Zobrazeno 1 - 10
of 81
pro vyhledávání: '"John T. Finch"'
Autor:
Ulf Skoglund, Dmitri I. Svergun, Ermanno Gherardi, Mark Youles, Maxim V. Petoukhov, John T. Finch, Tom L. Blundell, Ricardo Núñez Miguel, George F. Vande Woude, Sara Sandin, Lars-Göran Öfverstedt
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America 103, 4051 (2006). doi:10.1073/pnas.0509040103
The polypeptide growth factor, hepatocyte growth factor/scatter factor (HGF/SF), shares the multidomain structure and proteolytic mechanism of activation of plasminogen and other complex serine proteinases. HGF/SF, however, has no enzymatic activity.
Autor:
John T. Finch, Linda A. Amos
Publikováno v:
Trends in Cell Biology. 14:148-152
Aaron Klug's group was one of the first to use a combination of X-ray diffraction and electron microscopy to study the structures of macromolecules. He helped to provide the intellectual framework for understanding the self-assembly of regular viruse
Publikováno v:
Mechanisms of Development. 117(1-2):87-101
Each sensory organ of the Drosophila peripheral nervous system is derived from a single sensory organ precursor cell (SOP). These originate in territories defined by expression of the proneural genes of the Achaete-Scute complex (AS-C). Formation of
Autor:
John T. Finch, Ashley J. Wilson, David J. Scott, Jean L. Whittingham, Guy Dodson, Jens Brange, Karen Chance
Publikováno v:
Journal of Molecular Biology. 318:479-490
When insulin solutions are subjected to acid, heat and agitation, the normal pattern of insulin assembly (dimers-->tetramers-->hexamers) is disrupted; the molecule undergoes conformational changes allowing it to follow an alternative aggregation path
Publikováno v:
Nature. 407:409-413
The type 1 human immunodeficiency virus (HIV-1) contains a conical capsid comprising approximately 1,500 CA protein subunits, which organizes the viral RNA genome for uncoating and replication in a new host cell. In vitro, CA spontaneously assembles
Publikováno v:
Journal of Molecular Biology. 292:263-273
Importin-α is a cytosolic receptor that recognizes classical Nuclear Localization Signals (NLSs) and mediates import into the nucleus. We have used a number of methods to investigate the aggregation state of Xenopus importin-α both as a recombinant
Autor:
David A. Lomas, Robin W. Carrell, Diane W. Cox, James C. Whisstock, Richard C. Foreman, John T. Finch, Peter R. Elliott, Sanjiv K. Sidhar
Publikováno v:
Journal of Biological Chemistry. 270:16864-16870
The Z (Glu342-->Lys) and Siiyama (Ser53-->Phe) deficiency variants of alpha 1-antitrypsin result in the retention of protein in the endoplasmic reticulum of the hepatocyte by loop-sheet polymerization in which the reactive center loop of one molecule
Publikováno v:
Nature. 366:483-487
THE Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif1–3. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition4 suggesting that the zinc-finger might represent a candidate templa
Publikováno v:
Structure. 1:187-204
Background: The steroid/nuclear hormone receptors are a large family of conserved ligand-activated transcription factors that regulate gene expression through binding to response elements upstream of their target genes. Most members of this family bi
Publikováno v:
The Journal of Cell Biology
Monoclonal antibodies against the 110-kD component of the yeast spindle pole body (SPB) were used to clone the corresponding gene SPC110. SPC110 is identical to NUF1 (Mirzayan, C., C. S. Copeland, and M. Synder. 1992. J. Cell Biol. 116:1319-1332). SP