P. Steinert

J. V. Van Beeumen, B. Devreese, P. Steinert, 2004, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Postsynthetic modifications of mammalian epidermal alpha-keratin.

W. Idler, P. Steinert, 1979, Biochemistry.

Transglutaminase 1 Mutations in Lamellar Ichthyosis

G. Melino, P. Steinert, E. Candi, 1998, The Journal of Biological Chemistry.

Assembly of the epidermal cornified cell envelope.

P. Steinert, L. Marekov, A. Kalinin, 2001, Journal of cell science.

Structure of the human desmoplakins. Implications for function in the desmosomal plaque.

D. Parry, P. Steinert, B. Angst, 1990, The Journal of biological chemistry.

The cornified envelope: a model of cell death in the skin.

G. Melino, P. Steinert, E. Candi, 1998, Results and problems in cell differentiation.

Two Novel Mutations in the Keratin 1 Gene in Epidermolytic

P. Steinert, K. Ahn, Jun-Mo Yang, 2010 .

Two novel mutations in the keratin 1 gene in epidermolytic hyperkeratosis.

P. Steinert, K. Ahn, Jun-Mo Yang, 2002, The Journal of investigative dermatology.

An alanine to proline mutation in the 1A rod domain of the keratin 10 chain in epidermolytic hyperkeratosis.

K. Yoneda, P. Steinert, Jun-Mo Yang, 1997, The Journal of investigative dermatology.

A novel H1 mutation in the keratin 1 chain in epidermolytic hyperkeratosis.

P. Steinert, K. Park, K. Moon, 1996, The Journal of investigative dermatology.

Characterization of an immortalized cell line from a patient with epidermolytic hyperkeratosis.

C. Woodworth, P. Steinert, C. C. Chipev, 1996, The Journal of investigative dermatology.

Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis.

S. Bale, P. Steinert, Jun-Mo Yang, 1994, American journal of human genetics.

Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis.

S. Bale, P. Steinert, Jun-Mo Yang, 1994, The Journal of investigative dermatology.

Intermediate filament structure

P. Steinert, D. A. Perry, 1992, Current Biology.

Nuclear lamin proteins common structures for paracrystalline filamentous and lattice forms

D. Parry, P. Steinert, J. Conway, 1987 .

Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly.

D. Parry, P. Steinert, R. Fraser, 1993, Journal of molecular biology.

Concurrence between the molecular overlap regions in keratin intermediate filaments and the locations of keratin mutations in genodermatoses.

S. Bale, P. Steinert, J. Compton, 1993, Biochemical and biophysical research communications.

Residues in the 1A Rod Domain Segment and the Linker L2 Are Required for Stabilizing the A11 Molecular Alignment Mode in Keratin Intermediate Filaments*

D. Parry, P. Steinert, M. Morasso, 2001, The Journal of Biological Chemistry.

Organization, structure, and polymorphisms of the human profilaggrin gene.

O. Mcbride, W. Idler, P. Steinert, 1991, Biochemistry.

Intermediate Filaments An Overview

P. Steinert, R. Goldman, Rv Zackaroff, 1990 .

Crystallization and preliminary X-ray analysis of human transglutaminase 3 from zymogen to active form.

W. Idler, P. Steinert, Z. Nemes, 2001, Journal of structural biology.

The characterisation of protein-bound citrulline.

P. Steinert, G. Rogers, H. W. Harding, 1969, Biochimica et biophysica acta.

A role for the 1A and L1 rod domain segments in head domain organization and function of intermediate filaments: structural analysis of trichocyte keratin.

D. Parry, P. Steinert, L. Marekov, 2002, Journal of structural biology.

A glutamate to lysine mutation at the end of 2B rod domain of keratin 2e gene in ichthyosis bullosa of Siemens.

K. Yoneda, P. Steinert, K. Park, 1998, Acta dermato-venereologica.

A novel threonine --> proline mutation at the end of 2B rod domain in the keratin 2e chain in ichthyosis bullosa of Siemens.

