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Book ; Thesis: Starch branching enzymes in Solanum tuberosum and arabidopsis thaliana

Khoshnoodi, Jamshid

(Acta Universitatis Agriculturae Sueciae : Agraria ; 58)

1997

Author's details	Jamshid Khoshnoodi
Series title	Acta Universitatis Agriculturae Sueciae : Agraria ; 58 Acta Universitatis Agriculturae Sueciae Acta Universitatis Agriculturae Sueciae ; Agraria
Collection	Acta Universitatis Agriculturae Sueciae Acta Universitatis Agriculturae Sueciae ; Agraria
Size	Getr. Zählung : Ill., graph. Darst.
Publishing place	Uppsala
Publishing country	Sweden
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Uppsala, Swedish Univ. of Agricultural Sciences, Diss., 1997
HBZ-ID	HT008174982
ISBN	91-576-5277-5 ; 978-91-576-5277-5
Database	Catalogue ZB MED Nutrition, Environment, Agriculture

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Shelf mark	Loan status	Location
988/830	available for loan (reading room)	Freihandmagazin (U1)

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Article ; Online: Semimembranosus tendon avulsion fracture of the posteromedial tibial plateau associated with posterior cruciate ligament tear and capsular rupture.

Khoshnoodi, Pooria / Tehranzadeh, Arash D / Dunn, James M / Tehranzadeh, Jamshid

Skeletal radiology

2013 Volume 43, Issue 2, Page(s) 239–242

Abstract: Semimembranosus tendon avulsion fractures are an uncommon occurrence and are often associated with anterior cruciate ligament (ACL) and medial meniscus tears. We present the imaging features of an unusual case of semimembranosus avulsion fracture of the ... ...

Abstract	Semimembranosus tendon avulsion fractures are an uncommon occurrence and are often associated with anterior cruciate ligament (ACL) and medial meniscus tears. We present the imaging features of an unusual case of semimembranosus avulsion fracture of the posteromedial tibial plateau associated with posterior cruciate ligament (PCL) tear, medial meniscus tear, and capsular rupture in a 26-year-old man with a football injury.
MeSH term(s)	Adult ; Football/injuries ; Humans ; Knee Injuries/complications ; Knee Injuries/diagnosis ; Male ; Multiple Trauma/diagnosis ; Posterior Cruciate Ligament/diagnostic imaging ; Posterior Cruciate Ligament/injuries ; Posterior Cruciate Ligament/pathology ; Radiography ; Rupture ; Tendon Injuries/complications ; Tendon Injuries/diagnosis ; Tibial Fractures/diagnosis
Language	English
Publishing date	2013-09-12
Publishing country	Germany
Document type	Case Reports ; Journal Article
ZDB-ID	527592-1
ISSN	1432-2161 ; 0364-2348
ISSN (online)	1432-2161
ISSN	0364-2348
DOI	10.1007/s00256-013-1719-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 1304: Show issues

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Book ; Thesis: Starch branching enzymes in Solanum tuberosum and Arabidopsis thaliana

Khoshnoodi, Jamshid

(Acta Universitatis Agriculturae Sueciae : Agraria ; 58)

1997

Author's details	Jamshid Khoshnoodi
Series title	Acta Universitatis Agriculturae Sueciae : Agraria ; 58
Language	English
Size	Getr. Zählung, Ill., graph. Darst
Publisher	SLU Repro
Publishing place	Uppsala
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Swedish Univ. of Agricultural Sciences, Diss.--Uppsala, 1997
ISBN	9157652775 ; 9789157652775
Database	Special collection on veterinary medicine and general parasitology

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Article: Mammalian collagen IV.

Khoshnoodi, Jamshid / Pedchenko, Vadim / Hudson, Billy G

Microscopy research and technique

2007 Volume 71, Issue 5, Page(s) 357–370

Abstract: Four decades have passed since the first discovery of collagen IV by Kefalides in 1966. Since then collagen IV has been investigated extensively by a large number of research laboratories around the world. Advances in molecular genetics have resulted in ... ...

