I. Sohar

发表

Stretch-induced prostaglandins and protein turnover in cultured skeletal muscle.

H. Vandenburgh, J. Shansky, S. Hatfaludy, 1990, The American journal of physiology.

Intrathecal tripeptidyl-peptidase 1 reduces lysosomal storage in a canine model of late infantile neuronal ceroid lipofuscinosis.

S. Bunting, C. O’Neill, L. Tsuruda, 2011, Molecular genetics and metabolism.

Effective intravenous therapy for neurodegenerative disease with a therapeutic enzyme and a peptide that mediates delivery to the brain.

R. Jenkins, K. Reuhl, G. Sarkar, 2014, Molecular therapy : the journal of the American Society of Gene Therapy.

Mouse mutants lacking the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor are impaired in lysosomal enzyme transport: comparison of cation-independent and cation-dependent mannose 6-phosphate receptor-deficient mice.

D. Sleat, P. Lobel, T. Ludwig, 1998, The Biochemical journal.

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

R. Donnelly, D. Sleat, P. Lobel, 1997, Science.

Proteomic Analysis of Brain and Cerebrospinal Fluid from the Three Major Forms of Neuronal Ceroid Lipofuscinosis Reveals Potential Biomarkers.

Caifeng Zhao, K. Sims, D. Sleat, 2017, Journal of proteome research.

Tripeptidyl Peptidase I

D. Sleat, P. Lobel, I. Sohar, 2013 .

Rat Brain Contains High Levels of Mannose-6-phosphorylated Glycoproteins Including Lysosomal Enzymes and Palmitoyl-Protein Thioesterase, an Enzyme Implicated in Infantile Neuronal Lipofuscinosis*

J. Majercak, D. Sleat, P. Lobel, 1996, The Journal of Biological Chemistry.

alpha-Glucosidase and N-acetylglucosamine-6-sulphatase are the major mannose-6-phosphate glycoproteins in human urine.

S. Kraus, D. Sleat, P. Lobel, 1997, The Biochemical journal.

Loss of Niemann-Pick C1 or C2 Protein Results in Similar Biochemical Changes Suggesting That These Proteins Function in a Common Lysosomal Pathway

M. Jadot, D. Sleat, P. Lobel, 2011, PloS one.

Determination of the Substrate Specificity of Tripeptidyl-peptidase I Using Combinatorial Peptide Libraries and Development of Improved Fluorogenic Substrates*

John W. Taylor, P. Lobel, I. Sohar, 2006, Journal of Biological Chemistry.

Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.

T. Lerner, P. Uldall, R. Donnelly, 1999, American journal of human genetics.

Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus.

J. Kiss, N. Sohár, I. Sohar, 2005, World journal of gastroenterology.

Activity of the lysosomal cysteine proteinases (cathepsin B,H,L) and a metalloproteinase (MMP-7-ase) in the serum of cystic fibrosis homozygous children.

K. Gyurkovits, I. Sohar, A. László, 1987, Acta paediatrica Hungarica.

A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration

M. Baumann, D. Sleat, P. Lobel, 2000, The EMBO journal.

Enzyme-based diagnosis of classical late infantile neuronal ceroid lipofuscinosis: comparison of tripeptidyl peptidase I and pepstatin-insensitive protease assays.

P. Lobel, I. Sohar, L. Lin, 2000, Clinical chemistry.

Quantitation of oxidative damage to tissue proteins.

J. Fagan, I. Sohar, B. Sleczka, 1999, The international journal of biochemistry & cell biology.

Timing of therapeutic intervention determines functional and survival outcomes in a mouse model of late infantile batten disease.

B. Davidson, R. Scheule, L. Shihabuddin, 2007, Molecular therapy : the journal of the American Society of Gene Therapy.

Lysosomal Peptidases and Glycosidases in Rheumatoid Arthritis

N. Sohár, I. Sohar, H. Hammer, 2002, Biological chemistry.

Experimental investigations on hypokinesis of skeletal muscles with different function. IV. Changes in the sarcoplasmic proteins.

T. Szilágyi, I. Sohar, O. Takács, 1977, Acta biologica Academiae Scientiarum Hungaricae.

Changes in exopeptidase activities in skeletal muscles during disuse.

I. Sohar, R. Haschen, F. Guba, 1986, The International journal of biochemistry.

A frame shift mutation in canine TPP1 (the ortholog of human CLN2) in a juvenile Dachshund with neuronal ceroid lipofuscinosis.

G. Johnson, U. Giger, P. Lobel, 2006, Molecular genetics and metabolism.

A mutation in the cathepsin D gene (CTSD) in American Bulldogs with neuronal ceroid lipofuscinosis.

G. Johnson, P. Lobel, M. Katz, 2006, Molecular genetics and metabolism.

Large-volume intrathecal enzyme delivery increases survival of a mouse model of late infantile neuronal ceroid lipofuscinosis.

Lingling Wang, D. Sleat, P. Lobel, 2011, Molecular therapy : the journal of the American Society of Gene Therapy.

Lysosomal enzyme activities: new potential markers for Sjögren's syndrome.

N. Sohár, I. Sohar, H. Hammer, 2005, Clinical biochemistry.

Metabolic changes in the lower esophageal sphincter influencing the result of anti-reflux surgical interventions in chronic gastroesophageal reflux disease.