P. Steinert, S. Lee, W. Kim, 1997, The Journal of investigative dermatology.

Structure and Assembly of Intermediate Filaments: Multi- Faceted, Myosin-like (But Non-Motile) Cytoskeletal Polymers

B. Trus, A. Steven, P. Steinert, 1989 .

Cytoskeleton: Splitting hairs and other intermediate filaments

A. Steven, P. Steinert, 1985, Nature.

Epidermal keratin filaments assembled in vitro have masses-per-unit- length that scale according to average subunit mass: structural basis for homologous packing of subunits in intermediate filaments

B. Trus, J. Hainfeld, A. Steven, 1983, The Journal of cell biology.

Molecular Parameters of Type IV α-Internexin and Type IV-Type III α-Internexin-Vimentin Copolymer Intermediate Filaments*

D. Parry, P. Steinert, L. Marekov, 1999, The Journal of Biological Chemistry.

The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure.

D. Parry, P. Steinert, 1993, The Journal of biological chemistry.

Keratin 9 gene mutations in five Korean families with epidermolytic palmoplantar keratoderma

P. Steinert, K. Ahn, Jun-Mo Yang, 2003, Experimental dermatology.

The dynamic phosphorylation of the human intermediate filament keratin 1 chain.

P. Steinert, P M Steinert, 1988, The Journal of biological chemistry.

Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits.

A. Steven, D. Parry, W. Idler, 1985, The Journal of biological chemistry.

The polypeptide composition of bovine epidermal alpha-keratin.

W. Idler, P. Steinert, 1975, The Biochemical journal.

The complete sequence of the human intermediate filament chain keratin 10. Subdomainal divisions and model for folding of end domain sequences.

A. Steven, W. Idler, P. Steinert, 1988, The Journal of biological chemistry.

Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins.

D. Parry, P. Steinert, J. Conway, 1986, The Biochemical journal.

In vitro assembly of homopolymer and copolymer filaments from intermediate filament subunits of muscle and fibroblastic cells.

M. Gottesman, W. Idler, P. Steinert, 1981, Proceedings of the National Academy of Sciences of the United States of America.

Ten-nanometer filaments of hamster BHK-21 cells and epidermal keratin filaments have similar structures.

P. Steinert, R. Goldman, S. Zimmerman, 1978, Proceedings of the National Academy of Sciences of the United States of America.

The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer.

P. Steinert, 1990, The Journal of biological chemistry.

Structural-mechanical integration of keratin intermediate filaments with cell peripheral structures in the cornified epidermal keratinocyte.

P. Steinert, 1998, The Biological bulletin.

Structural changes in trichocyte keratin intermediate filaments during keratinization.

D. Parry, P. Steinert, R. Fraser, 2003, Journal of structural biology.

The Proteins Elafin, Filaggrin, Keratin Intermediate Filaments, Loricrin, and Small Proline-rich Proteins 1 and 2 Are Isodipeptide Cross-linked Components of the Human Epidermal Cornified Cell Envelope (*)

P. Steinert, L. Marekov, 1995, The Journal of Biological Chemistry.

Small proline‐rich protein 1 is the major component of the cell envelope of normal human oral keratinocytes

Soo-Youl Kim, P. Steinert, J. Brahim, 2000, FEBS letters.

Assays for transglutaminases in cell death.

G. Melino, P. Steinert, E. Candi, 2000, Methods in enzymology.

Transglutaminase Cross-linking Properties of the Small Proline-rich 1 Family of Cornified Cell Envelope Proteins

W. Idler, P. Steinert, E. Candi, 1999, The Journal of Biological Chemistry.

A novel in situ method for the detection of deficient transglutaminase activity in the skin

M. Raghunath, V. Wiebe, H. Hennies, 1998, Archives of Dermatological Research.

Structural and Transglutaminase Substrate Properties of the Small Proline-rich 2 Family of Cornified Cell Envelope Proteins*

W. Idler, P. Steinert, E. Candi, 1998, The Journal of Biological Chemistry.

The Transglutaminase 1 Enzyme Is Variably Acylated by Myristate and Palmitate during Differentiation in Epidermal Keratinocytes*

Soo-Youl Kim, P. Steinert, S. Chung, 1996, The Journal of Biological Chemistry.