Abstract	Four decades have passed since the first discovery of collagen IV by Kefalides in 1966. Since then collagen IV has been investigated extensively by a large number of research laboratories around the world. Advances in molecular genetics have resulted in identification of six evolutionary related mammalian genes encoding six different polypeptide chains of collagen IV. The genes are differentially expressed during the embryonic development, providing different tissues with specific collagen IV networks each having unique biochemical properties. Newly translated alpha-chains interact and assemble in the endoplasmic reticulum in a chain-specific fashion and form unique heterotrimers. Unlike most collagens, type IV collagen is an exclusive member of the basement membranes and through a complex inter- and intramolecular interactions form supramolecular networks that influence cell adhesion, migration, and differentiation. Collagen IV is directly involved in a number of genetic and acquired disease such as Alport's and Goodpasture's syndromes. Recent discoveries have also highlighted a new and direct role for collagen IV in the development of rare genetic diseases such as cerebral hemorrhage and porencephaly in infants and hemorrhagic stroke in adults. Years of intensive investigations have resulted in a vast body of information about the structure, function, and biology of collagen IV. In this review article, we will summarize essential findings on the structural and functional relationships of different collagen IV chains and their roles in health and disease.
MeSH term(s)	Animals ; Anti-Glomerular Basement Membrane Disease/genetics ; Anti-Glomerular Basement Membrane Disease/metabolism ; Chromosomes, Human ; Collagen Type IV/chemistry ; Collagen Type IV/genetics ; Collagen Type IV/metabolism ; Gene Expression Regulation, Developmental ; Genetic Diseases, Inborn/genetics ; Genetic Diseases, Inborn/metabolism ; Humans ; Integrins/metabolism ; Mammals/embryology ; Mammals/genetics ; Mammals/metabolism ; Multigene Family ; Nephritis, Hereditary/genetics ; Nephritis, Hereditary/metabolism ; Protein Conformation ; Protein Processing, Post-Translational
Chemical Substances	Collagen Type IV ; Integrins
Language	English
Publishing date	2007-10-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1099714-3
ISSN	1097-0029 ; 1059-910X
ISSN (online)	1097-0029
ISSN	1059-910X
DOI	10.1002/jemt.20564
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: N-linked glycosylation is critical for the plasma membrane localization of nephrin.

Yan, Kunimasa / Khoshnoodi, Jamshid / Ruotsalainen, Vesa / Tryggvason, Karl

Journal of the American Society of Nephrology : JASN

2002 Volume 13, Issue 5, Page(s) 1385–1389

Abstract: The expression pattern, subcellular localization, and the role of glycosylation of the human nephrin was examined in transfected cells. Stable cell lines, constitutively expressing a full-length human nephrin cDNA construct, were generated from ... ...

Abstract	The expression pattern, subcellular localization, and the role of glycosylation of the human nephrin was examined in transfected cells. Stable cell lines, constitutively expressing a full-length human nephrin cDNA construct, were generated from transfected immortalized mouse podocytes (IMP) and a human embryonic kidney cell line (HEK-293). Immunofluorescence confocal microscopy of transfected cells showed plasma membrane localization of the recombinant nephrin. Immunoblotting showed that the recombinant nephrin expressed in transfected cell lines migrated as a double band with a molecular weight of 185 kD. When cells were treated with the N-glycosylation inhibitor, tunicamycin, the molecular weight of nephrin was decreased to a single immunoband of 150 kD, indicating that the shift in the electrophoretic migration of nephrin is due to N-linked carbohydrate moieties. It was further shown that this glycosylation process is highly sensitive to inhibition by tunicamycin, which is a naturally occurring antibiotic, leading to retention of nonglycosylated nephrin molecules in the endoplasmic reticulum. It was concluded that N-glycosylation of nephrin is crucial for its proper folding and thereby plasma membrane localization; therefore, inhibition of this process might be an important factor in the onset of pathogenesis of some acquired glomerular diseases.
MeSH term(s)	Animals ; Cell Line ; Cell Membrane/metabolism ; Cloning, Molecular ; Glycosylation ; Humans ; Immunoblotting ; Kidney/cytology ; Membrane Proteins ; Mice ; Microscopy, Fluorescence ; Proteins/metabolism ; Transfection ; Tunicamycin/pharmacology
Chemical Substances	Membrane Proteins ; Proteins ; nephrin ; Tunicamycin (11089-65-9)
Language	English
Publishing date	2002-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1097/01.asn.0000013297.11876.5b
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 3344: Show issues

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Article: Molecular Recognition in the Assembly of Collagens: Terminal Noncollagenous Domains Are Key Recognition Modules in the Formation of Triple Helical Protomers

Khoshnoodi, Jamshid / Cartailler, Jean-Philippe / Alvares, Keith / Veis, Arthur / Hudson, Billy G

Journal of biological chemistry. 2006 Dec. 15, v. 281, no. 50

2006

Abstract: The α-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, ...

