number | 1417264425 |
|---|---|
| Provider Enumeration Date | 09/13/2010 |
| Last Update Date | 09/13/2010 |
| Identifier | Type | State | Issuer |
|---|---|---|---|
| 1417264425 | NPI | - | NPPES |
| 000077994 | Medicaid | AL |
| Taxonomy | Type | License (State) | Status |
|---|---|---|---|
| 207R00000X | Internal Medicine | 13208 (Alabama) | Primary |
News Archive
Gilead Sciences, Inc. announced today its results of operations for the quarter ended September 30, 2010. Total revenues for the third quarter of 2010 were $1.94 billion, up 8 percent compared to total revenues of $1.80 billion for the third quarter of 2009. Net income for the third quarter of 2010 was $704.9 million, or $0.83 per diluted share, compared to net income for the third quarter of 2009 of $673.0 million, or $0.72 per diluted share.
New research from UC San Francisco found that 60 percent of the city's homeless and unstably housed women who are HIV-infected or at high risk to become infected have endured a recent experience of some form of violence.
An international team of researchers, including a psychologist at Oregon State University, has developed a standardized measurement for pediatric facial palsy that will improve the care for current and future patients with the condition.
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Cells have evolved multiple mechanisms to ensure proper folding, but a number of molecular and biophysical events - such as changes in pH or temperature, mutations, and oxidation - can disrupt a protein's native shape.
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