The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity.

P. Steinert, S. Kim, S. I. Chung, 1994, The Journal of biological chemistry.

Characterization of a cDNA clone encoding human filaggrin and localization of the gene to chromosome region 1q21.

C. Croce, K. Huebner, D. Parry, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Retinoic acid induces transglutaminase activity but inhibits cornification of cultured epidermal cells.

P. Steinert, S. Yuspa, T. Ben, 1982, The Journal of biological chemistry.

Activator Protein 1 Activity Is Involved in the Regulation of the Cell Type-specific Expression from the Proximal Promoter of the Human Profilaggrin Gene*

P. Steinert, S. Jang, N. Markova, 1996, The Journal of Biological Chemistry.

Structure and organization of the human transglutaminase 1 gene.

O. Mcbride, M. Wang, W. Idler, 1992, The Journal of biological chemistry.

The structure of the gene for mouse filaggrin and a comparison of the repeating units.

P. Steinert, J. Rothnagel, 1990, The Journal of biological chemistry.

A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin.

D. Parry, P. Steinert, R. Goldman, 1999, The Journal of biological chemistry.

Profilaggrin is a major epidermal calcium-binding protein

W. Idler, P. Steinert, L. Marekov, 1993, Molecular and cellular biology.

Cytoplasmic localization of the trypanothione peroxidase system in Crithidia fasciculata.

P. Steinert, L. Flohé, K. Dittmar, 1999, Free radical biology & medicine.

Isolation and characterization of keratin-like proteins from cultured cells with fibroblastic morphology

P. Steinert, R. Goldman, A. Goldman, 1984, The Journal of cell biology.

Bmp-2 Downstream Targets in Mesenchymal Development Identiﬁed by Subtractive Cloning From Recombinant Mesenchymal Progenitors (C3H10T 1 ⁄ 2 ) the

A. Hoffmann, P. Steinert, L. Flohé, 1998 .

Structure of the human desmoplakins. Implications for function in the desmosomal plaque.

D. Parry, P. Steinert, B. Angst, 1990, The Journal of biological chemistry.

A model for the hierarchical structure of the human epidermal cornified cell envelope.

P. Steinert, 1995, Cell death and differentiation.

Structural and Functional Implications of Amino Acid Sequences of Keratin Intermediate Filament Subunits

A. Steven, D. Parry, W. Idler, 1985, Annals of the New York Academy of Sciences.

The Use of cDNA Clones and Monospecific Antibodies as Probes to Monitor Keratin Gene Expression

P. Steinert, D. Roop, S. Yuspa, 1985, Annals of the New York Academy of Sciences.

Growth and differentiation of mouse epidermal cells in culture: effects of extracellular calcium.

K. Holbrook, P. Steinert, S. Yuspa, 1981, Current problems in dermatology.

Overexpression of human loricrin in transgenic mice produces a normal phenotype.

K. Yoneda, P. Steinert, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Molecular biology of Loricrin.Recent findings.

P. Steinert, 1994 .

The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse.

P. Steinert, S. -. Park, J. Gorman, 1993, The Journal of biological chemistry.

Cultured human bronchial epithelial cells: blood group antigens, keratin, collagens, and fibronectin

J. Foidart, C. Harris, B. Trump, 1981, In Vitro.

The Fate of Trichohyalin

W. Idler, P. Steinert, E. Candi, 1997, The Journal of Biological Chemistry.

Intermediate filaments: conformity and diversity of expression and structure.

D A Parry, P M Steinert, D. Parry, 1985, Annual review of cell biology.

The molecular biology of intermediate filaments

A. Steven, P. Steinert, D. Roop, 1985, Cell.

Molecular and cellular biology of intermediate filaments.

