E. F. Benson

Edward Frederic Benson (24 July 1867 – 29 February 1940) was an English novelist, biographer, memoirist, archaeologist and short story writer, known professionally as E. F. Benson. His friends called him Fred.

Life

E. F. Benson was born at Wellington College in Berkshire, the fifth child of the headmaster, Edward White Benson (later Chancellor of Lincoln Cathedral, Bishop of Truro and Archbishop of Canterbury), and Mary Sidgwick Benson ("Minnie").

Benson was educated at Temple Grove School, then at Marlborough College, where he wrote some of his earliest works and upon which he based his novel David Blaize. He continued his education at King's College, Cambridge. At Cambridge, he was a member of the Pitt Club, and later in life he became an honorary fellow of Magdalene College.

E. F. Benson was the younger brother of Arthur Christopher Benson, who wrote the words to "Land of Hope and Glory", Monsignor Robert Hugh Benson, author of several novels and Roman Catholic apologetic works, and Margaret Benson (Maggie), an amateur Egyptologist. Two other siblings died young. Benson's parents had six children and no grandchildren. E. F. Benson never married, and is likely to have been homosexual. Certainly this reveals itself through the camp humour of his novels, the implicit homoeroticism of his university works such as David Blaize (1916), his love of the company of handsome men, and his close friendships with known homosexuals such as John Ellingham Brooks with whom he shared a villa in Capri. Prior to the First World War the island was extremely popular with wealthy gay men.

EF

EF or ef may refer to:

Computing

Culture

Linguistics

Organizations

Psychology

Science

Efavirenz

Efavirenz (EFV), sold under the brand names Sustiva among others, is a non-nucleoside reverse transcriptase inhibitor (NNRTI). It is used as part of highly active antiretroviral therapy (HAART) for the treatment of a human immunodeficiency virus (HIV) type 1. For HIV infection that has not previously been treated, the United States Department of Health and Human Services Panel on Antiretroviral Guidelines currently recommends the use of efavirenz in combination with tenofovir/emtricitabine (Truvada) as one of the preferred NNRTI-based regimens in adults and adolescents. Efavirenz is also used in combination with other antiretroviral agents as part of an expanded postexposure prophylaxis regimen to reduce the risk of HIV infection in people exposed to a significant risk (e.g. needlestick injuries, certain types of unprotected sex etc.).

It is usually taken on an empty stomach at bedtime to reduce neurological and psychiatric adverse effects.

Efavirenz was combined with the HIV medications tenofovir and emtricitabine, all of which are reverse transcriptase inhibitors. This combination of three medications under the brand name Atripla, provides HAART in a single tablet taken once a day.

E2F4

Transcription factor E2F4 is a protein that in humans is encoded by the E2F4 gene.

Function

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.

Structure

The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids (Asp + Glu), and a tumor suppressor protein association domain which is embedded within the transactivation domain.

E4F1

Transcription factor E4F1 is a protein that in humans is encoded by the E4F1 gene.

Function

The zinc finger protein encoded by this gene is one of several cellular transcription factors whose DNA-binding activities are regulated through the action of adenovirus E1A. A 50-kDa amino-terminal product is generated from the full-length protein through proteolytic cleavage. The protein is differentially regulated by E1A-induced phosphorylation. The full-length gene product represses transcription from the E4 promoter in the absence of E1A, while the 50-kDa form acts as a transcriptional activator in its presence.

Interactions

E4F1 has been shown to interact with:

References

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

E2F1

Transcription factor E2F1 is a protein that in humans is encoded by the E2F1 gene.

Function

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis.

E2F5

Transcription factor E2F5 is a protein that in humans is encoded by the E2F5 gene.

Function

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionarily conserved domains that are present in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein is differentially phosphorylated and is expressed in a wide variety of human tissues. It has higher identity to E2F4 than to other family members. Both this protein and E2F4 interact with tumor suppressor proteins p130 and p107, but not with pRB. Alternative splicing results in multiple variants encoding different isoforms.