Neuronal loss and brain atrophy in mice lacking cathepsins B and L - Wikidata - awgldk - TriplyDB

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

http://www.wikidata.org/entity/Q34030250

about

The cysteine protease cathepsin B is a key drug target and cysteine protease inhibitors are potential therapeutics for traumatic brain injury Cathepsin B is a New Drug Target for Traumatic Brain Injury Therapeutics: Evidence for E64d as a Promising Lead Drug Candidate Cathepsin L plays a role in quinolinic acid-induced NF-Κb activation and excitotoxicity in rat striatal neurons Autophagy in the Pathogenesis of Disease Reduced cathepsins B and D cause impaired autophagic degradation that can be almost completely restored by overexpression of these two proteases in Sap C-deficient fibroblasts Running-Induced Systemic Cathepsin B Secretion Is Associated with Memory Function Identification of a myeloid-derived suppressor cell cystatin-like protein that inhibits metastasis Expression of cathepsin P mRNA, protein and activity in the rat choriocarcinoma cell line, Rcho-1, during giant cell transformation Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation Profiling trait anxiety: transcriptome analysis reveals cathepsin B (Ctsb) as a novel candidate gene for emotionality in mice Expression Analysis of All Protease Genes Reveals Cathepsin K to Be Overexpressed in Glioblastoma Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9 Murine cathepsin F deficiency causes neuronal lipofuscinosis and late-onset neurological disease.Integrated single cell data analysis reveals cell specific networks and novel coactivation markers Differential cerebral cortex transcriptomes of baboon neonates consuming moderate and high docosahexaenoic acid formulas.Protein processing by the placental protease, cathepsin P.Cathepsin L inhibition suppresses drug resistance in vitro and in vivo: a putative mechanism.Do molecular signals from the conceptus influence endometrium decidualization in rodents?Cathepsin-D, a key protease in breast cancer, is up-regulated in obese mouse and human adipose tissue, and controls adipogenesis Deletion of PIK3C3/Vps34 in sensory neurons causes rapid neurodegeneration by disrupting the endosomal but not the autophagic pathway Cathepsin K deficiency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory deficits Focal cerebral ischemia induces active proteases that degrade microvascular matrix.Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits Distinct roles for cysteine cathepsin genes in multistage tumorigenesis Cathepsin B & L are not required for ebola virus replication Structural basis of reduction-dependent activation of human cystatin F.Cathepsin deficiency as a model for neuronal ceroid lipofuscinoses.Identification of a small molecule that induces ATG5-and-cathepsin-l-dependent cell death and modulates polyglutamine toxicity.Autophagy failure in Alzheimer's disease--locating the primary defect.Thyroid functions of mouse cathepsins B, K, and L.Family C1 cysteine proteases: biological diversity or redundancy?Cathepsin L suppression increases the radiosensitivity of human glioma U251 cells via G2/M cell cycle arrest and DNA damage.A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin.Excessive activity of cathepsin K is associated with cartilage defects in a zebrafish model of mucolipidosis II.Up-regulation of microglial cathepsin C expression and activity in lipopolysaccharide-induced neuroinflammation.Proteolytic mechanisms in necrotic cell death and neurodegeneration.Loss of Cathepsin B and L Leads to Lysosomal Dysfunction, NPC-Like Cholesterol Sequestration and Accumulation of the Key Alzheimer's Proteins Cathepsin L targeting in cancer treatment.Cathepsin L acutely alters microvessel integrity within the neurovascular unit during focal cerebral ischemia.

P2860

Q24601910-68A96914-29DB-424C-9C07-87E17575DF9E Q26782938-097E610C-0B82-4871-B773-1695195950AC Q27305158-FBB27279-AB64-4A70-9C7C-BD7CFBFA328B Q27860558-A3882E16-EE74-41F2-9C22-9DC2DAA2C803 Q28116738-A7A86E51-857E-4204-B134-B8D6A6CD4C82 Q28276622-D086DF97-7855-4813-8B69-B50243611081 Q28506334-C2E60FB5-3B71-4A3A-9B03-2C25F6A0054B Q28575366-6D7FC703-ADCB-4533-8355-D1B1F792B4AC Q28588877-49041CD2-5970-4175-8061-F3478040723F Q28590081-99C8DEBB-5043-40F3-BFC3-0BC75203B1AF Q28740918-1B9CCAD6-0914-450F-963D-407343A9AD0D Q29302290-D7C80D43-26A0-41DB-AA84-A9F1398636B0 Q29347250-24E61375-747C-4E57-90F8-8469819B5B54 Q30477117-824BFD2B-A846-4E5A-AAB0-9D4B3B7575E1 Q31155537-1F6A31D2-EF18-4903-BB8A-5DF594FB2A5D Q33281757-DDD3775C-BCD7-40F4-9873-839E5624BB69 Q33426731-0C3F6DDE-391F-446C-839E-EC375E0641B3 Q33703811-71C4D55B-7A10-4774-ABA4-F5505220ACCB Q33750485-8648AECE-0501-4AEB-A547-E551DF777B07 Q33818227-7F6B7811-8F74-4EE5-8EB9-BF1705A3A5CE Q33927079-BEA871BE-FA2B-4019-A840-6BDDDFAFB5BF Q33973023-E8FB2A59-286D-4B71-9A4D-B17D59C4B13C Q34301092-701EBD30-B212-4B01-A296-9FC1ED0AA72F Q34438646-117BD3CD-4A08-48E8-96DD-2DF6390DD7CE Q34471105-9C80936B-CB80-45AE-80B3-1107C7375B3F Q34511122-EEE96648-8596-4808-999C-8C24B9CE83CA Q34511593-443447BD-4F4F-4D64-96FC-78DF3228E138 Q34562951-5A40FE54-65AD-400D-8FDA-8D7696056C88 Q34669749-E3C941C8-FBEE-4D59-AF4C-5D97828AFF16 Q34987827-461C7B4E-0ACB-4AEC-AC05-9F6A0B576E46 Q35019251-5441F3DB-E528-4DFD-A629-3AFD77F05EAC Q35187211-7563C7B6-B121-446C-8965-6F5584E784B3 Q35669806-1BC1155D-D793-4C9B-BB46-AE08145D90D2 Q35778765-109FEDFF-0E99-4EEA-BCD6-442B7F80DA04 Q35794555-49C33DD5-83A0-4F08-8125-2F94CE8AA8FC Q36136789-DC197514-E70C-4B2A-8AA3-1CB437E8DEA0 Q36156010-7208756B-50A8-4D83-BE4C-89D323F2C84D Q36208265-4745E6C6-5691-4DBC-AF22-8C6A161BB33F Q36218199-77C6DBFC-3F13-42AD-9274-85FD1ED10DB3 Q36254387-58E8D936-4A84-4F1B-803F-71872A11DD40