P M Steinert, P. Steinert, D. Roop, 1988, Annual review of biochemistry.

Structures of Tryparedoxins Revealing Interaction with Trypanothione

P. Steinert, L. Flohé, H. Hecht, 2001, Biological chemistry.

Testosterone mediates expression of the selenoprotein PHGPx by induction of spermatogenesis and not by direct transcriptional gene activation

F. Ursini, P. Steinert, R. Brigelius-Flohé, 1998, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Sequence Analysis of the Tryparedoxin Peroxidase Gene fromCrithidia fasciculata and Its Functional Expression in Escherichia coli *

P. Steinert, L. Flohé, E. Nogoceke, 1998, The Journal of Biological Chemistry.

Role of Selenium in the Enzymatic Reduction of Hydroperoxides

P. Steinert, L. Flohé, K. Aumann, 1998 .

cDNA and deduced polypeptide sequence of a mouse selenoprotein P

P. Steinert, L. Flohé, G. Gross, 1997, BioFactors.

Estimation of protein sulfhydryl groups with 5,5'-(35S) dithio-bis(2-nitrobenzoate).

H. Munro, P. Steinert, B. S. Baliga, 1974, Analytical biochemistry.

Bricks and mortar of the epidermal barrier

P. Steinert, Z. Nemes, 1999, Experimental & Molecular Medicine.

Three‐dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation

P. Steinert, Z. Nemes, B. Ahvazi, 2002, The EMBO journal.

Intermediate filaments

R. D. Goldman, J. C. Jones, P. Steinert, 1984, The Journal of cell biology.

Evidence for novel functions of the keratin tail emerging from a mutation causing ichthyosis hystrix.

G. Richard, E. Sprecher, O. Becker, 2001, The Journal of investigative dermatology.

Mutations in the 1A rod domain segment of the keratin 9 gene in epidermolytic palmoplantar keratoderma.

P. Steinert, K. Park, S. Lee, 1998, Acta dermato-venereologica.

Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments

B. Trus, A. Steven, P. Steinert, 1983, Nature.

Microtubule disruption in keratinocytes induces cell-cell adhesion through activation of endogenous E-cadherin.

P. Steinert, S. Kee, 2001, Molecular biology of the cell.

A novel function for transglutaminase 1: attachment of long-chain omega-hydroxyceramides to involucrin by ester bond formation.

P M Steinert, P. Steinert, Z. Nemes, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Organization of coiled-coil molecules in native mouse keratin 1/keratin 10 intermediate filaments: evidence for alternating rows of antiparallel in-register and antiparallel staggered molecules.

P. Steinert, 1991, Journal of structural biology.

Biochemical Evidence That Small Proline-rich Proteins and Trichohyalin Function in Epithelia by Modulation of the Biomechanical Properties of Their Cornified Cell Envelopes*

P. Steinert, T. Kartasova, L. Marekov, 1998, The Journal of Biological Chemistry.

The ultrastructure of sugar beet during sugar manufacture.

P. Steinert, K. Buchholz, C. Buttersack, 1990 .

Anisotropic swelling of cell walls of sugar beet tissue: Influence of ion‐exchange and sucrose

P. Steinert, K. Buchholz, C. Buttersack, 1995 .

O-phosphoserine content of intermediate filament subunits.

W. Idler, P. Steinert, M. Wantz, 1982, Biochemistry.

The extraction and characterization of bovine epidermal alpha-keratin.

P. Steinert, 1975, The Biochemical journal.

Manganese-stimulated phosphatidylinositol 4-kinase from Dunaliella parva: purification and characterization

P. Steinert, K. Wagner, J. Wissing, 1994 .

Expression of murine epidermal differentiation markers is tightly regulated by restricted extracellular calcium concentrations in vitro

P M Steinert, P. Steinert, D. Roop, 1989, The Journal of cell biology.

