Sensitization of cells and retroviruses to human serum by (alpha 1-3) galactosyltransferase. (Q41240724)

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14 October 2019

title

Sensitization of cells and retroviruses to human serum by (alpha 1-3) galactosyltransferase (English)

1 reference

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14 October 2019

4

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14 October 2019

François-Loic Cosset

6

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14 October 2019

author name string

Takeuchi Y

1

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14 October 2019

Porter CD

2

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14 October 2019

Strahan KM

3

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14 October 2019

Gustafsson K

5

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14 October 2019

Weiss RA

7

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Collins MK

8

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language of work or name

English

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publication date

1 January 1996

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14 October 2019

number of pages

4

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inferred from page(s)

published in

Nature

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volume

379

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14 October 2019

issue

6560

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14 October 2019

page(s)

85-88

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Human serum lyses RNA tumour viruses

14 October 2019

cites work

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Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys

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Alpha 1,3galactosyltransferase: a target for in vivo genetic manipulation in xenotransplantation.

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cDNA sequence and chromosome localization of pig alpha 1,3 galactosyltransferase.

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Gal alpha (1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies

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Human natural anti-Gal IgG regulates alternative complement pathway activation on bacterial surfaces

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Glycoconjugates of Trypanosoma cruzi: a 74 kD antigen of trypomastigotes specifically reacts with lytic anti-alpha-galactosyl antibodies from patients with chronic Chagas disease

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Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation.

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Anti-pig IgM antibodies in human serum react predominantly with Gal(alpha 1-3)Gal epitopes

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Differential host-dependent expression of alpha-galactosyl epitopes on viral glycoproteins: a study of eastern equine encephalitis virus as a model

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Nudging xenotransplantation towards humans

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Human complement regulatory proteins protect swine-to-primate cardiac xenografts from humoral injury

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Retroviral retargeting by envelopes expressing an N-terminal binding domain.

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Human lymphocytotoxic and haemagglutinating activity against sheep and pig cells

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