Antibody response to epitopes of chlamydial major outer membrane proteins on infectious elementary bodies and of the reduced polyacrylamide gel electrophoresis-separated form.
about
Prediction of the membrane-spanning beta-strands of the major outer membrane protein of Chlamydia.Truncation of the carboxy-terminal 28 amino acids of glycoprotein B specified by herpes simplex virus type 1 mutant amb1511-7 causes extensive cell fusion.Detection and strain differentiation of Chlamydia psittaci mediated by a two-step polymerase chain reaction.Herpes simplex virus type 1 glycoprotein K is not essential for infectious virus production in actively replicating cells but is required for efficient envelopment and translocation of infectious virions from the cytoplasm to the extracellular space
P2860
Antibody response to epitopes of chlamydial major outer membrane proteins on infectious elementary bodies and of the reduced polyacrylamide gel electrophoresis-separated form.
description
article científic
@ca
article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1990
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
@da
vědecký článek
@cs
name
Antibody response to epitopes ...... lectrophoresis-separated form.
@en
Antibody response to epitopes ...... lectrophoresis-separated form.
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type
label
Antibody response to epitopes ...... lectrophoresis-separated form.
@en
Antibody response to epitopes ...... lectrophoresis-separated form.
@nl
prefLabel
Antibody response to epitopes ...... lectrophoresis-separated form.
@en
Antibody response to epitopes ...... lectrophoresis-separated form.
@nl
P2093
P2860
P1476
Antibody response to epitopes ...... lectrophoresis-separated form.
@en
P2093
P2860
P304
P407
P577
1990-05-01T00:00:00Z