In Vitro Assembly and Structure of Trichocyte Keratin Intermediate Filaments

D. Parry, W. Idler, P. Steinert, 2000, The Journal of cell biology.

Self-healing collodion baby: a dynamic phenotype explained by a particular transglutaminase-1 mutation.

M. Raghunath, H. Hennies, P. Steinert, 2003, The Journal of investigative dermatology.

Density-dependent modulation of synthesis of keratins 1 and 10 in the human keratinocyte line HACAT and in ras-transfected tumorigenic clones.

N. Fusenig, P. Steinert, D. Roop, 1989, Differentiation; research in biological diversity.

A High Molecular Weight Intermediate Filament-associated Protein in BHK-21 Cells Is Nestin, a Type VI Intermediate Filament Protein

D. Parry, P. Steinert, R. Goldman, 1999, The Journal of Biological Chemistry.

Available sulphydryl groups of mammalian ribosomes in different functional states.

H. Munro, P. Steinert, B. S. Baliga, 1974, Journal of molecular biology.

Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops.

O. Mcbride, P. Steinert, D. Mischke, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Direct Evidence That Involucrin Is a Major Early Isopeptide Cross-linked Component of the Keratinocyte Cornified Cell Envelope*

P M Steinert, P. Steinert, L. Marekov, 1997, The Journal of Biological Chemistry.

Assignment of the human transglutaminase 2 (TGM2) and transglutaminase 3 (TGM3) genes to chromosome 20q11.2.

O. Mcbride, M. Wang, P. Steinert, 1994, Genomics.

The function of intermediate filaments in cell shape and cytoskeletal integrity

P. Steinert, R. Goldman, Y. Chou, 1996, The Journal of cell biology.

The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis.

A. Steven, P. Steinert, J. W. Mack, 1993, Journal of molecular biology.

Human trichohyalin gene is clustered with the genes for other epidermal structural proteins and calcium-binding proteins at chromosomal locus 1q21.

O. Mcbride, M. Wang, P. Steinert, 1993, The Journal of investigative dermatology.

Loricrin Expression in Cultured Human Keratinocytes Is Controlled by a Complex Interplay between Transcription Factors of the Sp1, CREB, AP1, and AP2 Families*

P. Steinert, S. Jang, 2002, The Journal of Biological Chemistry.

Mouse Sprr2 genes: a clustered family of genes showing differential expression in epithelial tissues.

P. Steinert, T. Kuroki, N. Darwiche, 1999, Genomics.

Effect of AP1 transcription factors on the regulation of transcription in normal human epidermal keratinocytes.

P. Steinert, A. Rossi, S. Jang, 1998, The Journal of investigative dermatology.

Differential expression and cell envelope incorporation of small proline-rich protein 1 in different cornified epithelia.

A. Steven, P. Steinert, M. Jarnik, 1996, Journal of cell science.

The Proximal Promoter of the Human Transglutaminase 3 Gene

P. Steinert, S. Jang, Jun-Mo Yang, 1996, The Journal of Biological Chemistry.

Sequence and expression patterns of mouse SPR1: Correlation of expression with epithelial function.

P. Steinert, N. Huh, T. Kuroki, 1996, The Journal of investigative dermatology.

Biochemical, Structural, and Transglutaminase Substrate Properties Of Human Loricrin, the Major Epidermal Cornified Cell Envelope Protein (*)

G. Melino, P. Steinert, E. Candi, 1995, The Journal of Biological Chemistry.

Expression of transglutaminase 1 in human epidermis.

K. Yoneda, P. Steinert, S. Kim, 1995, The Journal of investigative dermatology.

Protein composition of cornified cell envelopes of epidermal keratinocytes.

A. Steven, P. Steinert, 1994, Journal of cell science.

Trichohyalin: a structural protein of hair, tongue, nail, and epidermis.

P. Steinert, E. O'Keefe, S. C. Lee, 1993, The Journal of investigative dermatology.

Profilaggrin Isa MajorEpidermal Calcium-Binding Protein

W. Idler, P. Steinert, S. Gan, 1993 .

The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain.

