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Institution

University of California, San Francisco

EducationSan Francisco, California, United States
About: University of California, San Francisco is a education organization based out in San Francisco, California, United States. It is known for research contribution in the topics: Population & Health care. The organization has 83381 authors who have published 186236 publications receiving 12068420 citations. The organization is also known as: UCSF & UC San Francisco.


Papers
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Journal ArticleDOI
19 Mar 1999-Cell
TL;DR: The characterization of three mammalian Slit homologs are described and it is shown that the Drosophila Slit protein and at least one of the mammals Slit proteins, Slit2, are proteolytically processed and show specific, high-affinity binding to Robo proteins.

1,167 citations

Journal ArticleDOI
TL;DR: Recent developments with InterPro (version 70.0) and its associated software are reported, including an 18% growth in the size of the database in terms on new InterPro entries, updates to content, the inclusion of an additional entry type, refined modelling of discontinuous domains, and the development of a new programmatic interface and website.
Abstract: The InterPro database (http://www.ebi.ac.uk/interpro/) classifies protein sequences into families and predicts the presence of functionally important domains and sites. Here, we report recent developments with InterPro (version 70.0) and its associated software, including an 18% growth in the size of the database in terms on new InterPro entries, updates to content, the inclusion of an additional entry type, refined modelling of discontinuous domains, and the development of a new programmatic interface and website. These developments extend and enrich the information provided by InterPro, and provide greater flexibility in terms of data access. We also show that InterPro's sequence coverage has kept pace with the growth of UniProtKB, and discuss how our evaluation of residue coverage may help guide future curation activities.

1,167 citations

Journal ArticleDOI
TL;DR: It is shown that overexpression of FAD(717V-->F)-mutant human APP in neurons of transgenic mice decreases the density of presynaptic terminals and neurons well before these mice develop amyloid plaques, suggesting a neurotoxic effect of Abeta that is independent of plaque formation.
Abstract: Autosomal dominant forms of familial Alzheimer’s disease (FAD) are associated with increased production of the amyloid β peptide, Aβ42, which is derived from the amyloid protein precursor (APP). In FAD, as well as in sporadic forms of the illness, Aβ peptides accumulate abnormally in the brain in the form of amyloid plaques. Here, we show that overexpression of FAD(717V→F)-mutant human APP in neurons of transgenic mice decreases the density of presynaptic terminals and neurons well before these mice develop amyloid plaques. Electrophysiological recordings from the hippocampus revealed prominent deficits in synaptic transmission, which also preceded amyloid deposition by several months. Although in young mice, functional and structural neuronal deficits were of similar magnitude, functional deficits became predominant with advancing age. Increased Aβ production in the context of decreased overall APP expression, achieved by addition of the Swedish FAD mutation to the APP transgene in a second line of mice, further increased synaptic transmission deficits in young APP mice without plaques. These results suggest a neurotoxic effect of Aβ that is independent of plaque formation.

1,165 citations

Journal ArticleDOI
TL;DR: The National Kidney Foundation-KDOQI guideline for evaluation, classification, and stratification of chronic kidney disease (CKD) was published in 2002 as mentioned in this paper, but concerns and criticisms arose as new evidence became available since the publication of the original guidelines.

1,165 citations

Journal ArticleDOI
TL;DR: The diffusion behavior of intracranial water in the cat brain and spine was examined with the use of diffusion-weighted magnetic resonance (MR) imaging, in which the direction of the diffusion-sensitizing gradient was varied between the x, y, and z axes of the magnet.
Abstract: The diffusion behavior of intracranial water in the cat brain and spine was examined with the use of diffusion-weighted magnetic resonance (MR) imaging, in which the direction of the diffusion-sensitizing gradient was varied between the x, y, and z axes of the magnet. At very high diffusion-sensitizing gradient strengths, no clear evidence of anisotropic water diffusion was found in either cortical or subcortical (basal ganglia) gray matter. Signal intensities clearly dependent on orientation were observed in the cortical and deep white matter of the brain and in the white matter of the spinal cord. Greater signal attenuation (faster diffusion) was observed when the relative orientation of white matter tracts to the diffusion-sensitizing gradient was parallel as compared to that obtained with a perpendicular alignment. These effects were seen on both premortem and immediate postmortem images obtained in all axial, sagittal, and coronal views. Potential applications of this MR imaging technique included the stereospecific evaluation of white matter in the brain and spinal cord and in the characterization of demyelinating and dysmyelinating diseases.

1,164 citations


Authors

Showing all 84066 results

NameH-indexPapersCitations
Robert Langer2812324326306
Meir J. Stampfer2771414283776
Gordon H. Guyatt2311620228631
Eugene Braunwald2301711264576
John Q. Trojanowski2261467213948
Fred H. Gage216967185732
Robert J. Lefkowitz214860147995
Peter Libby211932182724
Edward Giovannucci2061671179875
Rob Knight2011061253207
Irving L. Weissman2011141172504
Eugene V. Koonin1991063175111
Peter J. Barnes1941530166618
Virginia M.-Y. Lee194993148820
Gordon B. Mills1871273186451
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20241
2023179
2022981
202111,518
202010,575
20199,343