Abstract	The α-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds, and registers cognate α-chains for assembly of triple helical protomers that subsequently oligomerize into specific suprastructures. In this article, we review recent findings on the mechanism of chain selection and infer that terminal noncollagenous domains function as recognition modules in trimerization and are therefore key determinants of specificity in the assembly of suprastructures. This mechanism is also illustrated with computer-generated animations.
Language	English
Dates of publication	2006-1215
Size	p. 38117-38121.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Database	NAL-Catalogue (AGRICOLA)

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Article: Monoclonal antibodies to human nephrin.

Ruotsalainen, Vesa / Reponen, Paula / Khoshnoodi, Jamshid / Kilpeläinen, Pekka / Tryggvason, Karl

Hybridoma and hybridomics

2004 Volume 23, Issue 1, Page(s) 55–63

Abstract: Nephrin is a 180-200-kDa transmembrane protein of the immunoglobulin superfamily. In the kidney, nephrin localizes to the slit diaphragm (SD) between interdigitating podocyte foot processes and mutations in the nephrin gene cause congenital nephrotic ... ...

Abstract	Nephrin is a 180-200-kDa transmembrane protein of the immunoglobulin superfamily. In the kidney, nephrin localizes to the slit diaphragm (SD) between interdigitating podocyte foot processes and mutations in the nephrin gene cause congenital nephrotic syndrome. In addition to this rare genetic disorder, recent reports indicate that nephrin is more generally involved in the pathogenesis of glomerular disease. In this report, we describe production and characterization of mouse monoclonal antibodies to human nephrin, and discuss their applications. Recombinant human nephrin variants were produced in both prokaryotic and eukaryotic expression systems and purified proteins were used in an immunization protocol. A total of 16 antibodies were characterized for their reactivity with the nephrin by using ELISA, Western blots, immunoprecipitation and immunostaining of frozen and formaldehyde-fixed paraffin embedded tissue sections. The antibody epitopes were mapped using a variety of recombinant human nephrin variants. The detailed screening and characterization proved to be essential in order to find the most suitable antibody for each application. These antibodies will find wide use in studies of human nephrin and its involvement in kidney disease.
MeSH term(s)	Antibodies, Monoclonal/immunology ; Blotting, Western ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Humans ; Membrane Proteins ; Precipitin Tests ; Proteins/immunology
Chemical Substances	Antibodies, Monoclonal ; Membrane Proteins ; Proteins ; nephrin
Language	English
Publishing date	2004-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2079028-4
ISSN	1536-8599
ISSN	1536-8599
DOI	10.1089/153685904322772033
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Unraveling the Molecular Make-Up of the Glomerular Podocyte Slit Diaphragm

Khoshnoodi, Jamshid / Tryggvason, Karl

Nephron Experimental Nephrology

2001 Volume 9, Issue 6, Page(s) 355–359

Abstract: Recent discoveries in podocyte proteins involved in the renal filtration barrier have shed new light on the ultrastructure of the kidney filter and pathogenesis of proteinuria. The identification of nephrin, a component of the slit diaphragm, and the ... ...