I. Sohar, G. Sohár, Á. Altorjay, 2005, World journal of gastroenterology.

Specific alterations in levels of mannose 6-phosphorylated glycoproteins in different neuronal ceroid lipofuscinoses.

D. Sleat, P. Lobel, I. Sohar, 1998, The Biochemical journal.

Aminoglycoside-mediated suppression of nonsense mutations in late infantile neuronal ceroid lipofuscinosis.

D. Sleat, P. Lobel, I. Sohar, 2001, European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society.

Biochemical Characterization of a Lysosomal Protease Deficient in Classical Late Infantile Neuronal Ceroid Lipofuscinosis (LINCL) and Development of an Enzyme‐Based Assay for Diagnosis and Exclusion of LINCL in HUman Specimens and Animal Models

M. Jadot, D. Sleat, P. Lobel, 1999, Journal of neurochemistry.

Prenatal testing for late infantile neuronal ceroid lipofuscinosis

R. Donnelly, E. Berry-Kravis, D. Sleat, 2000, Annals of neurology.

The Human CLN2 Protein/Tripeptidyl-Peptidase I Is a Serine Protease That Autoactivates at Acidic pH*

P. Lobel, I. Sohar, Li Lin, 2001, The Journal of Biological Chemistry.

Systemic Administration of Tripeptidyl Peptidase I in a Mouse Model of Late Infantile Neuronal Ceroid Lipofuscinosis: Effect of Glycan Modification

D. Sleat, P. Lobel, Y. Meng, 2012, PloS one.

Crystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid Lipofuscinosis

Ann M Stock, K. Das, J. Guhaniyogi, 2009, Journal of Biological Chemistry.

Residual levels of tripeptidyl-peptidase I activity dramatically ameliorate disease in late-infantile neuronal ceroid lipofuscinosis.

S. Walkley, D. Sleat, P. Lobel, 2008, Molecular genetics and metabolism.

Demonstration of Lysosomal Localization for the Mammalian Ependymin-related Protein Using Classical Approaches Combined with a Novel Density Shift Method*

J. Pintar, M. Jadot, D. Sleat, 2006, Journal of Biological Chemistry.

Use of Combinatorial Peptide Libraries and LC/MS/MS to Study TPP I Substrate Specificity

P. Lobel, I. Sohar, Yu Tian, 2006 .

The human brain mannose 6‐phosphate glycoproteome: A complex mixture composed of multiple isoforms of many soluble lysosomal proteins

Hong Li, D. Sleat, P. Lobel, 2005, Proteomics.

Distribution of serum amylase isoenzymes in cystic fibrosis homozygotes and heterozygotes.

K. Gyurkovits, A. László, I. Sohar, 1977, Acta paediatrica Academiae Scientiarum Hungaricae.

Identification and Validation of Mannose 6-Phosphate Glycoproteins in Human Plasma Reveal a Wide Range of Lysosomal and Non-lysosomal Proteins*S

Hong Li, D. Sleat, Haiyan Zheng, 2006, Molecular & Cellular Proteomics.

Activation of microglia acidifies lysosomes and leads to degradation of Alzheimer amyloid fibrils.

F. Maxfield, P. Lobel, A. Majumdar, 2007, Molecular biology of the cell.

Cathepsin-B activity in otosclerosis

O. Ribári, J. Kiss, I. Sohar, 1983, Archives of oto-rhino-laryngology.

The influence of immobilization on soluble proteins of muscle.

I. Sohar, O. Takács, F. Guba, 1977, Acta biologica et medica Germanica.

Cysteine and metalloproteinase activities in serum of Duchenne muscular dystrophic genotypes.

F. Mechler, I. Sohar, K. Gaál, 1988, Biological chemistry Hoppe-Seyler.

Effect of vitamin E-deficiency on the activity of some lysosomal and non-lysosomal proteases in rabbit muscles.

I. Sohar, G. Katona, F. Guba, 1991, General physiology and biophysics.

Proteomic analysis of mouse models of Niemann‐Pick C disease reveals alterations in the steady‐state levels of lysosomal proteins within the brain

D. Sleat, Haiyan Zheng, D. Moore, 2012, Proteomics.

Regulation of proteinase activation in mammalian tissues.

I. Sohar, G. Katona, 1992, Biological chemistry Hoppe-Seyler.

Subcellular Localization of Mannose 6-Phosphate Glycoproteins in Rat Brain*

J. Pintar, R. Wattiaux, M. Jadot, 1999, The Journal of Biological Chemistry.

Proteases and proteinase inhibitors in experimental glucocorticosteroid myopathy.

I. Nagy, L. Heiner, I. Sohar, 1982, Acta physiologica Academiae Scientiarum Hungaricae.

Activity of cathepsin H,B and metalloproteinase in the serum of patients with acute myocardial infarction.

I. Sagi, Á. Kov́acs, I. Sohar, 1992, Clinica chimica acta; international journal of clinical chemistry.

Proteinase activities in normal and dystrophic chicken myoblasts in culture.

F. Roisen, G. Yorke, I. Sohar, 1985, Progress in clinical and biological research.

Localization of cysteine proteinases and an endogenous cysteine proteinase inhibitor in cultured muscle cells.

F. Roisen, G. Yorke, I. Sohar, 1985, Biochemical Society transactions.

Congenital ovine neuronal ceroid lipofuscinosis--a cathepsin D deficiency with increased levels of the inactive enzyme.

M. Baumann, R. Donnelly, D. Sleat, 2001, European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society.