P. Steinert, D. Mischke, J. Compton, 1992, The Journal of investigative dermatology.

The Cornified Cell Envelope: Loricrin and Transglutaminases

K. Yoneda, O. Mcbride, P. Steinert, 1992, The Journal of dermatology.

Structural Changes of Human Epidermal α-Keratin in Disorders of Keratinization

W. Idler, P. Steinert, G. Peck, 1981 .

Structural changes of human epidermal alpha-keratin in disorders of keratinization.

W. Idler, P. Steinert, G. Peck, 1980, Current problems in dermatology.

Trichohyalin Mechanically Strengthens the Hair Follicle

D. Parry, P. Steinert, L. Marekov, 2003, Journal of Biological Chemistry.

Organization, structure, and polymorphisms of the human profilaggrin gene.

O. Mcbride, W. Idler, P. Steinert, 1990, Biochemistry.

The expression of a novel, epithelium-specific ets transcription factor is restricted to the most differentiated layers in the epidermis.

P. Steinert, C. Coticchia, S. Jang, 1997, Nucleic acids research.

Inactive zymogen and highly active proteolytically processed membrane-bound forms of the transglutaminase 1 enzyme in human epidermal keratinocytes.

P. Steinert, S. Kim, S. Chung, 1996, Biochemical and biophysical research communications.

Characterization of a class of cationic proteins that specifically interact with intermediate filaments.

P. Steinert, D. Teller, J. Lonsdale-Eccles, 1981, Proceedings of the National Academy of Sciences of the United States of America.

Structure, function, and dynamics of keratin intermediate filaments.

P M Steinert, P. Steinert, 1993, The Journal of investigative dermatology.

Synthetic peptides corresponding to keratin subunits elicit highly specific antibodies.

P. Steinert, D. Roop, S. Yuspa, 1984, The Journal of biological chemistry.

Identification of a major keratinocyte cell envelope protein, loricrin

A. Steven, D. Hohl, P. Steinert, 1990, Cell.

Characterization of the keratin filament subunits unique to bovine snout epidermis.

W. Idler, P. Steinert, M. Wantz, 1980, The Biochemical journal.

Epidermal Keratin: Filaments and Matrix

P. Steinert, 1983 .

Isolation and characterization of intermediate filaments.

P. Steinert, R. Goldman, M. Aynardi-Whitman, 1982, Methods in cell biology.

Protein biosynthesis in cell-free systems prepared from hair follicel tissue of guinea pigs.

P. Steinert, G. Rogers, 1971, Biochimica et biophysica acta.

Bovine epidermal keratin filament assembly in vitro.

P. Steinert, M. I. Gullino, 1976, Biochemical and biophysical research communications.

Highly Active Soluble Processed Forms of the Transglutaminase 1 Enzyme in Epidermal Keratinocytes (*)

P. Steinert, S. Chung, Soo‐Youl Kim, 1995, The Journal of Biological Chemistry.

In vitro studies on the synthesis of guinea pig hair keratin proteins.

P. Steinert, G. Rogers, 1973, Biochimica et biophysica acta.

The synthesis of hair keratin proteins in vitro.

P. Steinert, G. Rogers, 1971, Biochimica et biophysica acta.

Human upper epidermal cytoplasmic antibodies are directed against keratin intermediate filament proteins.

P. Steinert, T. Lawley, H. Hintner, 1983, The Journal of clinical investigation.

Structural features of epidermal keratin filaments reassembled in vitro.

A. Steven, P. Steinert, D. Roop, 1983, The Journal of investigative dermatology.

Structure of the three-chain unit of the bovine epidermal keratin filament.

P. Steinert, P M Steinert, 1978, Journal of molecular biology.

Structural features of keratin intermediate filaments.

A. North, D. Parry, P. Steinert, 1994, The Journal of investigative dermatology.

Structure of fibroblastic intermediate filaments: analysis of scanning transmission electron microscopy.

J. Hainfeld, A. Steven, J. Wall, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Hair keratinization in health and disease.