Institution	Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm,Sweden
Abstract	Recent discoveries in podocyte proteins involved in the renal filtration barrier have shed new light on the ultrastructure of the kidney filter and pathogenesis of proteinuria. The identification of nephrin, a component of the slit diaphragm, and the intracellular slit diaphragm associated proteins CD2AP and podocin has demonstrated the existence of proteins that directly contribute to a functional kidney filter. Mutations in the genes for these three proteins result in proteinuria and nephrotic syndrome, and these proteins are also likely to be involved more generally in the pathomechanisms of proteinuria. This new knowledge has been promoted particularly through the powerful methods of molecular genetics and molecular biology. In this minireview, we present the recent progress in research of the podocyte slit diaphragm.
Keywords	Congenital nephrotic syndrome ; Podocyte ; Slit diaphragm ; Nephrin ; ZO-1 ; P-cadherin ; CD2AP
Language	English
Publishing date	2001-11-07
Publisher	S. Karger AG
Publishing place	Basel, Switzerland
Document type	Article
Note	Minireview
ZDB-ID	207121-6
ISSN	1660-2129 ; 1423-0186 ; 2235-3186 ; 1660-8151 ; 0028-2766
ISSN (online)	1660-2129 ; 1423-0186 ; 2235-3186
ISSN	1660-8151 ; 0028-2766
DOI	10.1159/000052632
Database	Karger publisher's database

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Article: Identification of N-linked glycosylation sites in human nephrin using mass spectrometry.

Khoshnoodi, Jamshid / Hill, Salisha / Tryggvason, Karl / Hudson, Billy / Friedman, David B

Journal of mass spectrometry : JMS

2007 Volume 42, Issue 3, Page(s) 370–379

Abstract: Nephrin is a type-1 transmembrane glycoprotein and the first identified principal component of the glomerular filtration barrier. Ten potential asparagine (N)-linked glycosylation sites have been predicted within the ectodomain of nephrin. However, it is ...

Abstract	Nephrin is a type-1 transmembrane glycoprotein and the first identified principal component of the glomerular filtration barrier. Ten potential asparagine (N)-linked glycosylation sites have been predicted within the ectodomain of nephrin. However, it is not known which of these potential sites are indeed glycosylated and what type of glycans are involved. In this work, we have identified the terminal sugar residues on the ectodomain of human nephrin and utilized a straightforward and reliable mass spectrometry-based approach to selectively identify which of the ten predicted sites are glycosylated. Purified recombinant nephrin was subjected to peptide-N-glycosidase F (PNGase F) to enzymatically remove all the N-linked glycans. Since PNGase F is an amidase, the asparagine residues from which the glycans have been removed are deaminated to aspartic acid residues, resulting in an increase in the peptide mass with 1 mass unit. Following trypsin digestion, deglycosylated tryptic peptides were selectively identified by MALDI-TOF MS and their sequence was confirmed by tandem TOF/TOF. The 1 Da increase in peptide mass for each asparagine-to-aspartic acid conversion, along with preferential cleavage of the amide bond carboxyl-terminal to aspartic acid residues in peptides where the charge is immobilized by an arginine residue, was used as a diagnostic signature to identify the glycosylated peptides. Thus, nine of ten potential glycosylation sites in nephrin were experimentally proven to be modified by N-linked glycosylation.
MeSH term(s)	Binding Sites ; Carbohydrates/chemistry ; Glycosylation ; Humans ; Membrane Proteins/chemistry ; Peptide Mapping/methods ; Protein Binding ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods
Chemical Substances	Carbohydrates ; Membrane Proteins ; nephrin
Language	English
Publishing date	2007-03
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1221763-3
ISSN	1096-9888 ; 1076-5174
ISSN (online)	1096-9888
ISSN	1076-5174
DOI	10.1002/jms.1170
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Zs.A 4254: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 220: Show issues

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Article: Molecular recognition in the assembly of collagens: terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers.

Khoshnoodi, Jamshid / Cartailler, Jean-Philippe / Alvares, Keith / Veis, Arthur / Hudson, Billy G

The Journal of biological chemistry

2006 Volume 281, Issue 50, Page(s) 38117–38121

Abstract: The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen ... ...

Abstract	The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds, and registers cognate alpha-chains for assembly of triple helical protomers that subsequently oligomerize into specific suprastructures. In this article, we review recent findings on the mechanism of chain selection and infer that terminal noncollagenous domains function as recognition modules in trimerization and are therefore key determinants of specificity in the assembly of suprastructures. This mechanism is also illustrated with computer-generated animations.
MeSH term(s)	Biopolymers ; Collagen/chemistry ; Collagen/metabolism ; Protein Conformation
Chemical Substances	Biopolymers ; Collagen (9007-34-5)
Language	English
Publishing date	2006-11-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.R600025200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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