P2860

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

http://www.wikidata.org/entity/Q34030250

description

2002 nî lūn-bûn

@nan

2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@ast

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@en

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@nl

type

label

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@ast

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@en

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@nl

prefLabel

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@ast

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@en

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@nl

P1433

Q34030250-AFE41AC2-1425-422A-B248-53EBEADB30C8

P1476

Q34030250-2AC83CCC-10A6-4AE9-AB07-DA6335FBC0F9

P2093

Q34030250-16AD4010-740B-4188-A892-EE18F669F360

Q34030250-3DA3A261-7E99-4827-BC1E-D43F615D2690

Q34030250-92C7BECB-1532-4C08-8671-A938BB08B6C1

Q34030250-CF6BB8CD-78F3-4B10-BC86-260C0759E003

Q34030250-DB4DA4EE-7CF6-4FA8-8A36-75C22239E5AC

P2860

Q34030250-08618250-83F0-4B5E-8232-CC885A5B759E

Q34030250-09CE98DD-7A2F-4653-9A3B-B042F4CEAAD4

Q34030250-09D34F00-FB99-4C2E-921E-84E4ECBA1FEB

Q34030250-0AD3C8D3-4346-4FD3-B264-6076DCC01B74

Q34030250-18A4C0AD-EE7D-43BD-A24C-A28937467673

Q34030250-1B0397F5-82A9-4C0A-8A53-E7954F5C9459

Q34030250-1E903F75-73FD-4F3F-85CC-A4FD03B5C08D

Q34030250-27AAE7B5-A7E4-4348-A574-A52C6DE757D1

Q34030250-27B9E39A-0D8A-4E81-853D-A6E718762535

Q34030250-291FDA45-B642-4F67-879A-F630A4EBFDDF

P304

Q34030250-77D301E3-13FC-41B2-A454-0A90D5F62FDA

P31

Q34030250-95BD389F-ABFF-4063-B38D-D6AA362F0452

P356

Q34030250-73756768-2C15-44F7-87FD-BB11C24D6F79

P407

Q34030250-7459F7C1-A5E4-46C1-82A1-97117A355788

P433

Q34030250-F0DD28DC-81C3-42A6-8670-B6C84F02C663

P478

Q34030250-86388858-161A-49A7-8E76-4D391990124A

P50

Q34030250-B6F23CA9-6F14-4E0C-9BD5-CA8883FF05DA

Q34030250-F44D11CC-78BD-4D79-9524-6BE781FA7E88

P577

Q34030250-2FA8ED57-D7BE-4377-A523-C519434DB5BE

P5875

Q34030250-8EAD5C7F-8D98-49CD-B6AA-570D8983388F

P698

Q34030250-CE30A3AE-7176-4835-AA13-F3E3560332E4

P932

Q34030250-AC4622F6-A375-4A3A-A343-9202A4EFDB56

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Neuronal loss and brain atrophy in mice lacking cathepsins B and L

@en

P2093

Bjorn R Olsen

http://www.w3.org/2001/XMLSchema#string

Hans H Goebel

http://www.w3.org/2001/XMLSchema#string

Hidde L Ploegh

http://www.w3.org/2001/XMLSchema#string

Roderick T Bronson

http://www.w3.org/2001/XMLSchema#string

Ute Felbor

http://www.w3.org/2001/XMLSchema#string

P2860

Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I

Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis

Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis

Secreted cathepsin L generates endostatin from collagen XVIII

Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation

Cathepsin expression during skeletal development

Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis

Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency

Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells

Two related proteolipids and dolichol-linked oligosaccharides accumulate in motor neuron degeneration mice (mnd/mnd), a model for neuronal ceroid lipofuscinosis

P304

7883-7888

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.112632299

http://www.w3.org/2001/XMLSchema#string

P407

P433

12

http://www.w3.org/2001/XMLSchema#string

P478

99

http://www.w3.org/2001/XMLSchema#string

P50

Benedikt M. Kessler

P577

2002-06-04T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11325696

http://www.w3.org/2001/XMLSchema#string

P698

12048238

http://www.w3.org/2001/XMLSchema#string

P932

122989

http://www.w3.org/2001/XMLSchema#string