P. Steinert, L. N. Jones, 1996, Dermatologic clinics.

A procedure for the culture of hair follicles as functionally intact organoids.

P. Steinert, D. Roop, S. Yuspa, 1988, Clinics in dermatology.

Intermediate filament dynamics

R. Liem, P. Steinert, 1990, Cell.

Molecular and biophysical characterization of assembly-starter units of human vimentin.

Ueli Aebi, Jörg Langowski, J. Langowski, 2004, Journal of molecular biology.

Modeling effects of mutations in coiled‐coil structures: Case study using epidermolysis bullosa simplex mutations in segment 1a of k5/k14 intermediate filaments

D. Parry, P. Steinert, T. A. Smith, 2004, Proteins.

Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments.

D. Parry, P. Steinert, S. Jang, 2000, Molecular biology of the cell.

Sjögren–Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene

P. Steinert, V. Laurenzi, W. Rizzo, 1996, Nature Genetics.

The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly.

A. Lustig, U. Aebi, P. Burkhard, 1999, Journal of molecular biology.

A highly conserved lysine residue on the head domain of type II keratins is essential for the attachment of keratin intermediate filaments to the cornified cell envelope through isopeptide crosslinking by transglutaminases.

P. Elias, P. Steinert, E. Candi, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The Structure and Evolution of Intermediate Filament Genes

P. Steinert, D. Roop, 1986 .

Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism

D. Parry, P. Steinert, Peter M. Steinert, 1999, Quarterly Reviews of Biophysics.

Genetic skin diseases caused by mutations in keratin intermediate filaments.

S. Bale, P. Steinert, 1993, Trends in genetics : TIG.

Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins.

A. Steven, P. Steinert, S. Haynes, 1991, International journal of biological macromolecules.

The Structure, Complexity, and Evolution of Intermediate Filament Genes

P. Steinert, D. Roop, 1990 .

Transglutaminases in disease

P. Steinert, T. Jeitner, Soo-Youl Kim, 2002, Neurochemistry International.

Radial distributions of density within macromolecular complexes determined from dark-field electron micrographs.

B. Trus, J. Hainfeld, A. Steven, 1984, Proceedings of the National Academy of Sciences of the United States of America.

What's where in intermediate filaments?

B. Trus, A. Steven, P. Steinert, 1987 .

Conformity and Diversity in the Structures of Intermediate Filaments

B. Trus, J. Hainfeld, A. Steven, 1985, Annals of the New York Academy of Sciences.

Cross‐linking of ubiquitin, HSP27, parkin and α‐synuclein by γ‐glutamyl‐ε‐lysine bonds in Alzheimer's neurofibrillary tangles

B. Devreese, P. Steinert, J. Beeumen, 2004 .

A model for the reaction mechanism of the transglutaminase 3 enzyme

P. Steinert, B. Ahvazi, 2003, Experimental & Molecular Medicine.

IFN-γ Induces Transglutaminase 2 Expression in Rat Small Intestinal Cells

P. Steinert, Soo‐Youl Kim, Eun-joo Jeong, 2002 .

The distribution of mass in heteropolymer intermediate filaments assembled in vitro. Stem analysis of vimentin/desmin and bovine epidermal keratin.

B. Trus, J. Hainfeld, A. Steven, 1983, The Journal of biological chemistry.

Transglutaminase crosslinking and structural studies of the human small proline rich 3 protein

G. Melino, P. Steinert, E. Candi, 1999, Cell Death and Differentiation.

Permutation of the Active Site Motif of Tryparedoxin 2

P. Steinert, L. Flohé, H. Hecht, 2000, Biological chemistry.

Sequence, heterologous expression and functional characterization of tryparedoxin1 from Crithidia fasciculata.

P. Steinert, L. Flohé, H. Hecht, 2001, European Journal of Biochemistry.

Linkage of epidermolytic hyperkeratosis to the type II keratin gene cluster on chromosome 12q

C. Amos, S. Bale, O. Mcbride, 1992, Nature Genetics.

Co-assembly of envoplakin and periplakin into oligomers and Ca(2+)-dependent vesicle binding: implications for cornified cell envelope formation in stratified squamous epithelia.

A. Steven, W. Idler, P. Steinert, 2004, The Journal of biological chemistry.

Protein Unfolding by Peptidylarginine Deiminase

G. Melino, P. Steinert, G. Mei, 1996, The Journal of Biological Chemistry.

A human epidermal differentiation-specific keratin gene is regulated by calcium but not negative modulators of differentiation in transgenic mouse keratinocytes.

C. Huff, P. Steinert, D. Roop, 1991, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research.

Analysis of the Mouse Selenoprotein P Gene

P. Steinert, L. Flohé, D. Bächner, 1998, Biological chemistry.

Characterization of human loricrin. Structure and function of a new class of epidermal cell envelope proteins.

D. Hohl, P. Steinert, D. Roop, 1991, The Journal of biological chemistry.

Solid-state NMR studies of the dynamics and structure of mouse keratin intermediate filaments.

D. Torchia, P. Steinert, J. W. Mack, 1988, Biochemistry.

Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments.

D A Parry, P M Steinert, D. Parry, 1993, The Journal of biological chemistry.

Two-hybrid Analysis Reveals Fundamental Differences in Direct Interactions between Desmoplakin and Cell Type-specific Intermediate Filaments*

P. Steinert, J. Meng, W. Ip, 1997, The Journal of Biological Chemistry.

Keratins: Dynamic, flexible structural proteins of epithelial cells

P. Steinert, 2001 .

The gene for mouse epidermal filaggrin precursor. Its partial characterization, expression, and sequence of a repeating filaggrin unit.

P M Steinert, W. Idler, P. Steinert, 1987, The Journal of biological chemistry.

Structure and organization of the human transglutaminase 3 gene: evolutionary relationship to the transglutaminase family.

P. Steinert, Jun-Mo Yang, J. Lee, 1994, The Journal of investigative dermatology.

Assembly of stratum corneum basic protein and keratin filaments in macrofibrils

K. Holbrook, P. Steinert, B. Dale, 1978, Nature.

Structural features of the alpha-type filaments of the inner root sheath cells of the guinea pig hair follicle.

P. Steinert, 1978, Biochemistry.

The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones.

W. Idler, P. Steinert, J. Han, 1991, The Journal of biological chemistry.

Charge derivatization by 4-sulfophenyl isothiocyanate enhances peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

P. Steinert, L. Marekov, 2003, Journal of mass spectrometry : JMS.

Sporadic Inclusion Body Myositis Correlates with Increased Expression and Cross-linking by Transglutaminases 1 and 2*

P M Steinert, P. Steinert, I. Sunwoo, 2000, The Journal of Biological Chemistry.

IFN-gamma induces transglutaminase 2 expression in rat small intestinal cells.

P. Steinert, Soo‐Youl Kim, Eun-joo Jeong, 2002, Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research.

Novel mutations of the transglutaminase 1 gene in lamellar ichthyosis.

C. H. Lee, G. Melino, K. Yoneda, 2001, The Journal of investigative dermatology.

Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium*

U. Baxa, W. Idler, P. Steinert, 2004, Journal of Biological Chemistry.

Intermediate filaments in health and disease

P. Steinert, 1996, Experimental & Molecular Medicine.

Sequence, Heterologous Expression and Functional Characterization of a Novel Tryparedoxin from Crithidia fasciculata

Mahavir Singh, P. Steinert, L. Flohé, 1998, Biological chemistry.

Organization of a type I keratin gene. Evidence for evolution of intermediate filaments from a common ancestral gene.

M. Schafer, P. Steinert, D. Roop, 1985, The Journal of biological chemistry.

The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 Da: analysis of sequence differences between type I and type II keratins.

B. Trus, A. Steven, D. Parry, 1984, Proceedings of the National Academy of Sciences of the United States of America.